Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor
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 Å crystal structure of the...
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Published in | Proteins, structure, function, and bioinformatics Vol. 54; no. 2; pp. 216 - 221 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
01.02.2004
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Subjects | |
Online Access | Get full text |
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Summary: | 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 Å 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. Proteins 2003;53:000–000. © 2003 Wiley‐Liss, Inc. |
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Bibliography: | National Institutes of Health - No. GM25521 istex:B727D0FAB0B2A07293E80079A05BA8FA69E5967A the Belgian Fonds National de la Recherche Scientifique (FRFC and ISSN grant) 'Action de Recherche Concertée' (ARC) financed by the French Community of Belgium and from the Belgian Fund for Joint Basic research ark:/67375/WNG-6H6CF4TT-8 ArticleID:PROT10573 L. Droogmans is a Research Associate of the Belgian Fonds National de la Recherche Scientifique. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0887-3585 1097-0134 |
DOI: | 10.1002/prot.10573 |