Literature summary for 5.4.99.5 extracted from

Lee, A.Y.; Zhang, S.; Kongsaeree, P.; Clardy, J.; Ganem, B.; Erickson,J.W.; Xie, D.
Thermodynamics of a transition state analogue inhibitor binding to Escherichia coli chorismate mutase: probing the charge state of an active site residue and its role in inhibitor binding and catalysis (1998), Biochemistry, 37, 9052-9057.

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Protein Variants

Protein Variants	Comment	Organism
Q88E	mutation of Gln88 to Glu in the monofunctional chorismate mutase results in an enzyme with a pH profile of activity significantly different from that of the wild-type protein	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
Transition state analogue inhibitor	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	monofunctional enzyme	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Chorismate	-	Escherichia coli	Prephenate	-	?

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Release 2023.1 (January 2023)