The Enzyme Database

Your query returned 2 entries.    printer_iconPrintable version



EC 2.4.1.182     
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 IVA 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, 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]
 
 
EC 2.7.1.130     
Accepted name: tetraacyldisaccharide 4′-kinase
Reaction: ATP + a lipid A disaccharide = ADP + a lipid IVA
For diagram of lipid IVA biosynthesis, click here
Glossary: a lipid A disaccharide = a dephospho-lipid IVA = 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 IVA = 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, 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]
 
 


Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald