Does phosphoglucoisomerase display anomeric specificity or selectivity towards alpha-D-glucose 6-phosphate? An assessment by two-dimensional phase-sensitive 31P exchange spectroscopy (EXSY) n.m.r

Biochem J. 1993 Oct 15;295 ( Pt 2)(Pt 2):607-9. doi: 10.1042/bj2950607.

Abstract

The study by two-dimensional phase-sensitive 31P exchange spectroscopy (EXSY) n.m.r. of hexose 6-phosphates interconversion in the reaction catalysed by yeast phosphoglucoisomerase reveals that the enzyme displays anomeric selectivity, rather than specificity, towards alpha-D-glucose 6-phosphate. Indeed, beta-D-glucose 6-phosphate participates for about 20% to the total and direct conversion of the aldohexose into oxohexose ester.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glucose-6-Phosphate
  • Glucose-6-Phosphate Isomerase / chemistry
  • Glucose-6-Phosphate Isomerase / metabolism*
  • Glucosephosphates / chemistry
  • Glucosephosphates / metabolism*
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Conformation
  • Phosphorus Isotopes
  • Substrate Specificity

Substances

  • Glucosephosphates
  • Phosphorus Isotopes
  • Glucose-6-Phosphate
  • Glucose-6-Phosphate Isomerase