Subunit interactions in yeast glyceraldehyde-3-phosphate dehydrogenase

Biochemistry
S C MockrinD E Koshland

Abstract

The spontaneous inactivation of yeast glyceraldehyde-3-phosphate dehydrogenase was found to fit a simple two-state model at pH 8.5 and 25 degrees. The first step is a relatively rapid dissociation of the tetramer to dimers with the equilibrium largely in favor of the tetramer. In the absence of NAD+ the dimer inactivates irreversibly. The apoenzyme is quite stable with a half-life for complete activity loss proportional to the square root of the enzyme concentration. Perturbances of the protein structure (by pH, ionic strength, and specific salts), which have no effect on the tetrameric state of the molecule, result in an alteration of the cooperativity of NAD+ binding, the reactivity of the active-site sulfhydryl group, and the catalytic activity of the enzyme. Covalent modification of two of the four active-site sulfhydryl groups has profound effects on the enzymic activity which are mediated by changes in the subunit interactions. Sedimentation analysis and hybridization studies indicate that the interaction between subunits remains strong after covalent modification. Under normal physiological and equilibrium dialysis conditions the protein is a tetramer. Equilibrium dialysis studies of NAD+ binding to the enzyme at pH 8.5 ...Continue Reading

Citations

Jan 1, 1980·Advances in Enzyme Regulation·N K NagradovaV I Muronetz
Jan 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·R E Gibson, S A Levin
Dec 7, 1979·Journal of Theoretical Biology·P Friedrich
Oct 4, 1976·Biochemical and Biophysical Research Communications·S McCaul, L D Byers
Mar 1, 1978·Archives of Biochemistry and Biophysics·L D Byers

Related Concepts

Striadyne
Cyanates
Glyceraldehyde-3-Phosphate Dehydrogenases
Hydrogen-Ion Concentration
NADH
Plasma Protein Binding Capacity
Protein Conformation
Protein Denaturation
Saccharomyces cerevisiae
Sodium Chloride, (24)NaCl

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