1nfs
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STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP
OverviewOverview
Isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase, is a key enzyme in the biosynthesis of isoprenoids. The reaction involves, protonation and deprotonation of the isoprenoid unit and proceeds through, a carbocationic transition state. Analysis of the crystal structures (2 A), of complexes of Escherichia coli IPP.DMAPPs isomerase with a transition, state analogue (N,N-dimethyl-2-amino-1-ethyl diphosphate) and a covalently, attached irreversible inhibitor (3,4-epoxy-3-methyl-1-butyl diphosphate), indicates that Glu-116, Tyr-104, and Cys-67 are involved in the, antarafacial addition/elimination of protons during isomerization. This, work provides a new perspective about the mechanism of the reaction.
About this StructureAbout this Structure
1NFS is a Single protein structure of sequence from Escherichia coli with MN, MG and DED as ligands. Active as Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2 Full crystallographic information is available from OCA.
ReferenceReference
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., Wouters J, Oudjama Y, Barkley SJ, Tricot C, Stalon V, Droogmans L, Poulter CD, J Biol Chem. 2003 Apr 4;278(14):11903-8. Epub 2003 Jan 22. PMID:12540835
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