Effect of bivalent cations on the interaction of transketolase with its donor substrate

Proteins. 2008 May 1;71(2):541-5. doi: 10.1002/prot.21880.

Abstract

The effect of the type of the cation cofactor of transketolase (i.e., Ca2+ or Mg2+) on its interaction with xylulose 5-phosphate (donor substrate) has been studied. In the presence of magnesium, the active centers of the enzyme were functionally equivalent with respect to xylulose 5-phosphate binding and exhibited identical affinities for the donor substrate. Substitution of Ca2+ for Mg2+ results in the loss of the equivalence. In particular, this becomes apparent on binding of xylulose 5-phosphates to one of the two active centers of the enzyme, which caused the second center to undergo a several fold decrease in the affinity for the donor substrate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites / drug effects
  • Calcium / pharmacology*
  • Cations, Divalent / pharmacology*
  • Kinetics
  • Magnesium / pharmacology*
  • Pentosephosphates / metabolism*
  • Saccharomyces cerevisiae / enzymology
  • Transketolase / drug effects
  • Transketolase / metabolism*

Substances

  • Cations, Divalent
  • Pentosephosphates
  • xylulose-5-phosphate
  • Transketolase
  • Magnesium
  • Calcium