Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:
UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferaseInferred from experiment: 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]]|.

Citations: [Buetow07, Bartling08, Kelly93]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


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

Bartling08: Bartling CM, Raetz CR (2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis." Biochemistry 47(19);5290-302. PMID: 18422345

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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.5 on Sun Nov 29, 2015, BIOCYC13A.