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| Creator | Title | Description | Subject | Date | ||
|---|---|---|---|---|---|---|
| 1 |
 | Poulter, Charles Dale | 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 | 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 ... | Catalytic Domain; Crystallography; Organophosphorus Compounds | 2003-04-04 |
| 2 |
 | Poulter, Charles Dale | Farnesyl pyrophosphate synthetase. Mechanistic studies of the 1'-4 coupling reaction with 2-fluorogeranyl pyrophosphate. | The mechanism of the 1'-4 coupling reaction between isopentenyl pyrophosphate and geranyl pyrophosphate catalyzed by farnesyl pyrophosphate synthetase from porcine liver was studied with the allylic substrate analogue 2-fluorogeranyl pyrophosphate. 2-Fluorogeranyl pyrophosphate is an alternate subst... | Kinetics; Liver; Mass Spectrometry; Organophosphorus Compounds; Protein Binding | 1978-10-25 |
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