Biology:UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
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UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.3.1.191 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC 2.3.1.191, 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), lpxD (gene)) is an enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine [math]\displaystyle{ \rightleftharpoons }[/math] UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + holo-[acyl-carrier protein]
The enzyme catalyses a step of lipid A biosynthesis.
References
- ↑ "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry 48 (36): 8672–83. September 2009. doi:10.1021/bi901025v. PMID 19655786.
- ↑ "Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis". Proceedings of the National Academy of Sciences of the United States of America 104 (11): 4321–6. March 2007. doi:10.1073/pnas.0606356104. PMID 17360522. Bibcode: 2007PNAS..104.4321B.
- ↑ "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry 47 (19): 5290–302. May 2008. doi:10.1021/bi800240r. PMID 18422345.
- ↑ "The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis". The Journal of Biological Chemistry 268 (26): 19866–74. September 1993. doi:10.1016/S0021-9258(19)36593-7. PMID 8366125.
- ↑ "Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis". Journal of Bacteriology 190 (13): 4549–58. July 2008. doi:10.1128/jb.00234-08. PMID 18456814.
External links
- UDP-3-O-(3-hydroxymyristoyl)glucosamine+N-acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase.
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