The existence of an electrophilic component in the reaction catalysed by triose phosphate isomerase

Biochem J. 1974 Aug;141(2):589-92. doi: 10.1042/bj1410589.

Abstract

In the presence of triose phosphate isomerase, the substrate dihydroxyacetone phosphate is reduced stereoselectively by NaBH(4). The reduction of enzyme-bound substrate is almost completely or completely stereoselective and occurs about one order of magnitude faster than that in free solution. This acceleration implies a polarization of the carbonyl group when dihydroxyacetone phosphate is bound.

MeSH terms

  • Acetone
  • Animals
  • Borohydrides
  • Carbohydrate Epimerases*
  • Chickens
  • Glycerophosphates
  • NAD
  • Organophosphorus Compounds
  • Trioses
  • Tritium

Substances

  • Borohydrides
  • Glycerophosphates
  • Organophosphorus Compounds
  • Trioses
  • NAD
  • Tritium
  • Acetone
  • Carbohydrate Epimerases