Effect of CrATP on the association of the reacting forms of yeast hexokinase.
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.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000494:pharmacology; D001665:Binding Sites; D002857:Chromium / Q000494:pharmacology*; D006593:Hexokinase / Q000378:metabolism; D046911:Macromolecular Substances; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D046911:Macromolecular Substances; D002857:Chromium; D000255:Adenosine Triphosphate; D006593:Hexokinase