Literature summary for 5.3.3.2 extracted from

Zheng, W.; Sun, F.; Bartlam, M.; Li, X.; Li, R.; Rao, Z.
The crystal structure of human isopentenyl diphosphate isomerase at 1.7 A resolution reveals its catalytic mechanism in isoprenoid biosynthesis (2007), J. Mol. Biol., 366, 1447-1458.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
native enzyme at 1.7 A and in complex with substrate at 1.9 A resolution. comparison with Escherichia coli enzyme structure	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q13907	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Isopentenyl diphosphate = dimethylallyl diphosphate	interconversion of substrate is catalyzed by a stereoselective antarafacial [1.3] transposition of a proton involving residues C87, E149, W197 and Y137	Homo sapiens	a

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Release 2023.1 (January 2023)