Literature summary for 2.3.1.157 extracted from

Min, J.; Lin, D.; Zhang, Q.; Zhang, J.; Yu, Z.
Structure-based virtual screening of novel inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU (2012), Eur. J. Med. Chem., 53, 150-158.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + alpha-D-glucosamine 1-phosphate	Xanthomonas oryzae	-	CoA + N-acetyl-alpha-D-glucosamine 1-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Xanthomonas oryzae	-	pv. oryzae	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + alpha-D-glucosamine 1-phosphate	-	Xanthomonas oryzae	CoA + N-acetyl-alpha-D-glucosamine 1-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
GlmU	-	Xanthomonas oryzae

General Information

General Information	Comment	Organism
physiological function	the bifunctional enzyme N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, catalyzes two-step formation of UDP-GlcNAc, an important precursor in bacterial peptidoglycan and lipopolysaccharide biosynthesis, which are important constituents of the cell wall of both Gram-positive and Gram-negative bacteria. The first activity of GlmU, the C-terminal domain (acetyltransferase), catalyzes the formation of N-acetylglucosamine-1-phosphate from glucosamine-1-phosphate using acetyl-CoA as the acetyl donor. The second activity of GlmU, the N-terminal and rate-limiting domain (uridyltransferase), catalyzes the formation of UDP-GlcNAc from GlcNAc-1-phosphate and uridine triphosphate, UTP	Xanthomonas oryzae

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Release 2023.1 (January 2023)