|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase: lpxD
In Pathway: lipid IVA biosynthesis
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
Enzyme Commission Synonyms: 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)
This is the third committed step in lipid A biosynthesis.
Enzyme Commission Summary:
The enzyme catalyzes a step of lipid A biosynthesis. LpxD from Escherichia prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] [Bartling09]. 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 [Bainbridge08]]|.
Bainbridge08: Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP (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(13);4549-58. PMID: 18456814
Bartling09: Bartling CM, Raetz CR (2009). "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis." Biochemistry 48(36);8672-83. PMID: 19655786
Buetow07: Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN (2007). "Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis." Proc Natl Acad Sci U S A 104(11);4321-6. PMID: 17360522
Kelly93: Kelly TM, Stachula SA, Raetz CR, Anderson MS (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 1993;268(26);19866-74. PMID: 8366125
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