Isopentenyl-diphosphate delta-isomerase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | ''E. coli'' IPPI contains 2 divalent ions which interact with the irreversible inhibitor EIPP<ref>PMID:12540835</ref>. | + | ''E. coli'' IPPI contains <scene name='59/595218/Cv/5'>2 divalent ions which interact with the irreversible inhibitor EIPP</scene><ref>PMID:12540835</ref>. |
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| + | <scene name='59/595218/Cv/6'>Mg coordination site</scene>. | ||
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| + | <scene name='59/595218/Cv/7'>Mn coordination site</scene>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:28, 10 April 2016
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3D structures of isopentenyl-diphosphate delta-isomerase
Updated on 10-April-2016
References
- ↑ 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
- ↑ 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
