Isopentenyl-diphosphate delta-isomerase

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<StructureSection load='1nfz' size='340' side='right' caption='Structure of isopentenyl-diphosphate delta-isomerase complex withIPP, Mg+2 and Mn+2 ions (green) and IPP (PDB code [[1nfz]]).' scene=''>
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<StructureSection load='1nfz' size='340' side='right' caption='Structure of E. coli isopentenyl-diphosphate delta-isomerase complex with EIPP, Mg+2 (green) and Mn+2 (purple) ions and EIPP (PDB code [[1nfz]]).' scene=''>
== Function ==
== Function ==
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'''Isopentenyl-diphosphate delta-isomerase''' (IPPI) catalyzes the conversion of the un-reactive isopentenyl diphosphate (IPP) to the more reactive dimethylallyl diphosphate (DMAPP). 3,4-epoxy-3-methyl butyl diphosphate (EIPP) is an irreversible inhibitor of IPPI. IPPI participates in isoprenoid biosynthesis<ref>PMID:3022798</ref>.
'''Isopentenyl-diphosphate delta-isomerase''' (IPPI) catalyzes the conversion of the un-reactive isopentenyl diphosphate (IPP) to the more reactive dimethylallyl diphosphate (DMAPP). 3,4-epoxy-3-methyl butyl diphosphate (EIPP) is an irreversible inhibitor of IPPI. IPPI participates in isoprenoid biosynthesis<ref>PMID:3022798</ref>.
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== Disease ==
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== Structural highlights ==
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''E. coli'' IPPI contains 2 divalent ions which interact with the irreversible inhibitor EIPP<ref>PMID:12540835</ref>.
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== Relevance ==
 
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== Structural highlights ==
 
</StructureSection>
</StructureSection>

Revision as of 09:14, 3 April 2016

Structure of E. coli isopentenyl-diphosphate delta-isomerase complex with EIPP, Mg+2 (green) and Mn+2 (purple) ions and EIPP (PDB code 1nfz).

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3D structures of isopentenyl-diphosphate delta-isomerase

Updated on 03-April-2016

References

  1. Reardon JE, Abeles RH. Mechanism of action of isopentenyl pyrophosphate isomerase: evidence for a carbonium ion intermediate. Biochemistry. 1986 Sep 23;25(19):5609-16. PMID:3022798
  2. Wouters J, Oudjama Y, Barkley SJ, Tricot C, Stalon V, Droogmans L, Poulter CD. 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. J Biol Chem. 2003 Apr 4;278(14):11903-8. Epub 2003 Jan 22. PMID:12540835 doi:http://dx.doi.org/10.1074/jbc.M212823200

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Michal Harel, Alexander Berchansky

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