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2.3.1.241

Relevance: 100%

Accepted name:

Kdo₂-lipid IV_A acyltransferase

Reaction:

a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IV_A] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IV_A] + an [acyl-carrier protein]

For diagram of Kdo-Kdo-Lipid IV_A metabolism, click here

Glossary:

Other name(s):

LpxL; htrB (gene name); dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A O-dodecanoyltransferase; lauroyl-[acyl-carrier protein]:Kdo₂-lipid IV_A O-lauroyltransferase; (Kdo)₂-lipid IV_A lauroyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IV_A lauroyltransferase; dodecanoyl-[acyl-carrier protein]:Kdo₂-lipid IV_A O-dodecanoyltransferase; Kdo₂-lipid IV_A lauroyltransferase

Systematic name:

fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IV_A] O-acyltransferase

Comments:

The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C₁₂) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Clementz, T., Bednarski, J.J. and Raetz, C.R. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271 (1996) 12095–12102. [DOI] [PMID: 8662613]
2.	van der Ley, P., Steeghs, L., Hamstra, H.J., ten Hove, J., Zomer, B. and van Alphen, L. Modification of lipid A biosynthesis in Neisseria meningitidis lpxL mutants: influence on lipopolysaccharide structure, toxicity, and adjuvant activity. Infect. Immun. 69 (2001) 5981–5990. [DOI] [PMID: 11553534]
3.	McLendon, M.K., Schilling, B., Hunt, J.R., Apicella, M.A. and Gibson, B.W. Identification of LpxL, a late acyltransferase of Francisella tularensis. Infect. Immun. 75 (2007) 5518–5531. [DOI] [PMID: 17724076]
4.	Six, D.A., Carty, S.M., Guan, Z. and Raetz, C.R. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47 (2008) 8623–8637. [DOI] [PMID: 18656959]
5.	Fathy Mohamed, Y., Hamad, M., Ortega, X.P. and Valvano, M.A. The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia. Mol. Microbiol. 104 (2017) 144–162. [DOI] [PMID: 28085228]

[EC 2.3.1.241 created 2014, modified 2021]

2.3.1.243

Relevance: 97%

Accepted name:

acyl-Kdo₂-lipid IV_A acyltransferase

Reaction:

a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IV_A] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)₂-[lipid IV_A] + an [acyl-carrier protein]

For diagram of Kdo-Kdo-Lipid IV_A metabolism, click here

Glossary:

Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
a lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IV_A] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose
an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)₂-[lipid IV_A] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-(acyloxy)acyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s):

lpxM (gene name); MsbB acyltransferase; myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IV_A O-myristoyltransferase; tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo₂-lipid IV_A O-tetradecanoyltransferase; lauroyl-Kdo₂-lipid IV_A myristoyltransferase

Systematic name:

fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IV_A] O-acyltransferase

Comments:

The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C₁₄) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Clementz, T., Zhou, Z. and Raetz, C.R. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB. J. Biol. Chem. 272 (1997) 10353–10360. [DOI] [PMID: 9099672]
2.	Dovala, D., Rath, C.M., Hu, Q., Sawyer, W.S., Shia, S., Elling, R.A., Knapp, M.S. and Metzger, L.E., 4th. Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism. Proc. Natl. Acad. Sci. USA 113 (2016) E6064–E6071. [DOI] [PMID: 27681620]

[EC 2.3.1.243 created 2014, modified 2021]

2.7.1.235

Relevance: 93.2%

Accepted name:

lipopolysaccharide core heptose(I) kinase

Reaction:

ATP + an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A]

Glossary:

Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It usually consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups.
Hep = L-glycero-β-D-manno-heptose

Other name(s):

WaaP; RfaP

Systematic name:

ATP:an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] heptose^I 4-O-phosphotransferase

Comments:

The enzyme catalyses the phosphorylation of L-glycero-D-manno-heptose I (the first heptose added to the lipid, Hep I) in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yethon, J.A. and Whitfield, C. Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability. J. Biol. Chem. 276 (2001) 5498–5504. [DOI] [PMID: 11069912]
2.	Zhao, X. and Lam, J.S. WaaP of Pseudomonas aeruginosa is a novel eukaryotic type protein-tyrosine kinase as well as a sugar kinase essential for the biosynthesis of core lipopolysaccharide. J. Biol. Chem. 277 (2002) 4722–4730. [DOI] [PMID: 11741974]
3.	Kreamer, N.NK., Chopra, R., Caughlan, R.E., Fabbro, D., Fang, E., Gee, P., Hunt, I., Li, M., Leon, B.C., Muller, L., Vash, B., Woods, A.L., Stams, T., Dean, C.R. and Uehara, T. Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase. Sci. Rep. 8:14124 (2018). [DOI] [PMID: 30237436]

[EC 2.7.1.235 created 2021]

2.3.1.242

Relevance: 88.6%

Accepted name:

Kdo₂-lipid IV_A palmitoleoyltransferase

Reaction:

a (9Z)-hexadec-9-enoyl-[acyl-carrier protein] + Kdo₂-lipid IV_A = (9Z)-hexadec-9-enoyl-Kdo₂-lipid IV_A + an [acyl-carrier protein]

For diagram of Kdo-Kdo-Lipid IV_A metabolism, click here

Glossary:

Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
lipid IV_A = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Kdo₂-lipid IV_A = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A
(9Z)-hexadec-9-enoyl = palmitoleoyl
(9Z)-hexadec-9-enoyl-Kdo₂-lipid IV_A = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-{(3R)-3-[(9Z)-hexadec-9-enoyl]tetradecanamido}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s):

LpxP; palmitoleoyl-acyl carrier protein-dependent acyltransferase; cold-induced palmitoleoyl transferase; palmitoleoyl-[acyl-carrier protein]:Kdo₂-lipid IV_A O-palmitoleoyltransferase; (Kdo)₂-lipid IV_A palmitoleoyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IV_A palmitoleoyltransferase

Systematic name:

(9Z)-hexadec-9-enoyl-[acyl-carrier protein]:Kdo₂-lipid IV_A O-palmitoleoyltransferase

Comments:

The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Carty, S.M., Sreekumar, K.R. and Raetz, C.R. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274 (1999) 9677–9685. [DOI] [PMID: 10092655]
2.	Vorachek-Warren, M.K., Carty, S.M., Lin, S., Cotter, R.J. and Raetz, C.R. An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C. J. Biol. Chem. 277 (2002) 14186–14193. [DOI] [PMID: 11830594]

[EC 2.3.1.242 created 2014]

2.4.99.25

Relevance: 87.6%

Accepted name:

lipopolysaccharide heptosyltransferase III

Reaction:

ADP-L-glycero-β-D-manno-heptose + an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→7)-α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A]

Glossary:

Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups.
Hep = L-glycero-D-manno-heptose

Other name(s):

waaQ (gene name); rfaQ (gene name)

Systematic name:

ADP-L-glycero-β-D-manno-heptose:an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] heptose^I 7-α-heptosyltransferase

Comments:

The enzyme catalyses a glycosylation step in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Mudapaka, J. and Taylor, E.A. Cloning and characterization of the Escherichia coli heptosyltransferase III: Exploring substrate specificity in lipopolysaccharide core biosynthesis. FEBS Lett. 589 (2015) 1423–1429. [DOI] [PMID: 25957775]

[EC 2.4.99.25 created 2022]

2.4.1.182

Relevance: 87.3%

Accepted name:

lipid-A-disaccharide synthase

Reaction:

a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + a lipid X = UDP + a lipid A disaccharide

For diagram of lipid IV_A biosynthesis, click here

Glossary:

a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine
a lipid A disaccharide = a 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s):

lpxB (gene name); UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis-(3-hydroxytetradecanoyl)-β-D-glucosaminyl-1-phosphate 2,3-bis(3-hydroxytetradecanoyl)-glucosaminyltransferase (incorrect)

Systematic name:

UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine:2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosaminyltransferase

Comments:

Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide 4′-kinase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-81-0

References:

1.	Ray, B.L., Painter, G. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A disaccharides from monosaccharide precursors in extracts of Escherichia coli. J. Biol. Chem. 259 (1984) 4852–4859. [PMID: 6370995]
2.	Crowell, D.N., Reznikoff, W.S. and Raetz, C.R.H. Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase. J. Bacteriol. 169 (1987) 5727–5734. [DOI] [PMID: 2824445]
3.	Metzger, L.E., 4th and Raetz, C.R. Purification and characterization of the lipid A disaccharide synthase (LpxB) from Escherichia coli, a peripheral membrane protein. Biochemistry 48 (2009) 11559–11571. [DOI] [PMID: 19883124]
4.	Bohl, T.E., Shi, K., Lee, J.K. and Aihara, H. Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat. Commun. 9:377 (2018). [DOI] [PMID: 29371662]

[EC 2.4.1.182 created 1990, modified 2021]

2.4.99.24

Relevance: 86.6%

Accepted name:

lipopolysaccharide heptosyltransferase II

Reaction:

ADP-L-glycero-β-D-manno-heptose + an α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A]

Glossary:

Other name(s):

HepII; rfaF (gene name); WaaF; heptosyltransferase II

Systematic name:

ADP-L-glycero-β-D-manno-heptose:an α-L-glycero-D-manno-heptosyl-(1→5)-[α-Kdo-(2→4)]-α -Kdo-(2→6)-[lipid A] 3-α-heptosyltransferase

Comments:

The enzyme catalyses a glycosylation step in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Allen, A.G., Isobe, T. and Maskell, D.J. Identification and cloning of waaF (rfaF) from Bordetella pertussis and use to generate mutants of Bordetella spp. with deep rough lipopolysaccharide. J. Bacteriol. 180 (1998) 35–40. [DOI] [PMID: 9422589]
2.	Bauer, B.A., Lumbley, S.R. and Hansen, E.J. Characterization of a WaaF (RfaF) homolog expressed by Haemophilus ducreyi. Infect. Immun. 67 (1999) 899–907. [DOI] [PMID: 9916106]
3.	Gronow, S., Brabetz, W. and Brade, H. Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli. Eur. J. Biochem. 267 (2000) 6602–6611. [DOI] [PMID: 11054112]
4.	Gronow, S., Oertelt, C., Ervela, E., Zamyatina, A., Kosma, P., Skurnik, M. and Holst, O. Characterization of the physiological substrate for lipopolysaccharide heptosyltransferases I and II. J Endotoxin Res 7 (2001) 263–270. [PMID: 11717579]
5.	Oldfield, N.J., Moran, A.P., Millar, L.A., Prendergast, M.M. and Ketley, J.M. Characterization of the Campylobacter jejuni heptosyltransferase II gene, waaF, provides genetic evidence that extracellular polysaccharide is lipid A core independent. J. Bacteriol. 184 (2002) 2100–2107. [DOI] [PMID: 11914340]

[EC 2.4.99.24 created 2022]

2.4.99.23

Relevance: 84.4%

Accepted name:

lipopolysaccharide heptosyltransferase I

Reaction:

ADP-L-glycero-β-D-manno-heptose + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A]

Glossary:

Other name(s):

HepI; rfaC (gene name); WaaC; heptosyltransferase I (ambiguous)

Systematic name:

ADP-L-glycero-β-D-manno-heptose:an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid A] 5-α-heptosyltransferase

Comments:

The enzyme catalyses a glycosylation step in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of many Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kadrmas, J.L. and Raetz, C.R. Enzymatic synthesis of lipopolysaccharide in Escherichia coli. Purification and properties of heptosyltransferase i. J. Biol. Chem. 273 (1998) 2799–2807. [DOI] [PMID: 9446588]
2.	de Kievit, T.R. and Lam, J.S. Isolation and characterization of two genes, waaC (rfaC) and waaF (rfaF), involved in Pseudomonas aeruginosa serotype O5 inner-core biosynthesis. J. Bacteriol. 179 (1997) 3451–3457. [DOI] [PMID: 9171387]
3.	Klena, J.D., Gray, S.A. and Konkel, M.E. Cloning, sequencing, and characterization of the lipopolysaccharide biosynthetic enzyme heptosyltransferase I gene (waaC) from Campylobacter jejuni and Campylobacter coli. Gene 222 (1998) 177–185. [DOI] [PMID: 9831648]
4.	Gronow, S., Oertelt, C., Ervela, E., Zamyatina, A., Kosma, P., Skurnik, M. and Holst, O. Characterization of the physiological substrate for lipopolysaccharide heptosyltransferases I and II. J Endotoxin Res 7 (2001) 263–270. [PMID: 11717579]
5.	Grizot, S., Salem, M., Vongsouthi, V., Durand, L., Moreau, F., Dohi, H., Vincent, S., Escaich, S. and Ducruix, A. Structure of the Escherichia coli heptosyltransferase WaaC: binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose. J. Mol. Biol. 363 (2006) 383–394. [DOI] [PMID: 16963083]

[EC 2.4.99.23 created 2022]

2.3.1.251

Relevance: 83.1%

Accepted name:

lipid IV_A palmitoyltransferase

Reaction:

(1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
(2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid II_A = 2-acyl-sn-glycero-3-phosphocholine + lipid II_B
(3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IV_A = 2-acyl-sn-glycero-3-phosphocholine + lipid IV_B

For diagram of lipid IV_B biosynthesis, click here

Glossary:

palmitoyl = hexadecanoyl
hexa-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
hepta-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid II_A = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid II_B = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IV_A = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IV_B = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s):

PagP; crcA (gene name)

Systematic name:

1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IV_A palmitoyltransferase

Comments:

Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2→4)-Kdo-(2→6)-lipid IV_A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I. and Raetz, C.R. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19 (2000) 5071–5080. [DOI] [PMID: 11013210]
2.	Cuesta-Seijo, J.A., Neale, C., Khan, M.A., Moktar, J., Tran, C.D., Bishop, R.E., Pomes, R. and Prive, G.G. PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure 18 (2010) 1210–1219. [DOI] [PMID: 20826347]

[EC 2.3.1.251 created 2015]

2.7.8.42

Relevance: 80.1%

Accepted name:

Kdo₂-lipid A phosphoethanolamine 7′′-transferase

Reaction:

(1) diacylphosphatidylethanolamine + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A
(2) diacylphosphatidylethanolamine + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid IV_A = diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid IV_A

Glossary:

lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid IV_A = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s):

eptB (gene name)

Systematic name:

diacylphosphatidylethanolamine:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A 7′′-phosphoethanolaminetransferase

Comments:

The enzyme has been characterized from the bacterium Escherichia coli. It is activated by Ca²⁺ ions and is silenced by the sRNA MgrR.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kanipes, M.I., Lin, S., Cotter, R.J. and Raetz, C.R. Ca²⁺-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli lipopolysaccharide. A novel membrane enzyme dependent upon phosphatidylethanolamine. J. Biol. Chem. 276 (2001) 1156–1163. [DOI] [PMID: 11042192]
2.	Reynolds, C.M., Kalb, S.R., Cotter, R.J. and Raetz, C.R. A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca²⁺ hypersensitivity of an eptB deletion mutant. J. Biol. Chem. 280 (2005) 21202–21211. [DOI] [PMID: 15795227]
3.	Moon, K., Six, D.A., Lee, H.J., Raetz, C.R. and Gottesman, S. Complex transcriptional and post-transcriptional regulation of an enzyme for lipopolysaccharide modification. Mol. Microbiol. 89 (2013) 52–64. [DOI] [PMID: 23659637]

[EC 2.7.8.42 created 2015]

2.7.1.130

Relevance: 79.8%

Accepted name:

tetraacyldisaccharide 4′-kinase

Reaction:

ATP + a lipid A disaccharide = ADP + a lipid IV_A

For diagram of lipid IV_A biosynthesis, click here

Glossary:

a lipid A disaccharide = a dephospho-lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
a lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s):

lpxK (gene name); lipid-A 4′-kinase; ATP:2,2′,3,3′-tetrakis[(3R)-3-hydroxytetradecanoyl]-β-D-glucosaminyl-(1→6)-α-D-glucosaminyl-phosphate 4′-O-phosphotransferase

Systematic name:

ATP:2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose 4′-O-phosphotransferase

Comments:

Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.4.1.182 (lipid-A-disaccharide synthase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 107309-06-8

References:

1.	Ray, B.L. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. A novel kinase in Escherichia coli membranes that incorporates the 4′-phosphate of lipid A. J. Biol. Chem. 262 (1987) 1122–1128. [PMID: 3027079]
2.	Emptage, R.P., Daughtry, K.D., Pemble, C.W., 4th and Raetz, C.R. Crystal structure of LpxK, the 4′-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface. Proc. Natl. Acad. Sci. USA 109 (2012) 12956–12961. [DOI] [PMID: 22826246]
3.	Emptage, R.P., Pemble, C.W., 4th, York, J.D., Raetz, C.R. and Zhou, P. Mechanistic characterization of the tetraacyldisaccharide-1-phosphate 4′-kinase LpxK involved in lipid A biosynthesis. Biochemistry 52 (2013) 2280–2290. [DOI] [PMID: 23464738]
4.	Emptage, R.P., Tonthat, N.K., York, J.D., Schumacher, M.A. and Zhou, P. Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4′-kinase LpxK. J. Biol. Chem. 289 (2014) 24059–24068. [DOI] [PMID: 25023290]

[EC 2.7.1.130 created 1990, modified 2021]

2.3.1.129

Relevance: 79.3%

Accepted name:

acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase

Reaction:

a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-N-acetyl-α-D-glucosamine = an [acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine

For diagram of lipid IV_A biosynthesis, click here

Other name(s):

lpxA (gene name); UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase

Systematic name:

(3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-N-acetyl-α-D-glucosamine 3-O-(3-hydroxyacyl)transferase

Comments:

Involved with EC 2.4.1.182, lipid-A-disaccharide synthase, and EC 2.7.1.130, tetraacyldisaccharide 4′-kinase, in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-69-4

References:

1.	Anderson, M.S., Bulawa, C.E. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A precursors from UDP-GlcNAc in extracts of Escherichia coli. J. Biol. Chem. 260 (1985) 15536–15541. [PMID: 3905795]
2.	Anderson, M.S., Bull, H.G., Galloway, S.M., Kelly, T.M., Mohan, S., Radika, K. and Raetz, C.R. UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable. J. Biol. Chem. 268 (1993) 19858–19865. [PMID: 8366124]
3.	Raetz, C.R. and Roderick, S.L. A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270 (1995) 997–1000. [DOI] [PMID: 7481807]
4.	Williams, A.H. and Raetz, C.R. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase. Proc. Natl. Acad. Sci. USA 104 (2007) 13543–13550. [DOI] [PMID: 17698807]
5.	Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190 (2008) 4549–4558. [DOI] [PMID: 18456814]

[EC 2.3.1.129 created 1990, modified 2021]

2.4.99.15

Relevance: 74.7%

Accepted name:

(Kdo)₃-lipid IV_A (2-4) 3-deoxy-D-manno-octulosonic acid transferase

Reaction:

α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP-β-Kdo = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP

For diagram of Kdo₄-Lipid IV_A biosynthesis, click here

Glossary:

(Kdo)₃-lipid IV_A = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(Kdo)₄-lipid IV_A = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-[(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)]-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate

Other name(s):

Kdo transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)₃-lipid IV_A (2-4) 3-deoxy-D-manno-octulosonic acid transferase

Systematic name:

CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)₃-lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase [(2→4) glycosidic bond-forming]

Comments:

The enzyme from Chlamydia psittaci transfers four Kdo residues to lipid A, forming a branched tetrasaccharide with the structure α-Kdo-(2,8)-[α-Kdo-(2,4)]-α-Kdo-(2,4)-α-Kdo (cf. EC 2.4.99.12 [lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase], EC 2.4.99.13 [(Kdo)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase], and EC 2.4.99.14 [(Kdo)₂-lipid IV_A (2-8) 3-deoxy-D-manno-octulosonic acid transferase]).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Brabetz, W., Lindner, B. and Brade, H. Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12. Eur. J. Biochem. 267 (2000) 5458–5465. [DOI] [PMID: 10951204]
2.	Holst, O., Bock, K., Brade, L. and Brade, H. The structures of oligosaccharide bisphosphates isolated from the lipopolysaccharide of a recombinant Escherichia coli strain expressing the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of Chlamydia psittaci 6BC. Eur. J. Biochem. 229 (1995) 194–200. [DOI] [PMID: 7744029]

[EC 2.4.99.15 created 2010, modified 2011]

2.3.1.191

Relevance: 72.1%

Accepted name:

UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

Reaction:

a (3R)-3-hydroxyacyl-[acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + a holo-[acyl-carrier protein]

For diagram of lipid IV_A biosynthesis, click here

Other name(s):

lpxD (gene name); UDP-3-O-acyl-glucosamine N-acyltransferase; UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase; acyltransferase LpxD; acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase; firA (gene name); (3R)-3-hydroxymyristoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxymyristoyl]-α-D-glucosamine N-acetyltransferase; UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase; (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine N-acetyltransferase

Systematic name:

(3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine N-acyltransferase

Comments:

The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] [3], but it does not have an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism [5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Kelly, T.M., Stachula, S.A., Raetz, C.R. and Anderson, M.S. The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. J. Biol. Chem. 268 (1993) 19866–19874. [PMID: 8366125]
2.	Buetow, L., Smith, T.K., Dawson, A., Fyffe, S. and Hunter, W.N. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. Proc. Natl. Acad. Sci. USA 104 (2007) 4321–4326. [DOI] [PMID: 17360522]
3.	Bartling, C.M. and Raetz, C.R. Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 47 (2008) 5290–5302. [DOI] [PMID: 18422345]
4.	Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190 (2008) 4549–4558. [DOI] [PMID: 18456814]
5.	Bartling, C.M. and Raetz, C.R. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 48 (2009) 8672–8683. [DOI] [PMID: 19655786]
6.	Badger, J., Chie-Leon, B., Logan, C., Sridhar, V., Sankaran, B., Zwart, P.H. and Nienaber, V. Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 (2013) 6–9. [DOI] [PMID: 23295477]
7.	Kroeck, K.G., Sacco, M.D., Smith, E.W., Zhang, X., Shoun, D., Akhtar, A., Darch, S.E., Cohen, F., Andrews, L.D., Knox, J.E. and Chen, Y. Discovery of dual-activity small-molecule ligands of Pseudomonas aeruginosa LpxA and LpxD using SPR and X-ray crystallography. Sci. Rep. 9:15450 (2019). [DOI] [PMID: 31664082]

[EC 2.3.1.191 created 2010, modified 2021]

2.7.1.166

Relevance: 71.4%

Accepted name:

3-deoxy-D-manno-octulosonic acid kinase

Reaction:

α-Kdo-(2→6)-lipid IV_A + ATP = 4-O-phospho-α-Kdo-(2→6)-lipid IV_A + ADP

Glossary:

(Kdo)-lipid IV_A = α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(4-O-phospho-KDO)-lipid IV_A = 4-O-phospho-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-4-O-phosphono-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose

Other name(s):

kdkA (gene name); Kdo kinase

Systematic name:

ATP:(Kdo)-lipid IV_A 3-deoxy-α-D-manno-oct-2-ulopyranose 4-phosphotransferase

Comments:

The enzyme phosphorylates the 4-OH position of Kdo in (Kdo)-lipid IV_A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Brabetz, W., Muller-Loennies, S. and Brade, H. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and kdo kinase (KdkA) of Haemophilus influenzae are both required to complement a waaA knockout mutation of Escherichia coli. J. Biol. Chem. 275 (2000) 34954–34962. [DOI] [PMID: 10952982]
2.	Harper, M., Boyce, J.D., Cox, A.D., St Michael, F., Wilkie, I.W., Blackall, P.J. and Adler, B. Pasteurella multocida expresses two lipopolysaccharide glycoforms simultaneously, but only a single form is required for virulence: identification of two acceptor-specific heptosyl I transferases. Infect. Immun. 75 (2007) 3885–3893. [DOI] [PMID: 17517879]
3.	White, K.A., Kaltashov, I.A., Cotter, R.J. and Raetz, C.R. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae. J. Biol. Chem. 272 (1997) 16555–16563. [DOI] [PMID: 9195966]
4.	White, K.A., Lin, S., Cotter, R.J. and Raetz, C.R. A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence. J. Biol. Chem. 274 (1999) 31391–31400. [DOI] [PMID: 10531340]

[EC 2.7.1.166 created 2010, modified 2011]

2.4.99.14

Relevance: 70.9%

Accepted name:

(Kdo)₂-lipid IV_A (2-8) 3-deoxy-D-manno-octulosonic acid transferase

Reaction:

α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP-β-Kdo = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP

For diagram of Kdo₄-Lipid IV_A biosynthesis, click here

Glossary:

(Kdo)₂-lipid IV_A = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(Kdo)₃-lipid IV_A = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate

Other name(s):

Kdo transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)₂-lipid IV_A (2-8) 3-deoxy-D-manno-octulosonic acid transferase

Systematic name:

CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)₂-lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase [(2→8) glycosidic bond-forming]

Comments:

The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Lobau, S., Mamat, U., Brabetz, W. and Brade, H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-α-D-manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol. Microbiol. 18 (1995) 391–399. [DOI] [PMID: 8748024]
2.	Mamat, U., Baumann, M., Schmidt, G. and Brade, H. The genus-specific lipopolysaccharide epitope of Chlamydia is assembled in C. psittaci and C. trachomatis by glycosyltransferases of low homology. Mol. Microbiol. 10 (1993) 935–941. [DOI] [PMID: 7523826]
3.	Belunis, C.J., Mdluli, K.E., Raetz, C.R. and Nano, F.E. A novel 3-deoxy-D-manno-octulosonic acid transferase from Chlamydia trachomatis required for expression of the genus-specific epitope. J. Biol. Chem. 267 (1992) 18702–18707. [PMID: 1382060]

[EC 2.4.99.14 created 2010, modified 2011]

2.4.1.256

Relevance: 70.7%

Accepted name:

dolichyl-P-Glc:Glc₂Man₉GlcNAc₂-PP-dolichol α-1,2-glucosyltransferase

Reaction:

dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = dolichyl phosphate + α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Other name(s):

ALG10; Dol-P-Glc:Glc₂Man₉GlcNAc₂-PP-Dol α-1,2-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-glucosyltransferase

Systematic name:

dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase (configuration-retaining)

Comments:

This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455–462. [DOI] [PMID: 9597543]

[EC 2.4.1.256 created 2011, modified 2012]

1.14.11.58

Relevance: 69.8%

Accepted name:

ornithine lipid ester-linked acyl 2-hydroxylase

Reaction:

an ornithine lipid + 2-oxoglutarate + O₂ = a 2-hydroxyornithine lipid + succinate + CO₂

Glossary:

an ornithine lipid = an N^α-[(3R)-3-(acyloxy)acyl]-L-ornithine
a 2-hydroxyornithine lipid = an N^α-[(3R)-3-(2-hydroxyacyloxy)acyl]-L-ornithine

Other name(s):

olsC (gene name)

Systematic name:

ornithine lipid,2-oxoglutarate:oxygen oxidoreductase (ester-linked acyl 2-hydroxylase)

Comments:

The enzyme, characterized from the bacterium Rhizobium tropici, catalyses the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Rojas-Jimenez, K., Sohlenkamp, C., Geiger, O., Martinez-Romero, E., Werner, D. and Vinuesa, P. A ClC chloride channel homolog and ornithine-containing membrane lipids of Rhizobium tropici CIAT899 are involved in symbiotic efficiency and acid tolerance. Mol. Plant Microbe Interact. 18 (2005) 1175–1185. [DOI] [PMID: 16353552]
2.	Vences-Guzman, M.A., Guan, Z., Ormeno-Orrillo, E., Gonzalez-Silva, N., Lopez-Lara, I.M., Martinez-Romero, E., Geiger, O. and Sohlenkamp, C. Hydroxylated ornithine lipids increase stress tolerance in Rhizobium tropici CIAT899. Mol. Microbiol. 79 (2011) 1496–1514. [DOI] [PMID: 21205018]

[EC 1.14.11.58 created 2018]

2.3.1.270

Relevance: 68.8%

Accepted name:

lyso-ornithine lipid O-acyltransferase

Reaction:

a lyso-ornithine lipid + an acyl-[acyl-carrier protein] = an ornithine lipid + a holo-[acyl-carrier protein]

Glossary:

a lyso-ornithine lipid = an N^α-[(3R)-3-hydroxyacyl]-L-ornithine
an ornithine lipid = an N^α-[(3R)-3-(acyloxy)acyl]-L-ornithine

Other name(s):

olsA (gene name)

Systematic name:

N^α-[(3R)-hydroxy-acyl]-L-ornithine O-acyltransferase

Comments:

This bacterial enzyme catalyses the second step in the formation of ornithine lipids.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Weissenmayer, B., Gao, J.L., Lopez-Lara, I.M. and Geiger, O. Identification of a gene required for the biosynthesis of ornithine-derived lipids. Mol. Microbiol. 45 (2002) 721–733. [PMID: 12139618]
2.	Aygun-Sunar, S., Bilaloglu, R., Goldfine, H. and Daldal, F. Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both ornithine lipid and phosphatidic acid biosynthesis. J. Bacteriol. 189 (2007) 8564–8574. [PMID: 17921310]
3.	Lewenza, S., Falsafi, R., Bains, M., Rohs, P., Stupak, J., Sprott, G.D. and Hancock, R.E. The olsA gene mediates the synthesis of an ornithine lipid in Pseudomonas aeruginosa during growth under phosphate-limiting conditions, but is not involved in antimicrobial peptide susceptibility. FEMS Microbiol. Lett. 320 (2011) 95–102. [DOI] [PMID: 21535098]

[EC 2.3.1.270 created 2018]

2.4.2.43

Relevance: 67.9%

Accepted name:

lipid IV_A 4-amino-4-deoxy-L-arabinosyltransferase

Reaction:

(1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-α-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IV_A = lipid II_A + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = 4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + ditrans,octacis-undecaprenyl phosphate

For diagram of lipid II_A biosynthesis, click here

Glossary:

lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
lipid II_A = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4′-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose

Other name(s):

undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK; arnT (gene name)

Systematic name:

4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl-phosphate:lipid IV_A 4-amino-4-deoxy-L-arabinopyranosyltransferase

Comments:

Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IV_A. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122–43131. [DOI] [PMID: 11535604]
2.	Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132–43144. [DOI] [PMID: 11535605]
3.	Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111–43121. [DOI] [PMID: 11535603]
4.	Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33–39. [DOI] [PMID: 16226890]
5.	Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29–35. [DOI] [PMID: 19947657]

[EC 2.4.2.43 created 2010, modified 2011]

1.14.19.47

Relevance: 67.1%

Accepted name:

acyl-lipid (9-3)-desaturase

Reaction:

(1) an α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = a stearidonoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O
(2) a linoleoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = a γ-linolenoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O

Glossary:

stearidonic acid = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid

Other name(s):

DES6 (gene name); acyl-lipid 6-desaturase; acyl-lipid Δ⁶-desaturase; Δ⁶-desaturase (ambiguous)

Systematic name:

Δ⁹ acyl-[glycerolipid],ferrocytochrome b₅:oxygen oxidoreductase (6,7-cis-dehydrogenating)

Comments:

The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Δ⁹ cis double bond. The enzyme contains a cytochrome b₅ domain that acts as the electron donor for the active site of the desaturase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Sayanova, O., Smith, M.A., Lapinskas, P., Stobart, A.K., Dobson, G., Christie, W.W., Shewry, P.R. and Napier, J.A. Expression of a borage desaturase cDNA containing an N-terminal cytochrome b₅ domain results in the accumulation of high levels of Δ⁶-desaturated fatty acids in transgenic tobacco. Proc. Natl. Acad. Sci. USA 94 (1997) 4211–4216. [DOI] [PMID: 9108131]
2.	Girke, T., Schmidt, H., Zähringer, U., Reski, R. and Heinz, E. Identification of a novel Δ⁶-acyl-group desaturase by targeted gene disruption in Physcomitrella patens. Plant J. 15 (1998) 39–48. [DOI] [PMID: 9744093]

[EC 1.14.19.47 created 2015]

2.7.4.29

Relevance: 66.7%

Accepted name:

Kdo₂-lipid A phosphotransferase

Reaction:

ditrans-octacis-undecaprenyl diphosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = ditrans-octacis-undecaprenyl phosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A 1-diphosphate

Glossary:

lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A 1-diphosphate =
2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl diphosphate

Other name(s):

lipid A undecaprenyl phosphotransferase; LpxT; YeiU

Systematic name:

ditrans-octacis-undecaprenyl-diphosphate:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A phosphotransferase

Comments:

An inner-membrane protein. The activity of the enzyme is regulated by PmrA. In vitro the enzyme can use diacylglycerol 3-diphosphate as the phosphate donor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Touze, T., Tran, A.X., Hankins, J.V., Mengin-Lecreulx, D. and Trent, M.S. Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate. Mol. Microbiol. 67 (2008) 264–277. [DOI] [PMID: 18047581]
2.	Herrera, C.M., Hankins, J.V. and Trent, M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76 (2010) 1444–1460. [DOI] [PMID: 20384697]

[EC 2.7.4.29 created 2015]

3.6.1.54

Relevance: 66.3%

Accepted name:

UDP-2,3-diacylglucosamine diphosphatase

Reaction:

a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + H₂O = a lipid X + UMP

For diagram of lipid IV_A biosynthesis, click here

Glossary:

a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine

Other name(s):

lpxH (gene name); UDP-2,3-diacylglucosamine hydrolase; UDP-2,3-diacylglucosamine pyrophosphatase; ybbF (gene name); UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-α-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-β-D-glucosaminyl 1-phosphate phosphohydrolase (incorrect); UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosaminyl 1-phosphate phosphohydrolase

Systematic name:

UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine-1-phosphate phosphohydrolase

Comments:

The enzyme catalyses a step in the biosynthesis of lipid A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Babinski, K.J., Ribeiro, A.A. and Raetz, C.R. The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis. J. Biol. Chem. 277 (2002) 25937–25946. [DOI] [PMID: 12000770]
2.	Babinski, K.J., Kanjilal, S.J. and Raetz, C.R. Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene. J. Biol. Chem. 277 (2002) 25947–25956. [DOI] [PMID: 12000771]
3.	Okada, C., Wakabayashi, H., Kobayashi, M., Shinoda, A., Tanaka, I. and Yao, M. Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa. Sci. Rep. 6:32822 (2016). [DOI] [PMID: 27609419]
4.	Cho, J., Lee, C.J., Zhao, J., Young, H.E. and Zhou, P. Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol 1:16154 (2016). [DOI] [PMID: 27780190]
5.	Arenas, J., Pupo, E., de Jonge, E., Perez-Ortega, J., Schaarschmidt, J., van der Ley, P. and Tommassen, J. Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A. J. Biol. Chem. 294 (2019) 7982–7989. [DOI] [PMID: 30926608]

[EC 3.6.1.54 created 2010, modified 2021]

1.14.19.33

Relevance: 65.9%

Accepted name:

Δ¹² acyl-lipid conjugase (11E,13E-forming)

Reaction:

(1) a linoleoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = an α-eleostearoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O
(2) a γ-linolenoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = an α-parinaroyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O

Glossary:

α-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
α-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
γ-linolenic acid = (6Z,9Z,12Z)-octadeca-6,9,12-trienoic acid
linoleic acid = (9Z,12Z)-octadeca-9,12-dienoic acid

Other name(s):

fatty acid Δ¹²-conjugase (ambiguous); FADX (gene name)

Systematic name:

Δ¹² acyl-lipid,ferrocytochrome-b₅:oxygen 11,14 allylic oxidase (11E,13E-forming)

Comments:

The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13. The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate. cf. EC 1.14.19.16, linoleoyl-lipid Δ¹² conjugase (11E,13Z-forming).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Cahoon, E.B., Carlson, T.J., Ripp, K.G., Schweiger, B.J., Cook, G.A., Hall, S.E. and Kinney, A.J. Biosynthetic origin of conjugated double bonds: production of fatty acid components of high-value drying oils in transgenic soybean embryos. Proc. Natl. Acad. Sci. USA 96 (1999) 12935–12940. [DOI] [PMID: 10536026]
2.	Dyer, J.M., Chapital, D.C., Kuan, J.C., Mullen, R.T., Turner, C., McKeon, T.A. and Pepperman, A.B. Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity. Plant Physiol. 130 (2002) 2027–2038. [DOI] [PMID: 12481086]

[EC 1.14.19.33 created 2015]

2.3.1.305

Relevance: 65.6%

Accepted name:

acyl-[acyl-carrier protein]—UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose N-acyltransferase

Reaction:

a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose = an [acyl-carrier protein] + a UDP-2-acetamido-2,3-dideoxy-3-{[(3R)-3-hydroxyacyl]amino}-α-D-glucopyranose

Other name(s):

lpxA (gene name) (ambiguous)

Systematic name:

(3R)-3-hydroxyacyl-[acyl-carrier-protein]:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose 3-N-[(3R)-hydroxyacyl]transferase

Comments:

The enzyme is found in bacterial species whose lipid A contains 2,3-diamino-2,3-dideoxy-D-glucopyranose. Some enzymes, such as that from Leptospira interrogans, are highly specific for 2,3-diamino-2,3-dideoxy-D-glucopyranose, while others, such as the enzyme from Acidithiobacillus ferrooxidans, are also able to accept UDP-N-acetyl-α-D-glucosamine (cf. EC 2.3.1.129, acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase). The enzymes from different organisms also differ in their specificity for the acyl donor. The enzyme from Leptospira interrogans is highly specific for (3R)-3-hydroxydodecanoyl-[acp], while that from Mesorhizobium loti functions almost equally well with 10-, 12-, and 14-carbon 3-hydroxyacyl-[acp]s.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Sweet, C.R., Williams, A.H., Karbarz, M.J., Werts, C., Kalb, S.R., Cotter, R.J. and Raetz, C.R. Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group. J. Biol. Chem. 279 (2004) 25411–25419. [DOI] [PMID: 15044493]
2.	Robins, L.I., Williams, A.H. and Raetz, C.R. Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA. Biochemistry 48 (2009) 6191–6201. [DOI] [PMID: 19456129]

[EC 2.3.1.305 created 2021]

2.7.4.30

Transferred entry:

lipid A phosphoethanolamine transferase. Now EC 2.7.8.43, lipid A phosphoethanolamine transferase

[EC 2.7.4.30 created 2015, deleted 2016]

2.7.8.43

Relevance: 65.2%

Accepted name:

lipid A phosphoethanolamine transferase

Reaction:

(1) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
(2) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4′-(2-aminoethyl diphosphate)
(3) diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4′-bis(2-aminoethyl diphosphate)

Glossary:

lipid A (Campylobacter jejuni) = 2,3-dideoxy-2,3-bis[(3R)-3-(hexadecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A (Escherichia coli) =
2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
lipid A (Helicobacter pylori) = 2-deoxy-2-[(3R)-3-(octadecanoyloxy)octadecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyhexadecanoyl]-2-[(3R)-3-hydroxyoctadecanamido]-α-D-glucopyranosyl phosphate
lipid A (Neisseria meningitidis) =
2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid A 1-[(2-aminoethyl) diphosphate] = P1-(2-aminoethyl)
P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate
lipid A 1,4′-bis(2-aminoethyl diphosphate) = P1-(2-aminoethyl)
P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-(2-aminoethyldiphospho)-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate

Other name(s):

lipid A PEA transferase; LptA

Systematic name:

diacylphosphatidylethanolamine:lipid-A ethanolaminephosphotransferase

Comments:

The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IV_A 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-β-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IV_A and Kdo₂-lipid A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Tran, A.X., Karbarz, M.J., Wang, X., Raetz, C.R., McGrath, S.C., Cotter, R.J. and Trent, M.S. Periplasmic cleavage and modification of the 1-phosphate group of Helicobacter pylori lipid A. J. Biol. Chem. 279 (2004) 55780–55791. [DOI] [PMID: 15489235]
2.	Herrera, C.M., Hankins, J.V. and Trent, M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76 (2010) 1444–1460. [DOI] [PMID: 20384697]
3.	Cullen, T.W. and Trent, M.S. A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni. Proc. Natl. Acad. Sci. USA 107 (2010) 5160–5165. [DOI] [PMID: 20194750]
4.	Anandan, A., Piek, S., Kahler, C.M. and Vrielink, A. Cloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 1494–1497. [DOI] [PMID: 23192031]
5.	Wanty, C., Anandan, A., Piek, S., Walshe, J., Ganguly, J., Carlson, R.W., Stubbs, K.A., Kahler, C.M. and Vrielink, A. The structure of the neisserial lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin. J. Mol. Biol. 425 (2013) 3389–3402. [DOI] [PMID: 23810904]

[EC 2.7.8.43 created 2015 as EC 2.7.4.30, transferred 2016 to EC 2.7.8.43]

2.4.99.13

Relevance: 64.9%

Accepted name:

(Kdo)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase

Reaction:

CMP-β-Kdo + an α-Kdo-(2→6)-[lipid IV_A] = CMP + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IV_A]

For diagram of Kdo₄-Lipid IV_A biosynthesis, click here

Glossary:

CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate
a lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s):

waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase; CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)-lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase; Kdo transferase (ambiguous)

Systematic name:

CMP-3-deoxy-β-D-manno-oct-2-ulosonate:α-Kdo-(2→6)-[lipid IV_A] 3-deoxy-D-manno-oct-2-ulosonate transferase (configuration-inverting)

Comments:

The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IV_A (cf. EC 2.4.99.12 [lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Belunis, C.J. and Raetz, C.R. Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli. J. Biol. Chem. 267 (1992) 9988–9997. [PMID: 1577828]
2.	Lobau, S., Mamat, U., Brabetz, W. and Brade, H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-α-D-manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol. Microbiol. 18 (1995) 391–399. [DOI] [PMID: 8748024]
3.	Schmidt, H., Hansen, G., Singh, S., Hanuszkiewicz, A., Lindner, B., Fukase, K., Woodard, R.W., Holst, O., Hilgenfeld, R., Mamat, U. and Mesters, J.R. Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis. Proc. Natl. Acad. Sci. USA 109 (2012) 6253–6258. [DOI] [PMID: 22474366]

[EC 2.4.99.13 created 2010, modified 2011, modified 2021]

3.5.1.108

Relevance: 64.5%

Accepted name:

UDP-3-O-acyl-N-acetylglucosamine deacetylase

Reaction:

a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine + H₂O = a UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine + acetate

For diagram of lipid IV_A biosynthesis, click here

Other name(s):

LpxC protein; LpxC enzyme; LpxC deacetylase; deacetylase LpxC; UDP-3-O-acyl-GlcNAc deacetylase; UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-acyl)-N-acetylglucosamine deacetylase; UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase; UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase

Systematic name:

UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine amidohydrolase

Comments:

A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. J. Biol. Chem. 280 (2005) 16969–16978. [DOI] [PMID: 15705580]
2.	Jackman, J.E., Raetz, C.R. and Fierke, C.A. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry 38 (1999) 1902–1911. [DOI] [PMID: 10026271]
3.	Hyland, S.A., Eveland, S.S. and Anderson, M.S. Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway. J. Bacteriol. 179 (1997) 2029–2037. [DOI] [PMID: 9068651]
4.	Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. Anal. Biochem. 290 (2001) 338–346. [DOI] [PMID: 11237337]
5.	Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 8146–8150. [DOI] [PMID: 12819349]
6.	Mochalkin, I., Knafels, J.D. and Lightle, S. Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor. Protein Sci. 17 (2008) 450–457. [DOI] [PMID: 18287278]

[EC 3.5.1.108 created 2010, modified 2021]

2.4.1.267

Relevance: 64.3%

Accepted name:

dolichyl-P-Glc:Man₉GlcNAc₂-PP-dolichol α-1,3-glucosyltransferase

Reaction:

dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Other name(s):

ALG6; Dol-P-Glc:Man₉GlcNAc₂-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase

Systematic name:

dolichyl β-D-glucosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)

Comments:

The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc₁Man₉GlcNAc₂-PP-Dol α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc₂Man₉GlcNAc₂-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493–498. [DOI] [PMID: 8877369]
2.	Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412–417. [PMID: 6423630]
3.	Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420–421. [DOI] [PMID: 14517965]

[EC 2.4.1.267 created 2011, modified 2012]

2.4.1.265

Relevance: 63.3%

Accepted name:

dolichyl-P-Glc:Glc₁Man₉GlcNAc₂-PP-dolichol α-1,3-glucosyltransferase

Reaction:

dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Other name(s):

ALG8; Dol-P-Glc:Glc₁Man₉GlcNAc₂-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase

Systematic name:

dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)

Comments:

The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man₉GlcNAc₂-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc₂Man₉GlcNAc₂-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977–5981. [DOI] [PMID: 8016100]
2.	Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582–15590. [PMID: 3536907]
3.	Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc₁Man₉GlcNAc₂-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962–9971. [DOI] [PMID: 12480927]

[EC 2.4.1.265 created 2011, modified 2012]

2.4.1.180

Relevance: 61.9%

Accepted name:

lipopolysaccharide N-acetylmannosaminouronosyltransferase

Reaction:

UDP-N-acetyl-α-D-mannosaminouronate + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Glossary:

N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate

Other name(s):

ManNAcA transferase; uridine diphosphoacetylmannosaminuronate-acetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminuronosyltransferase; UDP-N-acetyl-β-D-mannosaminouronate:lipid I N-acetyl-β-D-mannosaminouronosyltransferase (incorrect)

Systematic name:

UDP-N-acetyl-α-D-mannosaminouronate:lipid I N-acetyl-α-D-mannosaminouronosyltransferase

Comments:

Involved in the biosynthesis of common antigen in Enterobacteriaceae.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-30-1

References:

Barr, K., Ward, S., Meier-Dieter, U., Mayer, H. and Rick, P.D. Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis. J. Bacteriol. 170 (1988) 228–233. [DOI] [PMID: 3275612]

[EC 2.4.1.180 created 1990, modified 2011]

2.3.1.265

Relevance: 61.7%

Accepted name:

phosphatidylinositol dimannoside acyltransferase

Reaction:

(1) an acyl-CoA + 2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-α-D-mannosyl)-6-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2) an acyl-CoA + 2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol

Other name(s):

PIM2 acyltransferase; ptfP1 (gene name)

Systematic name:

acyl-CoA:2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol acyltransferase

Comments:

The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Svetlikova, Z., Barath, P., Jackson, M., Kordulakova, J. and Mikusova, K. Purification and characterization of the acyltransferase involved in biosynthesis of the major mycobacterial cell envelope glycolipid—monoacylated phosphatidylinositol dimannoside. Protein Expr. Purif. 100 (2014) 33–39. [DOI] [PMID: 24810911]

[EC 2.3.1.265 created 2017]

1.14.19.25

Relevance: 60.2%

Accepted name:

acyl-lipid ω-3 desaturase (cytochrome b₅)

Reaction:

a linoleoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = an α-linolenoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O

Glossary:

linoleoyl-[glycerolipid] = (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid]
α-linolenoyl-[glycerolipid] = (9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid]

Other name(s):

FAD3

Systematic name:

(9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid],ferrocytochrome b₅:oxygen oxidoreductase (15,16 cis-dehydrogenating)

Comments:

This microsomal enzyme introduces a cis double bond three carbons away from the methyl end of a fatty acid incorporated into a glycerolipid. The distance from the carboxylic acid end of the molecule does not have an effect. The plant enzyme acts on carbon 15 of linoleoyl groups incorporated into both the sn-1 and sn-2 positions of the glycerol backbone of phosphatidylcholine and other phospholipids, converting them into α-linolenoyl groups. The enzyme from the fungus Mortierella alpina acts on γ-linolenoyl and arachidonoyl groups, converting them into stearidonoyl and icosapentaenoyl groups, respectively [3]. cf. EC 1.14.19.35, sn-2 acyl-lipid ω-3 desaturase (ferredoxin).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Browse, J., McConn, M., James, D., Jr. and Miquel, M. Mutants of Arabidopsis deficient in the synthesis of α-linolenate. Biochemical and genetic characterization of the endoplasmic reticulum linoleoyl desaturase. J. Biol. Chem. 268 (1993) 16345–16351. [PMID: 8102138]
2.	Arondel, V., Lemieux, B., Hwang, I., Gibson, S., Goodman, H.M. and Somerville, C.R. Map-based cloning of a gene controlling ω-3 fatty acid desaturation in Arabidopsis. Science 258 (1992) 1353–1355. [DOI] [PMID: 1455229]
3.	Sakuradani, E., Abe, T., Iguchi, K. and Shimizu, S. A novel fungal ω³-desaturase with wide substrate specificity from arachidonic acid-producing Mortierella alpina 1S-4. Appl. Microbiol. Biotechnol. 66 (2005) 648–654. [DOI] [PMID: 15538555]

[EC 1.14.19.25 created 2015]

2.1.1.344

Relevance: 60.1%

Accepted name:

ornithine lipid N-methyltransferase

Reaction:

3 S-adenosyl-L-methionine + an ornithine lipid = 3 S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid (overall reaction)
(1a) S-adenosyl-L-methionine + an ornithine lipid = S-adenosyl-L-homocysteine + an N-methylornithine lipid
(1b) S-adenosyl-L-methionine + an N-methylornithine lipid = S-adenosyl-L-homocysteine + an N,N-dimethylornithine lipid
(1c) S-adenosyl-L-methionine + an N,N-dimethylornithine lipid = S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid

Glossary:

an ornithine lipid = an N^α-[(3R)-3-(acyloxy)acyl]-L-ornithine

Other name(s):

olsG (gene name)

Systematic name:

S-adenosyl-L-methionine:ornithine lipid N-methyltransferase

Comments:

The enzyme, characterized from the bacterium Singulisphaera acidiphila, catalyses three successive methylations of the terminal δ-nitrogen in ornithine lipids.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Escobedo-Hinojosa, W.I., Vences-Guzman, M.A., Schubotz, F., Sandoval-Calderon, M., Summons, R.E., Lopez-Lara, I.M., Geiger, O. and Sohlenkamp, C. OlsG (Sinac_1600) is an ornithine lipid N-methyltransferase from the planctomycete Singulisphaera acidiphila. J. Biol. Chem. 290 (2015) 15102–15111. [DOI] [PMID: 25925947]

[EC 2.1.1.344 created 2017]

1.14.19.12

Relevance: 59.5%

Accepted name:

acyl-lipid ω-(9-4) desaturase

Reaction:

(1) linoleoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = pinolenoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O
(2) α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = coniferonoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O

Glossary:

taxoleate = (5Z,9Z)-octadeca-5,9-dienoate
pinolenoate = (5Z,9Z,12Z)-octadeca-5,9,12-trienoate
coniferonate = (5Z,9Z,12Z,15Z)-octadeca-5,9,12,15-tetraenoate

Other name(s):

acyl-lipid ω-13 desaturase; acyl-lipid 7-desaturase (ambiguous)

Systematic name:

acyl-[glycerolipid],ferrocytochrome b₅:oxygen oxidoreductase [ω(9-4),ω(9-5) cis-dehydrogenating]

Comments:

The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in ω⁹ unsaturated C₁₈ or C₂₀ fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing ω⁹ bond, towards the carboxy end of the fatty acid (at the ω¹³ position). When acting on 20:2Δ(11,14) and 20:3Δ(11,14,17) substrates it introduces the new double bond between carbons 7 and 8. The enzyme contains a cytochrome b₅ domain that acts as the direct electron donor for the active site of the desaturase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Kajikawa, M., Yamato, K.T., Kohzu, Y., Shoji, S., Matsui, K., Tanaka, Y., Sakai, Y. and Fukuzawa, H. A front-end desaturase from Chlamydomonas reinhardtii produces pinolenic and coniferonic acids by ω¹³ desaturation in methylotrophic yeast and tobacco. Plant Cell Physiol. 47 (2006) 64–73. [DOI] [PMID: 16267098]

[EC 1.14.19.12 created 2015]

2.3.1.288

Relevance: 58.4%

Accepted name:

2-O-sulfo trehalose long-chain-acyltransferase

Reaction:

(1) stearoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2′-stearoyl-α,α-trehalose + CoA
(2) palmitoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2′-palmitoyl-α,α-trehalose + CoA

Other name(s):

papA₂ (gene name)

Systematic name:

acyl-CoA:2-O-sulfo-α,α-trehalose 2′-long-chain-acyltransferase

Comments:

This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-α,α-trehalose at the 2′ position by a C₁₆ or C₁₈ fatty acyl group during the biosynthesis of mycobacterial sulfolipids.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl. Acad. Sci. USA 104 (2007) 11221–11226. [PMID: 17592143]
2.	Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 287 (2012) 7990–8000. [PMID: 22194604]

[EC 2.3.1.288 created 2019]

2.4.1.130

Transferred entry:

dolichyl-phosphate-mannose—glycolipid α-mannosyltransferase. Now covered by EC 2.4.1.258 (Dol-P-Man:Man₅GlcNAc₂-PP-Dol α-1,3-mannosyltransferase), EC 2.4.1.259 (Dol-P-Man:Man₆GlcNAc₂-PP-Dol α-1,2-mannosyltransferase), EC 2.4.1.260 (Dol-P-Man:Man₇GlcNAc₂-PP-Dol α-1,6-mannosyltransferase) and EC 2.4.1.261 (Dol-P-Man:Man₈GlcNAc₂-PP-Dol α-1,2-mannosyltransferase).

[EC 2.4.1.130 created 1984, deleted 2011]

1.14.19.35

Relevance: 57.4%

Accepted name:

sn-2 acyl-lipid ω-3 desaturase (ferredoxin)

Reaction:

(1) a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O₂ + 2 H⁺ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H₂O
(2) a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O₂ + 2 H⁺ = an α-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H₂O

Glossary:

(9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid] = linoleoyl-[glycerolipid]
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid] = α-linolenoyl-[glycerolipid]

Other name(s):

FAD7; FAD8

Systematic name:

(7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (13,14 cis-dehydrogenating)

Comments:

This plastidial enzyme desaturates 16:2 fatty acids attached to the sn-2 position of glycerolipids to 16:3 fatty acids, and converts18:2 to 18:3 in both the sn-1 and sn-2 positions. It acts on all 16:2- or 18:2-containing chloroplast membrane lipids, including phosphatidylglycerol, monogalactosyldiacylglycerol, digalactosyldiaclyglycerol, and sulfoquinovosyldiacylglycerol. The enzyme introduces a cis double bond at a location 3 carbons away from the methyl end of the fatty acid. The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond. cf. EC 1.14.19.25, acyl-lipid ω-3 desaturase (cytochrome b₅) and EC 1.14.19.36, sn-1 acyl-lipid ω-3 desaturase (ferredoxin).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Iba, K., Gibson, S., Nishiuchi, T., Fuse, T., Nishimura, M., Arondel, V., Hugly, S. and Somerville, C. A gene encoding a chloroplast ω-3 fatty acid desaturase complements alterations in fatty acid desaturation and chloroplast copy number of the fad7 mutant of Arabidopsis thaliana. J. Biol. Chem. 268 (1993) 24099–24105. [PMID: 8226956]
2.	McConn, M., Hugly, S., Browse, J. and Somerville, C. A mutation at the fad8 locus of Arabidopsis identifies a second chloroplast ω-3 desaturase. Plant Physiol. 106 (1994) 1609–1614. [PMID: 12232435]
3.	Venegas-Caleron, M., Muro-Pastor, A.M., Garces, R. and Martinez-Force, E. Functional characterization of a plastidial ω-3 desaturase from sunflower (Helianthus annuus) in cyanobacteria. Plant Physiol. Biochem. 44 (2006) 517–525. [DOI] [PMID: 17064923]

[EC 1.14.19.35 created 2015]

1.14.19.36

Relevance: 57.1%

Accepted name:

sn-1 acyl-lipid ω-3 desaturase (ferredoxin)

Reaction:

(1) a 1-γ-linolenoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O₂ + 2 H⁺ = a 1-stearidonoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H₂O
(2) a 1-linoleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O₂ + 2 H⁺ = a 1-α-linolenoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H₂O

Glossary:

stearidonic acid = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid

Other name(s):

desB (gene name)

Systematic name:

1-γ-linolenoyl-2-acyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (15,16 cis-dehydrogenating)

Comments:

The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 15 of linoleoyl and γ-linolenoyl groups attached to the sn-1 position of glycerolipids. The enzyme is an ω desaturase, and determines the location of the double bond by counting three carbons from the methyl end of the fatty acid. It is nonspecific with respect to the polar head group of the glycerolipid. cf. EC 1.14.19.35, sn-2 acyl-lipid ω-3 desaturase (ferredoxin).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Sakamoto, T., Los, D.A., Higashi, S., Wada, H., Nishida, I., Ohmori, M. and Murata, N. Cloning of ω³ desaturase from cyanobacteria and its use in altering the degree of membrane-lipid unsaturation. Plant Mol. Biol. 26 (1994) 249–263. [PMID: 7524725]

[EC 1.14.19.36 created 2015]

4.6.1.14

Relevance: 57%

Accepted name:

glycosylphosphatidylinositol diacylglycerol-lyase

Reaction:

6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol

For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here

Other name(s):

(glycosyl)phosphatidylinositol-specific phospholipase C; GPI-PLC; GPI-specific phospholipase C; VSG-lipase; glycosyl inositol phospholipid anchor-hydrolyzing enzyme; glycosylphosphatidylinositol-phospholipase C; glycosylphosphatidylinositol-specific phospholipase C; variant-surface-glycoprotein phospholipase C; 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)

Systematic name:

6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming]

Comments:

This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC 3.1.4.50, glycosylphosphatidylinositol phospholipase D.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129070-68-4

References:

1.	Hereld, D., Krakow, J.L., Bangs, J.D., Hart, G.W. and Englund, P.T. A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein. J. Biol. Chem. 261 (1986) 13813–13819. [PMID: 3759991]
2.	Carnall, N., Webb, H. and Carrington, M. Mutagenesis study of the glycosylphosphatidylinositol phospholipase C of Trypanosoma brucei. Mol. Biochem. Parasitol. 90 (1997) 423–432. [DOI] [PMID: 9476790]
3.	Armah, D.A. and Mensa-Wilmot, K. Tetramerization of glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei. J. Biol. Chem. 275 (2000) 19334–19342. [DOI] [PMID: 10764777]

[EC 4.6.1.14 created 1989 as EC 3.1.4.47, transferred 2002 to EC 4.6.1.14]

2.4.1.346

Relevance: 56.8%

Accepted name:

phosphatidyl-myo-inositol dimannoside synthase

Reaction:

(1) GDP-α-D-mannose + 2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = GDP + 2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2) GDP-α-D-mannose + 2-O-(6-O-acyl-α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(6-O-acyl-α-D-mannosyl)-6-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol

Glossary:

1-phosphatidyl-1D-myo-inositol = PtdIns

Other name(s):

mannosyltransferase PimB; PimB; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase (ambiguous)

Systematic name:

GDP-α-D-mannose:2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol 6-α-D-mannosyltransferase (configuration-retaining)

Comments:

Requires Mg²⁺. The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Guerin, M.E., Kaur, D., Somashekar, B.S., Gibbs, S., Gest, P., Chatterjee, D., Brennan, P.J. and Jackson, M. New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB′ is an essential enzyme of Mycobacterium smegmatis. J. Biol. Chem. 284 (2009) 25687–25696. [DOI] [PMID: 19638342]
2.	Mishra, A.K., Batt, S., Krumbach, K., Eggeling, L. and Besra, G.S. Characterization of the Corynebacterium glutamicum Δ pimB′ Δ mgtA double deletion mutant and the role of Mycobacterium tuberculosis orthologues Rv2188c and Rv0557 in glycolipid biosynthesis. J. Bacteriol. 191 (2009) 4465–4472. [DOI] [PMID: 19395496]
3.	Batt, S.M., Jabeen, T., Mishra, A.K., Veerapen, N., Krumbach, K., Eggeling, L., Besra, G.S. and Futterer, K. Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB′. J. Biol. Chem. 285 (2010) 37741–37752. [DOI] [PMID: 20843801]

[EC 2.4.1.346 created 2017]

2.4.1.260

Relevance: 56.8%

Accepted name:

dolichyl-P-Man:Man₇GlcNAc₂-PP-dolichol α-1,6-mannosyltransferase

Reaction:

dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Other name(s):

ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man₇GlcNAc₂-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man₇GlcNAc₂-PP-dolichyl α6-mannosyltransferase; EBS4; Dol-P-Man:Man₇GlcNAc₂-PP-Dol α-1,6-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase

Systematic name:

dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting)

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]
2.	Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21 (2009) 3792–3802. [DOI] [PMID: 20023196]
3.	Cipollo, J.F. and Trimble, R.B. The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc₃Man₉GlcNAc₂-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12 (2002) 749–762. [PMID: 12460943]
4.	Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum. Mol. Genet. 11 (2002) 2331–2339. [DOI] [PMID: 12217961]

[EC 2.4.1.260 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.160, modified 2012]

1.14.19.34

Relevance: 56.6%

Accepted name:

acyl-lipid (9+3)-(E)-desaturase

Reaction:

(1) an oleoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O
(2) a palmitoleoyl-[glycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = a (9Z,12E)-hexadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b₅ + 2 H₂O

Other name(s):

acyl-lipid 12-(E)-desaturase; DsFAD2-1; FADX

Systematic name:

Δ⁹ acyl-lipid,ferrocytochrome b₅:oxygen oxidoreductase (12,13 trans-dehydrogenating)

Comments:

The enzymes from the plants Dimorphotheca sinuata (African daisy) and Vernicia fordii (tung oil tree) insert a trans double bond in position C-12 of oleate and palmitoleate incorporated into glycerolipids. The enzyme introduces the new double bond at a position three carbons away from an existing double bond at position 9, towards the methyl end of the fatty acid. The enzyme from tung oil tree also possesses the activity of EC 1.14.19.33, Δ¹² acyl-lipid conjugase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Dyer, J.M., Chapital, D.C., Kuan, J.C., Mullen, R.T., Turner, C., McKeon, T.A. and Pepperman, A.B. Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity. Plant Physiol. 130 (2002) 2027–2038. [DOI] [PMID: 12481086]
2.	Cahoon, E.B. and Kinney, A.J. Dimorphecolic acid is synthesized by the coordinate activities of two divergent Δ¹²-oleic acid desaturases. J. Biol. Chem. 279 (2004) 12495–12502. [DOI] [PMID: 14718523]

[EC 1.14.19.34 created 2015]

2.4.1.261

Relevance: 56.5%

Accepted name:

dolichyl-P-Man:Man₈GlcNAc₂-PP-dolichol α-1,2-mannosyltransferase

Reaction:

dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of dolichyltetradecasaccharide biosynthesis, click here

Other name(s):

ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man₈GlcNAc₂-PP-Dol α-1,2-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase

Systematic name:

dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)

Comments:

The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc₃Man₉GlcNAc₂ core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man₅GlcNAc₂-PP-Dol to Man₉Glc-NAc₂-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues: the addition of α-1,2-mannose to Man₆GlcNAc₂-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man₈GlcNAc₂-PP-Dol (EC 2.4.1.261).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [PMID: 19451548]
2.	Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]

[EC 2.4.1.261 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.261, modified 2012]

2.4.99.12

Relevance: 56.2%

Accepted name:

lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase

Reaction:

CMP-β-Kdo + a lipid IV_A + CMP-β-Kdo = CMP + an α-Kdo-(2→6)-[lipid IV_A]

For diagram of Kdo₄-Lipid IV_A biosynthesis, click here

Glossary:

CMP-β-Kdo = CMP-3-deoxy-β-D-manno-octulosonate = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate
a lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s):

waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; lipid IV_A KDO transferase; CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase; KDO transferase

Systematic name:

CMP-3-deoxy-β-D-manno-oct-2-ulosonate:[lipid IV_A] 3-deoxy-D-manno-oct-2-ulosonate transferase (configuration-inverting)

Comments:

The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IV_A (cf. EC 2.4.99.13 [(Kdo)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus and Haemophilus influenzae catalyse the transfer of a single 3-deoxy-D-manno-oct-2-ulosonate residue from CMP-3-deoxy-D-manno-oct-2-ulosonate to lipid IV_A [2-4]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Belunis, C.J. and Raetz, C.R. Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli. J. Biol. Chem. 267 (1992) 9988–9997. [PMID: 1577828]
2.	Isobe, T., White, K.A., Allen, A.G., Peacock, M., Raetz, C.R. and Maskell, D.J. Bordetella pertussis waaA encodes a monofunctional 2-keto-3-deoxy-D-manno-octulosonic acid transferase that can complement an Escherichia coli waaA mutation. J. Bacteriol. 181 (1999) 2648–2651. [DOI] [PMID: 10198035]
3.	Mamat, U., Schmidt, H., Munoz, E., Lindner, B., Fukase, K., Hanuszkiewicz, A., Wu, J., Meredith, T.C., Woodard, R.W., Hilgenfeld, R., Mesters, J.R. and Holst, O. WaaA of the hyperthermophilic bacterium Aquifex aeolicus is a monofunctional 3-deoxy-D-manno-oct-2-ulosonic acid transferase involved in lipopolysaccharide biosynthesis. J. Biol. Chem. 284 (2009) 22248–22262. [DOI] [PMID: 19546212]
4.	White, K.A., Kaltashov, I.A., Cotter, R.J. and Raetz, C.R. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae. J. Biol. Chem. 272 (1997) 16555–16563. [DOI] [PMID: 9195966]
5.	Lobau, S., Mamat, U., Brabetz, W. and Brade, H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-α-D-manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol. Microbiol. 18 (1995) 391–399. [DOI] [PMID: 8748024]

[EC 2.4.99.12 created 2010, modified 2011]

2.4.1.325

Relevance: 56.1%

Accepted name:

TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase

Reaction:

dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Glossary:

dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s):

TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)

Systematic name:

dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase

Comments:

Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509–6516. [DOI] [PMID: 11673418]

[EC 2.4.1.325 created 2014]

2.4.1.232

Relevance: 55.2%

Accepted name:

initiation-specific α-1,6-mannosyltransferase

Reaction:

Transfers an α-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an α-(1→6)-D-mannosyl-D-mannose linkage

Other name(s):

α-1,6-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase; GDP-mannose:glycolipid 1,6-α-D-mannosyltransferase; glycolipid 6-α-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase

Systematic name:

GDP-mannose:oligosaccharide 6-α-D-mannosyltransferase

Comments:

Requires Mn²⁺. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man₈GlcNAc and Man₉GlcNAc are equally good substrates.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 346003-17-6

References:

1.	Romero, P.A. and Herscovics, A. Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of α-1,6-mannosyltransferase which initiates outer chain formation. J. Biol. Chem. 264 (1989) 1946–1950. [PMID: 2644248]
2.	Reason, A.J., Dell, A., Romero, P.A. and Herscovics, A. Specificity of the mannosyltransferase which initiates outer chain formation in Saccharomyces cerevisiae. Glycobiology 1 (1991) 387–391. [DOI] [PMID: 1820199]
3.	Nakanishi-Shindo, Y., Nakayama, K., Tanaka, A., Toda, Y. and Jigami, Y. Structure of the N-linked oligosaccharides that show the complete loss of α-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 26338–26345. [PMID: 8253757]
4.	Yamamoto, K., Okamoto, M., Yoko-o, T. and Jigami, Y. Salt stress induces the expression of the Schizosaccharomyces pombe och1+, which encodes an initiation-specific α-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins. Biosci. Biotechnol. Biochem. 67 (2003) 927–929. [DOI] [PMID: 12784644]
5.	Cui, Z., Horecka, J. and Jigami, Y. Cdc4 is involved in the transcriptional control of OCH1, a gene encoding α-1,6-mannosyltransferase in Saccharomyces cerevisiae. Yeast 19 (2002) 69–77. [DOI] [PMID: 11754484]
6.	Tsukahara, K., Watanabe, T., Yoko-o, T. and Chigami, Y. Schizosaccharomyces pombe och1+ gene encoding α-1,6-mannosyltransferase and use of och1+ gene knockout fission yeast for production of glycoproteins with reduced glycosylation. Jpn. Kokai Tokkyo Koho Koho (2001) 11.
7.	Nakayama, K., Nakanishi-Shindo, Y., Tanaka, A., Haga-Toda, Y. and Jigami, Y. Substrate specificity of α-1,6-mannosyltransferase that initiates N-linked mannose outer chain elongation in Saccharomyces cerevisiae. FEBS Lett. 412 (1997) 547–550. [DOI] [PMID: 9276464]
8.	Suzuki, A., Shibata, N., Suzuki, M., Saitoh, F., Takata, Y., Oshie, A., Oyamada, H., Kobayashi, H., Suzuki, S. and Okawa, Y. Characterization of α-1,6-mannosyltransferase responsible for the synthesis of branched side chains in Candida albicans mannan. Eur. J. Biochem. 240 (1996) 37–44. [DOI] [PMID: 8797833]
9.	Yip, C.L., Welch, S.K., Klebl, F., Gilbert, T., Seidel, P., Grant, F., O'Hara, P.J. and MacKay, V.L. Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins. Proc. Natl. Acad. Sci. USA 91 (1994) 2723–2727. [DOI] [PMID: 8146181]

[EC 2.4.1.232 created 2004]

2.3.1.279

Relevance: 55.2%

Accepted name:

long-chain-acyl-CoA—trehalose acyltransferase

Reaction:

a long-chain-fatty acyl-CoA + α,α-trehalose = a 2-(long-chain-fatty acyl)-trehalose + CoA

Glossary:

polyacyltrehalose = PAT = a 2-(long-chain-fatty acyl)-2′,3,4′,6-tetramycolipenoyl-trehalose
a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA

Other name(s):

papA3 (gene name)

Systematic name:

long-chain-fatty acyl-CoA:α,α-trehalose 2-acyltransferase

Comments:

The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278, mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009) 12745–12751. [PMID: 19276083]

[EC 2.3.1.279 created 2018]

2.4.1.371

Relevance: 55.2%

Accepted name:

polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosylpolymerase

Reaction:

(1) 2 GDP-α-D-mannose + [α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]_n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = 2 GDP + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]_n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
(2) 2 GDP-α-D-mannose + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]_n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = 2 GDP + [α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]_n+1-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WbdA

Systematic name:

GDP-α-D-mannose:α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]_n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosyltransferase (configuration-retaining)

Comments:

The enzyme is involved in the biosynthesis of polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. The enzymes consists of two domains that are responsible for the 1→2 and 1→3 linkages, respectively.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078–35091. [DOI] [PMID: 22875852]
2.	Greenfield, L.K., Richards, M.R., Vinogradov, E., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens. J. Biol. Chem. 287 (2012) 38135–38149. [PMID: 22989876]
3.	Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075–1085. [DOI] [PMID: 25422321]

[EC 2.4.1.371 created 2019]