Literature summary for 2.3.1.157 extracted from

Olsen, L.R.; Vetting, M.W.; Roderick, S.L.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products (2007), Protein Sci., 16, 1230-1235.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with acetyl-CoA, CoA and glucosamine-1-phosphate, and with desulfo-CoA and N-acetylglucosamine-1-phosphate. The 2-amino group of glucosamine-1-phosphate is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate	the 2-amino group of glucosamine-1-phosphate is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism	Escherichia coli	a

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Release 2023.1 (January 2023)