Literature summary for 5.3.3.2 extracted from

Wouters, J.; Oudjama, Y.; Barkley, S.J.; Tricot, C.; Stalon, V.; Droogmans, L.; Poulter, C.D.
Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors (2003), J. Biol. Chem., 278, 11903-11908.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystal structures of complexes with transition state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate and the covalently attached irreversible inhibitors 3,4-epoxy-3-methyl-1-butyl diphosphate at 1.96 A resolution	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	key enzyme in biosynthesis of isoprenoids	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q46822	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Isopentenyl diphosphate = dimethylallyl diphosphate	reaction involves protonation and deprotonation of the isoprenoid unit and proceeds through a carbocationic transition state. Glu116/Tyr104 and Cys67 are involved in the antarafacial addition/elimination of protons during isomerization	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	key enzyme in biosynthesis of isoprenoids	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)