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2.3.1.251

Relevance: 100%

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]

2.7.1.130

Relevance: 98.7%

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]

2.4.1.154

Deleted entry:

globotriosylceramide β-1,6-N-acetylgalactosaminyl-transferase. The enzyme is identical to EC 2.4.1.79, globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase. The reference cited referred to a 1→3 linkage and not to a 1→6 linkage, as indicated in the enzyme entry

[EC 2.4.1.154 created 1986, deleted 2006]

5.3.1.31

Relevance: 98.1%

Accepted name:

sulfoquinovose isomerase

Reaction:

(1) β-sulfoquinovose = 6-deoxy-6-sulfo-D-fructose
(2) β-sulfoquinovose = 6-sulfo-D-rhamnose

For diagram of sulphoglycolysis of sulfoquinovose, click here

Glossary:

sulfoquinovose = 6-deoxy-6-sulfo-D-glucopyranose

Other name(s):

yihS (gene name)

Systematic name:

6-deoxy-6-sulfo-β-D-glucopyranose aldose-ketose-isomerase

Comments:

The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Denger, K., Weiss, M., Felux, A.K., Schneider, A., Mayer, C., Spiteller, D., Huhn, T., Cook, A.M. and Schleheck, D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature 507 (2014) 114–117. [DOI] [PMID: 24463506]
2.	Sharma, M., Abayakoon, P., Epa, R., Jin, Y., Lingford, J.P., Shimada, T., Nakano, M., Mui, J.W., Ishihama, A., Goddard-Borger, E.D., Davies, G.J. and Williams, S.J. Molecular basis of sulfosugar selectivity in sulfoglycolysis. ACS Cent. Sci. 7 (2021) 476–487. [DOI] [PMID: 33791429]

[EC 5.3.1.31 created 2014, modified 2022]

2.7.8.30

Transferred entry:

undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase. Now EC 2.4.2.53, undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

[EC 2.7.8.30 created 2010, modified 2011, deleted 2013]

3.2.1.124

Relevance: 97.1%

Accepted name:

3-deoxy-2-octulosonidase

Reaction:

Endohydrolysis of the β-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides

Other name(s):

2-keto-3-deoxyoctonate hydrolase; octulosylono hydrolase; octulofuranosylono hydrolase; octulopyranosylonohydrolase

Systematic name:

capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase

Comments:

The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 103171-48-8

References:

1.	Altmann, F., Kwiatkowski, B., Stirm, S., März, L. and Unger, F.M. A bacteriophage-associated glycanase cleaving β-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO). Biochem. Biophys. Res. Commun. 136 (1986) 329–335. [DOI] [PMID: 3707579]

[EC 3.2.1.124 created 1989]

2.4.1.317

Relevance: 96.7%

Accepted name:

O-mycaminosyltylonolide 6-deoxyallosyltransferase

Reaction:

5-O-β-D-mycaminosyltylonolide + dTDP-6-deoxy-α-D-allose = dTDP + demethyllactenocin

For diagram of tylosin biosynthesis, click here

Glossary:

mycaminose = 3,6-dideoxy-3-dimethylamino-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxooxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-β-D-allopyranoside

Other name(s):

tylN (gene name)

Systematic name:

dTDP-6-deoxy-α-D-allose:5-O-β-D-mycaminosyltylonolide 23-O-6-deoxy-α-D-allosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Wilson, V.T. and Cundliffe, E. Characterization and targeted disruption of a glycosyltransferase gene in the tylosin producer, Streptomyces fradiae. Gene 214 (1998) 95–100. [DOI] [PMID: 9651492]

[EC 2.4.1.317 created 2014]

2.7.1.166

Relevance: 95.9%

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]

1.14.15.8

Relevance: 95.6%

Accepted name:

steroid 15β-monooxygenase

Reaction:

progesterone + 2 reduced [2Fe-2S] ferredoxin + O₂ = 15β-hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H₂O

Other name(s):

cytochrome P-450_meg; cytochrome P450_meg; steroid 15β-hydroxylase; CYP106A2; BmCYP106A2

Systematic name:

progesterone,reduced-ferredoxin:oxygen oxidoreductase (15β-hydroxylating)

Comments:

The enzyme from the bacterium Bacillus megaterium hydroxylates a variety of 3-oxo-Δ⁴-steroids in position 15β. Ring A-reduced, aromatic, and 3β-hydroxy-Δ⁴-steroids do not serve as substrates [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264–5271. [PMID: 109432]
2.	Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J. Biol. Chem. 251 (1976) 2831–2838. [PMID: 177422]
3.	Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry. Biochem. Biophys. Res. Commun. 319 (2004) 677–682. [DOI] [PMID: 15178459]
4.	Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368. Biochim. Biophys. Acta 1794 (2009) 1635–1642. [DOI] [PMID: 19635596]
5.	Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. ChemBioChem 9 (2008) 1439–1449. [DOI] [PMID: 18481342]

[EC 1.14.15.8 created 2010]

2.4.1.244

Relevance: 95%

Accepted name:

N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-glucosaminyl group = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group

Glossary:

N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosamine = N,N′-diacetyllactosediamine

Other name(s):

β1,4-N-acetylgalactosaminyltransferase III; β4GalNAc-T3; β1,4-N-acetylgalactosaminyltransferase IV; β4GalNAc-T4; UDP-N-acetyl-D-galactosamine:N-acetyl-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase

Systematic name:

UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase

Comments:

The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-β-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Sato, T., Gotoh, M., Kiyohara, K., Kameyama, A., Kubota, T., Kikuchi, N., Ishizuka, Y., Iwasaki, H., Togayachi, A., Kudo, T., Ohkura, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of a novel human β1,4-N-acetylgalactosaminyltransferase, β4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, GalNAc β1-4GlcNAc. J. Biol. Chem. 278 (2003) 47534–47544. [DOI] [PMID: 12966086]

Gotoh, M., Sato, T., Kiyohara, K., Kameyama, A., Kikuchi, N., Kwon, Y.D., Ishizuka, Y., Iwai, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of β1,4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine. FEBS Lett. 562 (2004) 134–140. [DOI] [PMID: 15044014]

[EC 2.4.1.244 created 2006]

5.3.1.30

Relevance: 93.4%

Accepted name:

5-deoxy-glucuronate isomerase

Reaction:

5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate

For diagram of inositol catabolism, click here

Glossary:

5-dehydro-2-deoxy-D-gluconate = 2-deoxy-D-threo-hex-5-ulosonic acid
5-deoxy-D-glucuronate = 5-deoxy-D-xylo-hexuronic acid

Other name(s):

5DG isomerase; IolB

Systematic name:

5-deoxy-D-glucuronate aldose-ketose-isomerase

Comments:

The enzyme, found in the bacterium Bacillus subtilis, is part of a myo-inositol degradation pathway leading to acetyl-CoA.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yoshida, K., Yamaguchi, M., Morinaga, T., Kinehara, M., Ikeuchi, M., Ashida, H. and Fujita, Y. myo-Inositol catabolism in Bacillus subtilis. J. Biol. Chem. 283 (2008) 10415–10424. [DOI] [PMID: 18310071]

[EC 5.3.1.30 created 2014]

1.1.1.434

Relevance: 91.8%

Accepted name:

2-dehydro-3-deoxy-L-fuconate 4-dehydrogenase

Reaction:

2-dehydro-3-deoxy-L-fuconate + NAD⁺ = 2,4-didehydro-3-deoxy-L-fuconate + NADH + H⁺

For diagram of L-fucose catabolism, click here

Glossary:

2-dehydro-3-deoxy-L-fuconate = (4S,5S)-4,5-dihydroxy-2-oxohexanoate
2,4-didehydro-3-deoxy-L-fuconate = (5S)-5-hydroxy-2,4-dioxohexanoate

Systematic name:

2-dehydro-3-deoxy-L-fuconate:NAD⁺ 4-oxidoreductase

Comments:

The enzyme, originally described from the bacterium Xanthomonas campestris pv. campestris, participates in an L-fucose degradation pathway. It can also act on 2-dehydro-3-deoxy-L-galactonate and 2-dehydro-3-deoxy-D-pentonate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yew, W.S., Fedorov, A.A., Fedorov, E.V., Rakus, J.F., Pierce, R.W., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris. Biochemistry 45 (2006) 14582–14597. [DOI] [PMID: 17144652]
2.	Watanabe, S., Fukumori, F., Nishiwaki, H., Sakurai, Y., Tajima, K. and Watanabe, Y. Novel non-phosphorylative pathway of pentose metabolism from bacteria. Sci. Rep. 9:155 (2019). [DOI] [PMID: 30655589]

[EC 1.1.1.434 created 2022]

3.2.1.14

Relevance: 91.7%

Accepted name:

chitinase

Reaction:

Random endo-hydrolysis of N-acetyl-β-D-glucosaminide (1→4)-β-linkages in chitin and chitodextrins

Glossary:

chitin = [(1→4)-β-D-GlcpNAc]_n = (1→4)-2-acetamido-2-deoxy-β-D-glucan

Other name(s):

ChiC; chitodextrinase (ambiguous); 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase

Systematic name:

(1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase

Comments:

The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-06-3

References:

1.	Zechmeister, L. and Tóth, G. Chromatographic adsorption of the enzymes of emulsin which act on chitins. Enzymologia 7 (1939) 165–169.
2.	Tracey, M.V. Chitinase in some basidiomycetes. Biochem. J. 61 (1955) 579–586. [PMID: 13276340]
3.	Fischer, E.H. and Stein, E.A. Cleavage of O- and S-glycosidic bonds (survey). In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 301–312.
4.	Connell, T.D., Metzger, D.J., Lynch, J. and Folster, J.P. Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae. J. Bacteriol. 180 (1998) 5591–5600. [PMID: 9791107]
5.	Francetic, O., Badaut, C., Rimsky, S. and Pugsley, A.P. The ChiA (YheB) protein of Escherichia coli K-12 is an endochitinase whose gene is negatively controlled by the nucleoid-structuring protein H-NS. Mol. Microbiol. 35 (2000) 1506–1517. [DOI] [PMID: 10760150]
6.	Zverlov, V.V., Fuchs, K.P. and Schwarz, W.H. Chi18A, the endochitinase in the cellulosome of the thermophilic, cellulolytic bacterium Clostridium thermocellum. Appl. Environ. Microbiol. 68 (2002) 3176–3179. [DOI] [PMID: 12039789]
7.	Rottloff, S., Stieber, R., Maischak, H., Turini, F.G., Heubl, G. and Mithofer, A. Functional characterization of a class III acid endochitinase from the traps of the carnivorous pitcher plant genus, Nepenthes. J. Exp. Bot. 62 (2011) 4639–4647. [DOI] [PMID: 21633084]

[EC 3.2.1.14 created 1961, modified 2017]

2.4.1.331

Relevance: 90.9%

Accepted name:

8-demethyltetracenomycin C L-rhamnosyltransferase

Reaction:

dTDP-β-L-rhamnose + 8-demethyltetracenomycin C = dTDP + 8-demethyl-8-α-L-rhamnosyltetracenomycin C

For diagram of elloramycin biosynthesis, click here

Glossary:

dTDP-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose

Other name(s):

elmGT

Systematic name:

dTDP-β-L-rhamnose:8-demethyltetracenomycin C 3-α-L-rhamnosyltransferase

Comments:

Isolated from Streptomyces olivaceus Tü2353. Involved in elloramycin biosynthesis. In vitro it can also utilize other 6-deoxy D- or L-hexoses.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Blanco, G., Patallo, E.P., Brana, A.F., Trefzer, A., Bechthold, A., Rohr, J., Mendez, C. and Salas, J.A. Identification of a sugar flexible glycosyltransferase from Streptomyces olivaceus, the producer of the antitumor polyketide elloramycin. Chem. Biol. 8 (2001) 253–263. [DOI] [PMID: 11306350]

[EC 2.4.1.331 created 2014]

3.2.1.92

Relevance: 90.9%

Accepted name:

peptidoglycan β-N-acetylmuramidase

Reaction:

Hydrolysis of terminal, non-reducing N-acetylmuramic residues

Other name(s):

exo-β-N-acetylmuramidase; exo-β-acetylmuramidase; β-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-D-glucoside acetamidodeoxyglucohydrolase

Systematic name:

peptidoglycan β-N-acetylmuramoylexohydrolase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52219-03-1

References:

1.	Del Rio, L.A. and Berkeley, R.C.W. Exo-β-N-acetylmuramidase - a novel hexosaminidase. Production by Bacillus subtilis B, purification and characterization. Eur. J. Biochem. 65 (1976) 3–12. [DOI] [PMID: 6281]

[EC 3.2.1.92 created 1976]

3.2.1.190

Relevance: 90.5%

Accepted name:

dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming)

Reaction:

3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin + 2 H₂O = 2 L-rhamnopyranose + diosgenin 3-O-β-D-glucopyranoside

For diagram of diosgenin catabolism, click here

Glossary:

3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin = (3β,25R)-spirost-5-en-3-yl 6-deoxy-α-L-mannopyranosyl-(1→2)-[6-deoxy-α-L-mannopyranosyl-(1→4)]-β-D-glucopyranoside = dioscin
diosgenin = (3β,25R)-spirost-5-en-3-ol

Other name(s):

dioscin-α-L-rhamnosidase

Systematic name:

3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin (3-O-β-D-Glc-diosgenin-forming)

Comments:

The enzyme is involved in the hydrolysis of the steroid saponin dioscin by the digestive system of Sus scrofa (pig). cf. EC 3.2.1.189, dioscin glycosidase (diosgenin-forming).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Qian, S., Yu, H., Zhang, C., Lu, M., Wang, H. and Jin, F. Purification and characterization of dioscin-α-L-rhamnosidase from pig liver. Chem Pharm Bull (Tokyo) 53 (2005) 911–914. [PMID: 16079518]

[EC 3.2.1.190 created 2013]

5.3.3.22

Relevance: 90.3%

Accepted name:

lutein isomerase

Reaction:

lutein = meso-zeaxanthin

For diagram of lutein biosynthesis, click here

Glossary:

lutein = (3R,3′R)-dihydroxy-α-carotene
meso-zeaxanthin = (3R,3′S)-β,β-carotene-3,3′-diol

Other name(s):

RPE65 (gene name); meso-zeaxanthin isomerase

Systematic name:

lutein Δ⁴-Δ⁵-isomerase

Comments:

The enzyme is found in the retinal pigment epithelium (RPE) of vertebrates. It also has the activity of EC 3.1.1.64, retinoid isomerohydrolase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Shyam, R., Gorusupudi, A., Nelson, K., Horvath, M.P. and Bernstein, P.S. RPE65 has an additional function as the lutein to meso-zeaxanthin isomerase in the vertebrate eye. Proc. Natl. Acad. Sci. USA 114 (2017) 10882–10887. [DOI] [PMID: 28874556]

[EC 5.3.3.22 created 2018]

5.1.3.13

Relevance: 90.2%

Accepted name:

dTDP-4-dehydrorhamnose 3,5-epimerase

Reaction:

dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-4-dehydro-β-L-rhamnose

For diagram of dtdp-6-deoxyhexose biosynthesis, click here and for diagram of 6-deoxyhexose biosynthesis, click here

Glossary:

dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose

Other name(s):

dTDP-L-rhamnose synthetase; dTDP-L-rhamnose synthase; thymidine diphospho-4-ketorhamnose 3,5-epimerase; TDP-4-ketorhamnose 3,5-epimerase; dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase; TDP-4-keto-L-rhamnose-3,5-epimerase

Systematic name:

dTDP-4-dehydro-6-deoxy-α-D-glucose 3,5-epimerase

Comments:

The enzyme occurs in a complex with EC 1.1.1.133 dTDP-4-dehydrorhamnose reductase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-39-1

References:

1.	Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041–6049. [PMID: 4199258]
2.	Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475–1478. [PMID: 4384782]

[EC 5.1.3.13 created 1972]

2.3.1.243

Relevance: 88.9%

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]

2.4.1.146

Relevance: 88.3%

Accepted name:

β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] = UDP + 3-O-{N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]

Glossary:

core 2 = 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]

Other name(s):

O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase (elongating); elongation 3β-GalNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to β-D-galactose of β-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→3)-[N-acetyl-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase; B3GNT3 (gene name)

Systematic name:

UDP-N-acetyl-α-D-glucosamine:3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] 3-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)

Comments:

The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 2 structure of O-glycans.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87927-99-9

References:

1.	Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
2.	Shiraishi, N., Natsume, A., Togayachi, A., Endo, T., Akashima, T., Yamada, Y., Imai, N., Nakagawa, S., Koizumi, S., Sekine, S., Narimatsu, H. and Sasaki, K. Identification and characterization of three novel β 1,3-N-acetylglucosaminyltransferases structurally related to the β 1,3-galactosyltransferase family. J. Biol. Chem. 276 (2001) 3498–3507. [PMID: 11042166]

[EC 2.4.1.146 created 1984, modified 2018]

2.4.1.212

Relevance: 88.1%

Accepted name:

hyaluronan synthase

Reaction:

(1) UDP-N-acetyl-α-D-glucosamine + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] = UDP + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan]
(2) UDP-α-D-glucuronate + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan] = UDP + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan]

For diagram of reaction, click here

Glossary:

GlcA = glucuronic acid

Other name(s):

spHAS; seHAS; Alternating UDP-α-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase

Systematic name:

Alternating UDP-N-acetyl-α-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase (configuration-inverting)

Comments:

The enzyme from Streptococcus Group A and Group C requires Mg²⁺. The enzyme adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc [3]. The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. Similar enzymes have been found in a variety of organisms.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39346-43-5

References:

1.	DeAngelis, P.L., Papaconstantinou, J. and Weigel, P.H. Molecular cloning, identification and sequence of the hyaluronan synthase gene from Group A Streptococcus pyogenes. J. Biol. Chem. 268 (1993) 19181–19184. [PMID: 8366070]
2.	Jing, W. and DeAngelis, P.L. Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. Glycobiology 10 (2000) 883–889. [DOI] [PMID: 10988250]
3.	DeAngelis, P.L. Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase. J. Biol. Chem. 274 (1999) 26557–26562. [DOI] [PMID: 10473619]
4.	Tlapak-Simmons, V.L., Baron, C.A. and Weigel, P.H. Characterization of the purified hyaluronan synthase from Streptococcus equisimilis. Biochemistry 43 (2004) 9234–9242. [DOI] [PMID: 15248781]

[EC 2.4.1.212 created 2001, modified 2007]

3.2.1.189

Relevance: 87.2%

Accepted name:

dioscin glycosidase (diosgenin-forming)

Reaction:

3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin + 3 H₂O = D-glucose + 2 L-rhamnose + diosgenin

For diagram of diosgenin catabolism, click here

Glossary:

Other name(s):

dioscin glycosidase (aglycone-forming)

Systematic name:

3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin hydrolase (diosgenin-forming)

Comments:

The enzyme is involved in degradation of the steroid saponin dioscin by some fungi of the Absidia genus. The enzyme can also hydrolyse 3-O-[α-L-Ara-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin into diosgenin and free sugars as the final products. cf. EC 3.2.1.190, dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Fu, Y., Yu, H., Tang, S.H., Hu, X., Wang, Y., Liu, B., Yu, C. and Jin, F. New dioscin-glycosidase hydrolyzing multi-glycosides of dioscin from Absidia strain. J. Microbiol. Biotechnol. 20 (2010) 1011–1017. [PMID: 20622501]

[EC 3.2.1.189 created 2013]

2.7.1.229

Relevance: 87.1%

Accepted name:

deoxyribokinase

Reaction:

ATP + 2-deoxy-D-ribose = ADP + 2-deoxy-D-ribose 5-phosphate

Other name(s):

deoK (gene name)

Systematic name:

ATP:2-deoxy-D-ribose 5-phosphotransferase

Comments:

The enzyme, characterized from bacteria, is much more active with 2-deoxy-D-ribose than with D-ribose. cf. EC 2.7.1.15, ribokinase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Domagk, G.F. and Horecker, B.L. Pentose fermentation by Lactobacillus plantarum. V. Fermentation of 2-deoxy-D-ribose. J. Biol. Chem. 233 (1958) 283–286. [PMID: 13563487]
2.	Ginsburg, A. A deoxyribokinase from Lactobacillus plantarum. J. Biol. Chem. 234 (1959) 481–487. [PMID: 13641245]
3.	Hoffee, P.A. 2-deoxyribose gene-enzyme complex in Salmonella typhimurium. I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants. J. Bacteriol. 95 (1968) 449–457. [PMID: 4867740]
4.	Tourneux, L., Bucurenci, N., Saveanu, C., Kaminski, P.A., Bouzon, M., Pistotnik, E., Namane, A., Marliere, P., Barzu, O., Li De La Sierra, I., Neuhard, J. and Gilles, A.M. Genetic and biochemical characterization of Salmonella enterica serovar Typhi deoxyribokinase. J. Bacteriol. 182 (2000) 869–873. [PMID: 10648508]

[EC 2.7.1.229 created 2019]

3.2.1.112

Relevance: 86.2%

Accepted name:

2-deoxyglucosidase

Reaction:

a 2-deoxy-α-D-glucoside + H₂O = 2-deoxy-D-glucose + an alcohol

Other name(s):

2-deoxy-α-glucosidase; 2-deoxy-α-D-glucosidase

Systematic name:

2-deoxy-α-D-glucoside deoxyglucohydrolase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 92480-05-2

References:

1.	Canellakis, Z.N., Bondy, P.K., May, J.A., Jr., Myers-Robfogel, M.K. and Sartorelli, A.C. Identification of a glycosidase activity with apparent specificity for 2-deoxy-D-glucose in glycosidic linkage. Eur. J. Biochem. 143 (1984) 159–163. [DOI] [PMID: 6468386]

[EC 3.2.1.112 created 1986]

1.3.1.114

Relevance: 86%

Accepted name:

3-dehydro-bile acid Δ^4,6-reductase

Reaction:

(1) 3-oxocholan-24-oyl-CoA + NAD⁺ = 3-oxochol-4-en-24-oyl-CoA + NADH + H⁺
(2) 3-oxochol-4-en-24-oyl-CoA + NAD⁺ = 3-oxochol-4,6-dien-24-oyl-CoA + NADH + H⁺
(3) 12α-hydroxy-3-oxocholan-24-oyl-CoA + NAD⁺ = 12α-hydroxy-3-oxochol-4-en-24-oyl-CoA + NADH + H⁺
(4) 12α-hydroxy-3-oxochol-4-en-24-oyl-CoA + NAD⁺ = 12α-hydroxy-3-oxochol-4,6-dien-24-oyl-CoA + NADH + H⁺

Other name(s):

baiN (gene name)

Systematic name:

3-oxocholan-24-oyl-CoA Δ^4,6-oxidoreductase

Comments:

Contains flavin. The enzyme, characterized from the bacterium Clostridium scindens, participates in the bile acid 7α-dehydroxylation pathway. The enzyme catalyses two subsequent reductions of the double bonds within the bile acid A/B rings, following 7α-dehydration.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Harris, S.C., Devendran, S., Alves, J.MP., Mythen, S.M., Hylemon, P.B. and Ridlon, J.M. Identification of a gene encoding a flavoprotein involved in bile acid metabolism by the human gut bacterium Clostridium scindens ATCC 35704. Biochim. Biophys. Acta 1863 (2018) 276–283. [DOI] [PMID: 29217478]

[EC 1.3.1.114 created 2018]

4.2.1.141

Relevance: 86%

Accepted name:

2-dehydro-3-deoxy-D-arabinonate dehydratase

Reaction:

2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H₂O

For diagram of D-arabinose catabolism, click here

Glossary:

2-dehydro-3-deoxy-D-arabinonate = 2-dehydro-3-deoxy-D-xylonate = 3-deoxy-L-glycero-pent-2-ulonate

Systematic name:

2-dehydro-3-deoxy-D-arabinonate hydro-lyase (2,5-dioxopentanoate-forming)

Comments:

The enzyme participates in pentose oxidation pathways that convert pentose sugars to the tricarboxylic acid cycle intermediate 2-oxoglutarate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Brouns, S.J., Walther, J., Snijders, A.P., van de Werken, H.J., Willemen, H.L., Worm, P., de Vos, M.G., Andersson, A., Lundgren, M., Mazon, H.F., van den Heuvel, R.H., Nilsson, P., Salmon, L., de Vos, W.M., Wright, P.C., Bernander, R. and van der Oost, J. Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment. J. Biol. Chem. 281 (2006) 27378–27388. [DOI] [PMID: 16849334]
2.	Brouns, S.J., Barends, T.R., Worm, P., Akerboom, J., Turnbull, A.P., Salmon, L. and van der Oost, J. Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features of the FAH superfamily. J. Mol. Biol. 379 (2008) 357–371. [DOI] [PMID: 18448118]
3.	Johnsen, U., Dambeck, M., Zaiss, H., Fuhrer, T., Soppa, J., Sauer, U. and Schonheit, P. D-Xylose degradation pathway in the halophilic archaeon Haloferax volcanii. J. Biol. Chem. 284 (2009) 27290–27303. [DOI] [PMID: 19584053]

[EC 4.2.1.141 created 2013]

2.7.1.178

Relevance: 86%

Accepted name:

2-dehydro-3-deoxyglucono/galactono-kinase

Reaction:

(1) ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
(2) ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate

For diagram of the Entner-Doudoroff pathway, click here

Other name(s):

KDG kinase (ambiguous); KDGK (ambiguous); 2-keto-3-deoxy-D-gluconate kinase (ambiguous)

Systematic name:

ATP:2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase

Comments:

The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency. cf. EC 2.7.1.45, 2-dehydro-3-deoxygluconokinase and EC 2.7.1.58, 2-dehydro-3-deoxygalactonokinase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Lamble, H.J., Theodossis, A., Milburn, C.C., Taylor, G.L., Bull, S.D., Hough, D.W. and Danson, M.J. Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus. FEBS Lett. 579 (2005) 6865–6869. [DOI] [PMID: 16330030]
2.	Potter, J.A., Kerou, M., Lamble, H.J., Bull, S.D., Hough, D.W., Danson, M.J. and Taylor, G.L. The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase. Acta Crystallogr. D Biol. Crystallogr. 64 (2008) 1283–1287. [DOI] [PMID: 19018105]
3.	Kim, S. and Lee, S.B. Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway. Biosci. Biotechnol. Biochem. 70 (2006) 1308–1316. [DOI] [PMID: 16794308]

[EC 2.7.1.178 created 2013]

2.7.8.42

Relevance: 86%

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]

5.3.1.17

Relevance: 85.7%

Accepted name:

5-dehydro-4-deoxy-D-glucuronate isomerase

Reaction:

5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate

Glossary:

5-dehydro-4-deoxy-D-glucuronate = (4S,5R)-4,5-dihydroxy-2,6-dioxohexanoate
3-deoxy-D-glycero-2,5-hexodiulosonate = (4S)-4,6-dihydroxy-2,5-dioxohexanoate

Other name(s):

4-deoxy-L-threo-5-hexulose uronate isomerase; 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase; kduI (gene name)

Systematic name:

5-dehydro-4-deoxy-D-glucuronate aldose-ketose-isomerase

Comments:

The enzyme is involved in the degradation of polygalacturonate, a later stage in the degradation of pectin by many microorganisms.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-44-8

References:

1.	Preiss, J. 4-Deoxy-L-threo-5-hexosulose uronic acid isomerase. Methods Enzymol. 9 (1966) 602–604.
2.	Condemine, G. and Robert-Baudouy, J. Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation. Mol. Microbiol. 5 (1991) 2191–2202. [DOI] [PMID: 1766386]
3.	Dunten, P., Jaffe, H. and Aksamit, R.R. Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 678–680. [PMID: 9761873]
4.	Crowther, R.L. and Georgiadis, M.M. The crystal structure of 5-keto-4-deoxyuronate isomerase from Escherichia coli. Proteins 61 (2005) 680–684. [DOI] [PMID: 16152643]

[EC 5.3.1.17 created 1972, modified 2012]

2.7.7.38

Relevance: 85.4%

Accepted name:

3-deoxy-manno-octulosonate cytidylyltransferase

Reaction:

CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate

Other name(s):

CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase; 2-keto-3-deoxyoctonate cytidylyltransferase; 3-Deoxy-D-manno-octulosonate cytidylyltransferase; CMP-3-deoxy-D-manno-octulosonate synthetase; CMP-KDO synthetase; CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase; cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase

Systematic name:

CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-28-7

References:

1.	Ghalambor, M.A. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-D-manno-octulosonate synthetase. J. Biol. Chem. 241 (1966) 3216–3221. [PMID: 5330266]

[EC 2.7.7.38 created 1972]

4.1.2.18

Relevance: 84.7%

Accepted name:

2-dehydro-3-deoxy-L-pentonate aldolase

Reaction:

2-dehydro-3-deoxy-L-pentonate = pyruvate + glycolaldehyde

For diagram of L-arabinose catabolism, click here

Other name(s):

2-keto-3-deoxy-L-pentonate aldolase; 2-keto-3-deoxy-L-arabonate aldolase; 2-keto-3-deoxy-D-xylonate aldolase; 3-deoxy-D-pentulosonic acid aldolase; 2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase

Systematic name:

2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase (pyruvate-forming)

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9076-49-7

References:

1.	Dahms, A.S. and Anderson, R.L. 2-Keto-3-deoxy-L-arabonate aldolase and its role in a new pathway of L-arabinose degradation. Biochem. Biophys. Res. Commun. 36 (1969) 809–814. [DOI] [PMID: 5808295]

[EC 4.1.2.18 created 1972, modified 1976]

4.1.2.53

Relevance: 84.4%

Accepted name:

2-keto-3-deoxy-L-rhamnonate aldolase

Reaction:

2-dehydro-3-deoxy-L-rhamnonate = pyruvate + (S)-lactaldehyde

For diagram of L-Rhamnose metabolism, click here

Glossary:

2-dehydro-3-deoxy-L-rhamnonate = 3,6-dideoxy-L-erythro-hex-2-ulosonate

Other name(s):

KDR aldolase; 2-dehydro-3-deoxyrhamnonate aldolase; 2-keto-3-deoxy acid sugar aldolase; YfaU; 2-dehydro-3-deoxy-L-rhamnonate (S)-lactaldehyde lyase (pyruvate-forming); 2-dehydro-3-deoxy-L-rhamnonate (R)-lactaldehyde lyase (pyruvate-forming)

Systematic name:

2-dehydro-3-deoxy-L-rhamnonate (S)-lactaldehyde-lyase (pyruvate-forming)

Comments:

Requires Mg²⁺ for activity. The enzyme can also use 2-oxo-3-deoxy-L-mannonate, 2-oxo-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) as substrates [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Rakus, J.F., Fedorov, A.A., Fedorov, E.V., Glasner, M.E., Hubbard, B.K., Delli, J.D., Babbitt, P.C., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase. Biochemistry 47 (2008) 9944–9954. [DOI] [PMID: 18754693]
2.	Rea, D., Hovington, R., Rakus, J.F., Gerlt, J.A., Fulop, V., Bugg, T.D. and Roper, D.I. Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry 47 (2008) 9955–9965. [DOI] [PMID: 18754683]

[EC 4.1.2.53 created 2013]

1.1.1.145

Relevance: 84.2%

Accepted name:

3β-hydroxy-Δ⁵-steroid dehydrogenase

Reaction:

a 3β-hydroxy-Δ⁵-steroid + NAD⁺ = a 3-oxo-Δ⁵-steroid + NADH + H⁺

For diagram of cholesterol catabolism (rings a, B and c), click here

Other name(s):

progesterone reductase; Δ⁵-3β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene steroid dehydrogenase; 3β-hydroxy steroid dehydrogenase/isomerase; 3β-hydroxy-Δ⁵-C₂₇-steroid dehydrogenase/isomerase; 3β-hydroxy-Δ⁵-C₂₇-steroid oxidoreductase; 3β-hydroxy-5-ene-steroid oxidoreductase; steroid-Δ⁵-3β-ol dehydrogenase; 3β-HSDH; 5-ene-3-β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene-steroid dehydrogenase

Systematic name:

3β-hydroxy-Δ⁵-steroid:NAD⁺ 3-oxidoreductase

Comments:

This activity is found in several bifunctional enzymes that catalyse the oxidative conversion of Δ⁵-3-hydroxy steroids to a Δ⁴-3-oxo configuration. This conversion is carried out in two separate, sequential reactions; in the first reaction, which requires NAD⁺, the enzyme catalyses the dehydrogenation of the 3β-hydroxy steroid to a 3-oxo intermediate. In the second reaction the reduced cosubstrate, which remains attached to the enzyme, activates the isomerization of the Δ⁵ form to a Δ⁴ form (cf. EC 5.3.3.1, steroid Δ-isomerase). Substrates include dehydroepiandrosterone (which is converted into androst-5-ene-3,17-dione), pregnenolone (converted to progesterone) and cholest-5-en-3-one, an intermediate of cholesterol degradation.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-85-3

References:

1.	Cheatum, S.G. and Warren, J.C. Purification and properties of 3-β-hydroxysteroid dehydrogenase and Δ-5-3-ketosteroid isomerase from bovine corpora lutea. Biochim. Biophys. Acta 122 (1966) 1–13. [PMID: 4226148]
2.	Koritz, S.B. The conversion of prepnenolone to progesterone by small particle from rat adrenal. Biochemistry 3 (1964) 1098–1102. [PMID: 14220672]
3.	Neville, A.M., Orr, J.C. and Engel, L.L. Δ⁵-3β-Hydroxy steroid dehydrogenase activities of bovine adrenal cortex. Biochem. J. 107 (1968) 20.

[EC 1.1.1.145 created 1972]

2.4.1.289

Relevance: 84.1%

Accepted name:

N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase

Reaction:

dTDP-6-deoxy-β-L-mannose + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol = dTDP + α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol

For diagram of galactofuranan biosynthesis, click here

Glossary:

dTDP-6-deoxy-β-L-mannose = dTDP-4-β-L-rhamnose

Other name(s):

WbbL

Systematic name:

dTDP-6-deoxy-β-L-mannose:N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-α-L-rhamnosyltransferase

Comments:

Requires Mn²⁺ or Mg²⁺. Isolated from Mycobacterium smegmatis [1] and Mycobacterium tuberculosis [2]. The enzyme catalyses the addition of a rhamnosyl unit to N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol, completing the synthesis of the linkage unit that attaches the arabinogalactan moiety to the peptidoglycan moiety in Mycobacterial cell wall.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Mills, J.A., Motichka, K., Jucker, M., Wu, H.P., Uhlik, B.C., Stern, R.J., Scherman, M.S., Vissa, V.D., Pan, F., Kundu, M., Ma, Y.F. and McNeil, M. Inactivation of the mycobacterial rhamnosyltransferase, which is needed for the formation of the arabinogalactan-peptidoglycan linker, leads to irreversible loss of viability. J. Biol. Chem. 279 (2004) 43540–43546. [DOI] [PMID: 15294902]
2.	Grzegorzewicz, A.E., Ma, Y., Jones, V., Crick, D., Liav, A. and McNeil, M.R. Development of a microtitre plate-based assay for lipid-linked glycosyltransferase products using the mycobacterial cell wall rhamnosyltransferase WbbL. Microbiology 154 (2008) 3724–3730. [DOI] [PMID: 19047740]

[EC 2.4.1.289 created 2012]

2.4.1.79

Relevance: 84%

Accepted name:

globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-galactosamine + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of globotetraosylceramide biosynthesis, click here. For diagram of reaction, click here

Glossary:

α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotriaosylceramide = P^k antigen
N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotetraosylceramide = globoside = P antigen

Other name(s):

uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgalactosamine:globotriaosylceramide β-3-N-acetylgalactosaminyltransferase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase; globoside synthase; gUDP-N-acetyl-D-galactosamine:D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide β-N-acetyl-D-galactosaminyltransferase; β3GalNAc-T1; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3^III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3^III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III³-β-N-acetyl-D-galactosaminyltransferase

Systematic name:

UDP-N-acetyl-α-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III³-β-N-acetyl-D-galactosaminyltransferase

Comments:

Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn²⁺ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted ’3′ in the systematic name, see GL-5.3.4.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-46-1

References:

1.	Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917]
2.	Ishibashi, T., Kijimoto, S. and Makita, A. Biosynthesis of globoside and Forssman hapten from trihexosylceramide and properties of β-N-acetyl-galactosaminyltransferase of guinea pig kidney. Biochim. Biophys. Acta 337 (1974) 92–106. [DOI] [PMID: 4433547]
3.	Taniguchi, N. and Makita, A. Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide β-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen. J. Biol. Chem. 259 (1984) 5637–5642. [PMID: 6425294]
4.	Okajima, T., Nakamura, Y., Uchikawa, M., Haslam, D.B., Numata, S.I., Furukawa, K., Urano, T. and Furukawa, K. Expression cloning of human globoside synthase cDNAs. Identification of β3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase. J. Biol. Chem. 275 (2000) 40498–40503. [DOI] [PMID: 10993897]

[EC 2.4.1.79 created 1976, modified 2006]

4.2.2.3

Relevance: 83.6%

Accepted name:

mannuronate-specific alginate lyase

Reaction:

Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at their reducing end.

Other name(s):

alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly(β-D-1,4-mannuronide) lyase; poly(β-D-mannuronate) lyase; aly (gene name) (ambiguous); poly[(1→4)-β-D-mannuronide] lyase

Systematic name:

alginate β-D-mannuronate—uronate lyase

Comments:

The enzyme catalyses the degradation of alginate by a β-elimination reaction. It cleaves the (1→4) bond between β-D-mannuronate and either α-L-guluronate or β-D-mannuronate, generating oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to four residues, with preference for shorter products. cf. EC 4.2.2.11, guluronate-specific alginate lyase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-15-1

References:

1.	Davidson, I.W., Lawson, C.J. and Sutherland, I.W. An alginate lysate from Azotobacter vinelandii phage. J. Gen. Microbiol. 98 (1977) 223–229. [DOI] [PMID: 13144]
2.	Nakada, H.I. and Sweeny, P.C. Alginic acid degradation by eliminases from abalone hepatopancreas. J. Biol. Chem. 242 (1967) 845–851. [PMID: 6020438]
3.	Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid. J. Biol. Chem. 237 (1962) 309–316. [PMID: 14488584]

[EC 4.2.2.3 created 1965 as EC 4.2.99.4, transferred 1972 to EC 4.2.2.3, modified 1990, modified 2015]

4.2.1.159

Relevance: 83.5%

Accepted name:

dTDP-4-dehydro-6-deoxy-α-D-glucopyranose 2,3-dehydratase

Reaction:

dTDP-4-dehydro-6-deoxy-α-D-glucopyranose = dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose + H₂O (overall reaction)
(1a) dTDP-4-dehydro-6-deoxy-α-D-glucopyranose = dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose + H₂O
(1b) dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose = dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose (spontaneous)

For diagram of dTDP-forosamine biosynthesis, click here

Other name(s):

jadO (gene name); evaA (gene name); megBVI (gene name); eryBV (gene name); mtmV (gene name); oleV (gene name); spnO (gene name); TDP-4-keto-6-deoxy-D-glucose 2,3-dehydratase; dTDP-4-dehydro-6-deoxy-α-D-glucopyranose hydro-lyase (dTDP-(2R,6S)-2,4-dihydroxy-6-methyl-2,6-dihydropyran-3-one-forming)

Systematic name:

dTDP-4-dehydro-6-deoxy-α-D-glucopyranose hydro-lyase (dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose-forming)

Comments:

The enzyme participates in the biosynthesis of several deoxysugars, including β-L-4-epi-vancosamine, α-L-megosamine, L- and D-olivose, D-oliose, D-mycarose, forosamine and β-L-digitoxose. In vitro the intermediate can undergo a spontaneous decomposition to maltol [2,3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Aguirrezabalaga, I., Olano, C., Allende, N., Rodriguez, L., Brana, A.F., Mendez, C. and Salas, J.A. Identification and expression of genes involved in biosynthesis of L-oleandrose and its intermediate L-olivose in the oleandomycin producer Streptomyces antibioticus. Antimicrob. Agents Chemother. 44 (2000) 1266–1275. [DOI] [PMID: 10770761]
2.	Chen, H., Thomas, M.G., Hubbard, B.K., Losey, H.C., Walsh, C.T. and Burkart, M.D. Deoxysugars in glycopeptide antibiotics: enzymatic synthesis of TDP-L-epivancosamine in chloroeremomycin biosynthesis. Proc. Natl. Acad. Sci. USA 97 (2000) 11942–11947. [DOI] [PMID: 11035791]
3.	Gonzalez, A., Remsing, L.L., Lombo, F., Fernandez, M.J., Prado, L., Brana, A.F., Kunzel, E., Rohr, J., Mendez, C. and Salas, J.A. The mtmVUC genes of the mithramycin gene cluster in Streptomyces argillaceus are involved in the biosynthesis of the sugar moieties. Mol. Gen. Genet. 264 (2001) 827–835. [PMID: 11254130]
4.	Wang, L., White, R.L. and Vining, L.C. Biosynthesis of the dideoxysugar component of jadomycin B: genes in the jad cluster of Streptomyces venezuelae ISP5230 for L-digitoxose assembly and transfer to the angucycline aglycone. Microbiology 148 (2002) 1091–1103. [DOI] [PMID: 11932454]
5.	Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. J. Am. Chem. Soc. 130 (2008) 4954–4967. [DOI] [PMID: 18345667]
6.	Useglio, M., Peiru, S., Rodriguez, E., Labadie, G.R., Carney, J.R. and Gramajo, H. TDP-L-megosamine biosynthesis pathway elucidation and megalomicin a production in Escherichia coli. Appl. Environ. Microbiol. 76 (2010) 3869–3877. [DOI] [PMID: 20418422]

[EC 4.2.1.159 created 2015]

1.1.1.135

Relevance: 83.2%

Accepted name:

GDP-6-deoxy-D-talose 4-dehydrogenase

Reaction:

GDP-6-deoxy-α-D-talose + NAD(P)⁺ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H⁺

For diagram of gdp-l-fucose and GDP-mannose biosynthesis, click here

Glossary:

GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose

Other name(s):

guanosine diphospho-6-deoxy-D-talose dehydrogenase; GDP-6-deoxy-D-talose:NAD(P)⁺ 4-oxidoreductase

Systematic name:

GDP-6-deoxy-α-D-talose:NAD(P)⁺ 4-oxidoreductase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-66-1

References:

1.	Markovitz, A. Biosynthesis of guanosine diphosphate D-rhamnose and guanosine diphosphate D-talomethylose from guanosine diphosphate α-D-mannose. J. Biol. Chem. 239 (1964) 2091–2098. [PMID: 14209931]

[EC 1.1.1.135 created 1972, modified 1976]

1.1.1.389

Relevance: 82.9%

Accepted name:

2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase

Reaction:

2-dehydro-3-deoxy-L-galactonate + NAD⁺ = 3-deoxy-D-glycero-2,5-hexodiulosonate + NADH + H⁺

Systematic name:

2-dehydro-3-deoxy-L-galactonate:NAD⁺ 5-oxidoreductase

Comments:

The enzyme, characterized from agarose-degrading bacteria, is involved in a degradation pathway for 3,6-anhydro-α-L-galactopyranose, a major component of the polysaccharides of red macroalgae.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Lee, S.B., Cho, S.J., Kim, J.A., Lee, S.Y., Kim, S.M. and Lim, H.S. Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading microorganisms. Biotechnol. Bioprocess Eng. 19 (2014) 866–878.

[EC 1.1.1.389 created 2015]

1.1.1.125

Relevance: 82.7%

Accepted name:

2-deoxy-D-gluconate 3-dehydrogenase

Reaction:

2-deoxy-D-gluconate + NAD⁺ = 3-dehydro-2-deoxy-D-gluconate + NADH + H⁺

Other name(s):

2-deoxygluconate dehydrogenase

Systematic name:

2-deoxy-D-gluconate:NAD⁺ 3-oxidoreductase

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-54-7

References:

1.	Eichhorn, M.M. and Cynkin, M.A. Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid dehydrogenase. Biochemistry 4 (1965) 159–165. [PMID: 14285233]

[EC 1.1.1.125 created 1972]

2.2.1.14

Relevance: 82.2%

Accepted name:

6-deoxy-6-sulfo-D-fructose transaldolase

Reaction:

6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde 3-phosphate = (2S)-3-sulfolactaldehyde + β-D-fructofuranose 6-phosphate

Glossary:

(2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate

Other name(s):

sftT (gene name)

Systematic name:

6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glyceronetransferase

Comments:

The enzyme, characterized from the bacterium Bacillus aryabhattai SOS1, is involved in a degradation pathway for 6-sulfo-D-quinovose. The enzyme can also use D-erythrose 4-phosphate as the acceptor, forming D-sedoheptulose 7-phosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Frommeyer, B., Fiedler, A.W., Oehler, S.R., Hanson, B.T., Loy, A., Franchini, P., Spiteller, D. and Schleheck, D. Environmental and intestinal phylum Firmicutes bacteria metabolize the plant sugar sulfoquinovose via a 6-deoxy-6-sulfofructose transaldolase pathway. iScience 23:101510 (2020). [DOI] [PMID: 32919372]

[EC 2.2.1.14 created 2021]

4.1.2.64

Relevance: 82.1%

Accepted name:

2-dehydro-3-deoxy-L-fuconate aldolase

Reaction:

2-dehydro-3-deoxy-L-fuconate = pyruvate + (S)-lactaldehyde

Other name(s):

2-keto-3-deoxy-L-fuconate aldolase; L-2-keto-3-deoxyfuconate aldolase; fucH (gene name)

Systematic name:

2-dehydro-3-deoxy-L-fuconate (S)-lactaldehyde-lyase (pyruvate-forming)

Comments:

The enzyme, characterized from the bacteria Veillonella ratti and Campylobacter jejuni, participates in an L-fucose degradation pathway. It also has significant activity with 2-dehydro-3-deoxy-D-pentonate (cf. EC 4.1.2.28, 2-dehydro-3-deoxy-D-pentonate aldolase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Watanabe, S. Characterization of L-2-keto-3-deoxyfuconate aldolases in a nonphosphorylating L-fucose metabolism pathway in anaerobic bacteria. J. Biol. Chem. 295 (2020) 1338–1349. [DOI] [PMID: 31914410]

[EC 4.1.2.64 created 2023]

1.1.1.127

Relevance: 82%

Accepted name:

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase

Reaction:

2-dehydro-3-deoxy-D-gluconate + NAD⁺ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H⁺

Other name(s):

2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase (ambiguous)

Systematic name:

2-dehydro-3-deoxy-D-gluconate:NAD⁺ 5-oxidoreductase

Comments:

The enzyme from Pseudomonas acts equally well on NAD⁺ or NADP⁺, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-56-9

References:

1.	Condemine, G., Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J. An enzyme in the pectolytic pathway of Erwinia chrysanthemi: 3-keto-3-deoxygluconate oxidoreductase. J. Gen. Microbiol. 130 (1984) 2839–2844.
2.	Preiss, J. and Ashwell, G. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid. J. Biol. Chem. 238 (1963) 1577–1583. [PMID: 13986017]

[EC 1.1.1.127 created 1972, modified 1976, modified 1989]

1.1.1.187

Relevance: 81.6%

Accepted name:

GDP-4-dehydro-D-rhamnose reductase

Reaction:

(1) GDP-α-D-rhamnose + NAD(P)⁺ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H⁺
(2) GDP-6-deoxy-α-D-talose + NAD(P)⁺ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H⁺

For diagram of gdp-l-fucose and GDP-mannose biosynthesis, click here

Glossary:

GDP-α-D-rhamnose = GDP-6-deoxy-α-D-mannose
GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose

Other name(s):

GDP-4-keto-6-deoxy-D-mannose reductase; GDP-4-keto-D-rhamnose reductase; guanosine diphosphate-4-keto-D-rhamnose reductase; GDP-6-deoxy-D-mannose:NAD(P)⁺ 4-oxidoreductase; GDP-6-deoxy-α-D-mannose:NAD(P)⁺ 4-oxidoreductase

Systematic name:

GDP-4-dehydro-α-D-rhamnose:NAD(P)⁺ 4-oxidoreductase

Comments:

The enzyme, which operates in the opposite direction to that shown, forms a mixture of GDP-α-D-rhamnose and its C-4 epimer, GDP-6-deoxy-α-D-talose. cf. EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase and EC 1.1.1.135, GDP-6-deoxy-D-talose 4-dehydrogenase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-56-3

References:

1.	Barber, G.A. The synthesis of guanosine 5′-diphosphate D-rhamnose by enzymes of a higher plant. Biochim. Biophys. Acta 165 (1968) 68–75. [DOI] [PMID: 4386238]
2.	Winkler, N.W. and Markovitz, A. Guanosine diphosphate-4-keto-D-rhamnose reductase. A non-stereoselective enzyme. J. Biol. Chem. 246 (1971) 5868–5876. [PMID: 4398966]

[EC 1.1.1.187 created 1984]

4.2.2.14

Relevance: 81.4%

Accepted name:

glucuronan lyase

Reaction:

Eliminative cleavage of (1→4)-β-D-glucuronans to give oligosaccharides with 4-deoxy-β-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.

For diagram of reaction, click here

Other name(s):

(1,4)-β-D-glucuronan lyase

Systematic name:

(1→4)-β-D-glucuronan lyase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 193766-71-1

References:

1.	Michaud, P., Pheulpin, P., Petit, E., Seguin, J.P., Barbotin, J.N., Heyraud, A., Courtois, B. and Courtois, J. Identification of glucuronan lyase from a mutant strain of Rhizobium meliloti. Int. J. Biol. Macromol. 21 (1997) 3–9. [DOI] [PMID: 9283009]

[EC 4.2.2.14 created 2000]

1.1.1.401

Relevance: 81.3%

Accepted name:

2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD⁺)

Reaction:

2-dehydro-3-deoxy-L-rhamnonate + NAD⁺ = 2,4-didehydro-3-deoxy-L-rhamnonate + NADH + H⁺

For diagram of L-rhamnose metabolism, click here

Other name(s):

2-keto-3-deoxy-L-rhamnonate dehydrogenase

Systematic name:

2-dehydro-3-deoxy-L-rhamnonate:NAD⁺ 4-oxidoreductase

Comments:

The enzyme, characterized from the bacteria Sphingomonas sp. SKA58 and Sulfobacillus thermosulfidooxidans, is involved in the non-phosphorylative degradation pathway for L-rhamnose. It does not show any detectable activity with NADP⁺ or with other aldoses.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Watanabe, S. and Makino, K. Novel modified version of nonphosphorylated sugar metabolism - an alternative L-rhamnose pathway of Sphingomonas sp. FEBS J. 276 (2009) 1554–1567. [DOI] [PMID: 19187228]
2.	Bae, J., Kim, S.M. and Lee, S.B. Identification and characterization of 2-keto-3-deoxy-L-rhamnonate dehydrogenase belonging to the MDR superfamily from the thermoacidophilic bacterium Sulfobacillus thermosulfidooxidans: implications to L-rhamnose metabolism in archaea. Extremophiles 19 (2015) 469–478. [DOI] [PMID: 25617114]

[EC 1.1.1.401 created 2016]

3.1.1.109

Relevance: 81.3%

Accepted name:

iron(III)-salmochelin esterase

Reaction:

(1) iron(III)-[diglucosyl-enterobactin] complex + H₂O = iron(III)-[salmochelin S2] complex
(2) iron(III)-[monoglucosyl-enterobactin] complex + H₂O = iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)₃] complex
(3) iron(III)-[salmochelin S2] complex + H₂O = iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)₂] complex + N-(2,3-dihydroxybenzoyl)-L-serine
(4) iron(III)-[salmochelin S2] complex + H₂O = iron(III)-[salmochelin S1] complex + salmochelin SX
(5) iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)₃] complex + H₂O = iron(III)-[salmochelin S1] complex + N-(2,3-dihydroxybenzoyl)-L-serine
(6) iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)₂] complex + H₂O = iron(III)-[salmochelin SX] complex + salmochelin SX

Glossary:

salmochelin S2 = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl]-N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine
salmochelin S1 = O-3-[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-deoxy-β-D-glucosyl-2,3-dihydroxybenzoyl)-L-serine
monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-[3→1(3)]-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE
diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-[3→1(3)]-lactone = salmochelin S4 = di-C-glucosyl-enterobactin
salmochelin SX = N-(C-5-deoxy-β-D-glucosyl-2,3-dihydroxybenzoyl)-L-serine

Other name(s):

iroD (gene name); ferric-salmochelin esterase

Systematic name:

iron(III)-salmochelin complex hydrolase

Comments:

This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. The enzyme acts on iron(III)-bound enterobactin and C-glucosylated derivatives known as salmochelins. Unlike EC 3.1.1.107, apo-salmochelin esterase (IroE), IroD prefers iron(III)-bound siderophores as substrates, and is assumed to act after the iron-siderophore complexes are imported into the cell. It catalyses several hydrolytic reactions, producing a mixture of iron(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] complex and salmochelin SX.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Lin, H., Fischbach, M.A., Liu, D.R. and Walsh, C.T. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J. Am. Chem. Soc. 127 (2005) 11075–11084. [PMID: 16076215]

[EC 3.1.1.109 created 2019]

5.3.1.37

Relevance: 81.1%

Accepted name:

4-deoxy-4-sulfo-D-erythrose isomerase

Reaction:

4-deoxy-4-sulfo-D-erythrose = 4-deoxy-4-sulfo-D-erythrulose

Other name(s):

sqwI (gene name)

Systematic name:

4-deoxy-4-sulfo-D-erythrose ketose-aldose isomerase

Comments:

The enzyme, characterized from the bacterium Clostridium sp. MSTE9, is involved in a D-sulfoquinovose degradation pathway.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. [DOI]

[EC 5.3.1.37 created 2022]

2.7.7.92

Relevance: 81%

Accepted name:

3-deoxy-D-glycero-D-galacto-nonulopyranosonate cytidylyltransferase

Reaction:

CTP + 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate = diphosphate + CMP-3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate

Systematic name:

CTP:3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate cytidylyltransferase

Comments:

The enzyme is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Terada, T., Kitazume, S., Kitajima, K., Inoue, S., Ito, F., Troy, F.A. and Inoue, Y. Synthesis of CMP-deaminoneuraminic acid (CMP-KDN) using the CTP:CMP-3-deoxynonulosonate cytidylyltransferase from rainbow trout testis. Identification and characterization of a CMP-KDN synthetase. J. Biol. Chem. 268 (1993) 2640–2648. [PMID: 8381411]
2.	Terada, T., Kitajima, K., Inoue, S., Koppert, K., Brossmer, R. and Inoue, Y. Substrate specificity of rainbow trout testis CMP-3-deoxy-D-glycero-D-galacto-nonulosonic acid (CMP-Kdn) synthetase: kinetic studies of the reaction of natural and synthetic analogues of nonulosonic acid catalyzed by CMP-Kdn synthetase. Eur. J. Biochem. 236 (1996) 852–855. [DOI] [PMID: 8665905]
3.	Nakata, D., Munster, A.K., Gerardy-Schahn, R., Aoki, N., Matsuda, T. and Kitajima, K. Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates. Glycobiology 11 (2001) 685–692. [DOI] [PMID: 11479279]
4.	Tiralongo, J., Fujita, A., Sato, C., Kitajima, K., Lehmann, F., Oschlies, M., Gerardy-Schahn, R. and Munster-Kuhnel, A.K. The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme. Glycobiology 17 (2007) 945–954. [DOI] [PMID: 17580313]
5.	Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893–897. [DOI] [PMID: 18804026]

[EC 2.7.7.92 created 2016]

4.1.2.51

Relevance: 81%

Accepted name:

2-dehydro-3-deoxy-D-gluconate aldolase

Reaction:

2-dehydro-3-deoxy-D-gluconate = pyruvate + D-glyceraldehyde

For diagram of the Entner-Doudoroff pathway, click here

Other name(s):

Pto1279 (gene name); KDGA; KDG-specific aldolase

Systematic name:

2-dehydro-3-deoxy-D-gluconate D-glyceraldehyde-lyase (pyruvate-forming)

Comments:

The enzyme from the archaeon Picrophilus torridus is involved in D-glucose and D-galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. In the direction of aldol synthesis the enzyme catalyses the formation of 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at a similar ratio. It shows no activity with 2-dehydro-3-deoxy-D-gluconate 6-phosphate. cf. EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Reher, M., Fuhrer, T., Bott, M. and Schonheit, P. The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate- specific aldolase. J. Bacteriol. 192 (2010) 964–974. [DOI] [PMID: 20023024]

[EC 4.1.2.51 created 2013]