PMID: 37912Jul 11, 1979

Subunit structure and kinetic properties of L-beta-hydroxy acid dehydrogenase of Drosophila

Biochimica Et Biophysica Acta
V J CannistraroT Chase


L-beta-hydroxyacid dehydrogeanse (L-gulonate:NAD+ 3-oxidoreductase, EC of Drosophila is made up of two non-identical subunits with molecular weights of 40 000 and 23 500. Michaelis constants calculated at saturating concentrations of the other substrate were 0.13 mM for NAD+, 0.85 mM for L-gulonate, 14.8 mM for L-beta-hydroxybutyrate; dissociation constants (Kia) were 2.8 mM for L-gulonate, 22 mM for L-beta-hydroxybutyrate. The maximum velocity with L-gulonate as substrate was ten-fold greater than with beta-hydroxybutyrate. As product inhibitors, both NADH and acetoacetate are competitive vs. both substrates, suggesting a rapid equilibrium random mechanism.


Jan 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·N Ramachandran, R F Colman
Jul 1, 1957·Archives of Biochemistry and Biophysics·A P GROLLMAN, A L LEHNINGER

Related Concepts

Carbohydrate Dehydrogenases
Drosophila melanogaster
3-Hydroxybutyrate Dehydrogenase
Sugar Acids

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