Literature summary for 2.3.1.191 extracted from

Jenkins, R.J.; Heslip, K.A.; Meagher, J.L.; Stuckey, J.A.; Dotson, G.D.
Structural basis for the recognition of peptide RJPXD33 by acyltransferases in lipid A biosynthesis (2014), J. Biol. Chem., 289, 15527-15535.

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Inhibitors

Inhibitors	Comment	Organism	Structure
RJPXD33	i.e. TNLYMLPKWDIP, peptide inhibitor, binds to both UDP-N-acetylglucosamine acyltransferase (LpxA, EC 2.3.1.129) and UDP-3-O-(acyl)-glucosamine acyltransferase. Comparison with binding to LpxA suggests overlap with the acyl-phosphopantetheine arm of acyl-ACP, thereby inhibiting acyl-ACP from binding to LpxD. RJPXD33 binds to LpxD without the prior binding of other ligands	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)