Literature summary for 5.3.3.2 extracted from

Carrigan, C.N.; Poulter, C.D.
Zinc is an essential cofactor for type I isopentenyl diphosphate:dimethylallyl diphosphate isomerase (2003), J. Am. Chem. Soc., 125, 9008-9009.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer	Escherichia coli
Mn2+	the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer	Escherichia coli
Zinc	essential cofactor. Type I enzyme contains an atom of tinc. The metal is located in an unusual six-coordinate pocket and may facilitate protonation of the unactivated carbon-carbon double bond in isopentenyl diphosphate	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	type I isopentenyl-diphosphate D-isomerase	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	zinc is located in an unusual six-coordinate pocket and may facilitate protonation of the unactivated carbon-carbon double bond in isopentenyl diphosphate. The sulfhydryl moiety C67, perhaps in the thiolate form, is in position to remove a proton from the resulting tertiary carbocation to complete the reaction	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)