Effect of CrATP on the association of the reacting forms of yeast hexokinase.
J Biol Chem, 1977/3/25;252(6):1844-6.
PMID: 321444
Abstract
Reacting enzyme sedimentation studies have been performed with yeast hexokinase isozymes A and B in the presence and absence of chromium ATP at pH 6.75. Preincubation of either isozyme with CrATP causes a shift in the monomer-dimer equilibrium toward the monomeric form. The results are consistent with the observed increase in inhibition caused by CrATP (Danenberg, K.D., and Cleland, W.W. (1975) Biochemistry 14, 28-39) being due to a conformational change in the protein which causes a decrease in the association constant for the monomer.
MeSH terms
Adenosine Triphosphate; Binding Sites; Chromium; Hexokinase; Macromolecular Substances; Protein Conformation; Saccharomyces cerevisiae
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