Literature summary for 2.5.1.7 extracted from

Samland, A.K.; Jelesarov, I.; Kuhn, R.; Amrhein, N.; Macheroux, P.
Thermodynamic characterization of ligand-induced conformational changes in UDP-N-acetylglucosamine enolpyruvyl transferase (2001), Biochemistry, 40, 9950-9956.

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Organism

Organism	UniProt	Comment	Textmining
Enterobacter cloacae	P33038	MurA	-
Enterobacter cloacae	P33038	recombinant purified enzyme	-
Enterobacter cloacae DSM 30054	P33038	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	thermodynamical investigation of substrate binding and binding of inhibitory substrate analogue fosfomycin	Enterobacter cloacae	a

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
More	structure	Enterobacter cloacae

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Release 2023.1 (January 2023)