Literature summary for 2.5.1.7 extracted from

Schonbrunn, E.; Svergun, D.I.; Amrhein, N.; Koch, M.H.J.
Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA) (1998), Eur. J. Biochem., 253, 406-412.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray structure analysis of ligated and unligated MurA	Enterobacter cloacae

Organism

Organism	UniProt	Comment	Textmining
Enterobacter cloacae	-	MurA	-
Enterobacter cloacae	-	recombinant purified enzyme	-
Enterobacter cloacae DSM 30054	-	MurA	-

Reaction

Reaction	Comment	Organism	Reaction ID
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine	structure analysis of conformational changes upon substrate binding	Enterobacter cloacae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine	substrate binding structure	Enterobacter cloacae	phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine	-	?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine	substrate binding structure	Enterobacter cloacae DSM 30054	phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine	-	?

Subunits

Subunits	Comment	Organism
More	structure	Enterobacter cloacae

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Release 2023.1 (January 2023)