1ow2: Difference between revisions

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[[Image:1ow2.jpg|left|200px]]
{{Seed}}
[[Image:1ow2.png|left|200px]]


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{{STRUCTURE_1ow2|  PDB=1ow2  |  SCENE=  }}  
{{STRUCTURE_1ow2|  PDB=1ow2  |  SCENE=  }}  


'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX OF C67A MUTANT WITH EIPP'''
===STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX OF C67A MUTANT WITH EIPP===




==Overview==
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Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate. Analysis of the 1.97 A crystal structure of the inactive C67A mutant of E. coli isopentenyl diphosphate:dimethylallyl diphosphate isomerase complexed with the mechanism-based inactivator 3,4-epoxy-3-methyl-1-butyl diphosphate is in agreement with an isomerization mechanism involving Glu 116, Tyr 104, and Cys 67. In particular, the results are consistent with a mechanism where Glu116 is involved in the protonation step and Cys67 in the elimination step.
The line below this paragraph, {{ABSTRACT_PUBMED_14696183}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_14696183}}


==About this Structure==
==About this Structure==
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[[Category: Wouters, J.]]
[[Category: Wouters, J.]]
[[Category: Complex]]
[[Category: Complex]]
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