Kinetic studies on the prenyl chain elongation by undecaprenyl diphosphate synthase with artificial substrate homologues

FEBS Lett. 1989 Oct 23;257(1):71-4. doi: 10.1016/0014-5793(89)81789-2.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkyl and Aryl Transferases*
  • Bacillus subtilis / enzymology
  • Binding Sites
  • Kinetics
  • Polyisoprenyl Phosphates / pharmacology*
  • Structure-Activity Relationship
  • Transferases / antagonists & inhibitors
  • Transferases / metabolism*

Substances

  • Polyisoprenyl Phosphates
  • Transferases
  • Alkyl and Aryl Transferases
  • undecaprenyl pyrophosphate synthetase