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| Creator | Title | Description | Subject | Date | ||
|---|---|---|---|---|---|---|
| 1 |
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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 |
| 2 |
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Poulter, Charles Dale | Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme. | Prenyltransferase catalyzes the sequential, irreversible 1'-4 condensation of isopentenyl-PP with dimethylallyl-PP and geranyl-PP to yield farnesyl-PP. A kinetic study shows substrate inhibition by isopentenyl-PP at concentrations above 0.7 microM when the concentration of geranyl-PP is 1.0 microM o... | Birds; Kinetics; Structure-Activity Relationship; Substrate Specificity | 1979-10-10 |
| 3 |
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Poulter, Charles Dale | Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH | Squalene synthase catalyzes the condensation of two molecules of farnesyl diphosphate (FPP) to give presqualene diphosphate (PSPP) and the subsequent reductive rearrangement of PSPP to squalene. Previous studies of the mechanism of addition of FPP to the enzyme have led to conflicting interpretation... | Enzyme Activation; Sesquiterpenes; Kinetics | 1993-04-15 |
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