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Kinetic studies on the prenyl chain elongation by undecaprenyl diphosphate synthase with artificial substrate homologues
Authors:S Ohnuma  T Koyama  K Ogura
Affiliation:Chemical Research Institute of Non-Aqueous Solutions, Tohoku University, Sendai, Japan.
Abstract:
In the undecaprenyl diphosphate synthase reaction, an allylic substrate homologue, (2Z,6E,10E)-4-methyl-geranylgeranyl diphosphate was found to be a potent competitive inhibitor against the allylic primer, (2Z,6E,10E)-geranylgeranyl diphosphate. On the other hand, it acted as a strong noncompetitive inhibitor against isopentenyl diphosphate. On the basis of these facts, the topology of the substrate-binding sites as well as the reason why the synthase reaction with (E)-3-methyl-3-pentenyl diphosphate always stops completely at the first stage of condensation, yielding an allylic diphosphate with a methyl group at the 4-position, are discussed.
Keywords:
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