The Enzyme Database

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EC 2.3.1.191     
Accepted name: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
Reaction: (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine = UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine + a holo-[acyl-carrier protein]
For diagram of lipid IVA biosynthesis, click here
Glossary: myristoyl = tetradecanoyl
Other name(s): 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 name); lpxD (gene name); (3R)-3-hydroxymyristoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxymyristoyl]-α-D-glucosamine N-acetyltransferase
Systematic name: (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine N-acetyltransferase
Comments: The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia prefers (R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] over (R,S)-3-hydroxyhexadecanoyl-[acyl-carrier protein] [1]. Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available. When grown on 1% propionic acid, lipid A also contains the odd-chain fatty acids tridecanoic acid, pentadecanoic acid, hydroxytridecanoic acid, and hydroxypentadecanoic acid [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bartling, C.M. and Raetz, C.R. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 48 (2009) 8672–8683. [PMID: 19655786]
2.  Buetow, L., Smith, T.K., Dawson, A., Fyffe, S. and Hunter, W.N. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. Proc. Natl. Acad. Sci. USA 104 (2007) 4321–4326. [PMID: 17360522]
3.  Bartling, C.M. and Raetz, C.R. Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 47 (2008) 5290–5302. [PMID: 18422345]
4.  Kelly, T.M., Stachula, S.A., Raetz, C.R. and Anderson, M.S. 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 (1993) 19866–19874. [PMID: 8366125]
5.  Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. 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 (2008) 4549–4558. [PMID: 18456814]
[EC 2.3.1.191 created 2010]
 
 


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