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

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

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 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[edit]

  1. ^ Bartling, C.M.; Raetz, C.R. (2009). "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 48: 8672–8683. doi:10.1021/bi901025v. PMC 2748855Freely accessible. PMID 19655786. 
  2. ^ Buetow, L.; Smith, T.K.; Dawson, A.; Fyffe, S.; Hunter, W.N. (2007). "Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis". Proc. Natl. Acad. Sci. USA. 104: 4321–4326. doi:10.1073/pnas.0606356104. PMC 1810333Freely accessible. PMID 17360522. 
  3. ^ Bartling, C.M.; Raetz, C.R. (2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 47: 5290–5302. doi:10.1021/bi800240r. PMC 2435086Freely accessible. PMID 18422345. 
  4. ^ Kelly, T.M.; Stachula, S.A.; Raetz, C.R.; Anderson, M.S. (1993). "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: 19866–19874. PMID 8366125. 
  5. ^ Bainbridge, B.W.; Karimi-Naser, L.; Reife, R.; Blethen, F.; Ernst, R.K.; Darveau, R.P. (2008). "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: 4549–4558. doi:10.1128/jb.00234-08. PMC 2446808Freely accessible. PMID 18456814. 

External links[edit]