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

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UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC, 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.


  1. ^ Bartling CM, Raetz CR (September 2009). "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 48 (36): 8672–83. doi:10.1021/bi901025v. PMC 2748855Freely accessible. PMID 19655786. 
  2. ^ Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN (March 2007). "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. doi:10.1073/pnas.0606356104. PMC 1810333Freely accessible. PMID 17360522. 
  3. ^ Bartling CM, Raetz CR (May 2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 47 (19): 5290–302. doi:10.1021/bi800240r. PMC 2435086Freely accessible. PMID 18422345. 
  4. ^ Kelly TM, Stachula SA, Raetz CR, Anderson MS (September 1993). "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. PMID 8366125. 
  5. ^ Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP (July 2008). "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. doi:10.1128/jb.00234-08. PMC 2446808Freely accessible. PMID 18456814. 

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