Literature summary for 2.3.1.129 extracted from

Williams, A.H.; Raetz, C.R.
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase (2007), Proc. Natl. Acad. Sci. USA, 104, 13543-13550.

Search for more literature for 2.3.1.129

Application

Application	Comment	Organism
medicine	structures helps to design new inhibitors that target LpxA, antibiotics	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
by using the hanging drop vapor diffusion method, in the presence of a 25-fold molar excess of either UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc or UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc, structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A722	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine	first step in lipid A biosynthesis	Escherichia coli	[acyl-carrier protein] + UDP-3-O-(3-hydroxymyristoyl)-N-acetyl-alpha-D-glucosamine	-	?
R-3-hydroxydecanoyl-[acyl carrier protein] + UDP-N-acetylglucosamine	first step in lipid A biosynthesis	Escherichia coli	[acyl-carrier protein] + UDP-3-O-hydroxydecanoyl-N-acetylglucosamine	-	?

Synonyms

Synonyms	Comment	Organism
LpxA	-	Escherichia coli
UDP-N-acetylglucosamine acyltransferase	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)