Change in alpha-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH

V I Bunik; O A Buneeva; V S Gomazkova

doi:10.1016/0014-5793(90)81166-l

Change in alpha-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH

FEBS Lett. 1990 Aug 20;269(1):252-4. doi: 10.1016/0014-5793(90)81166-l.

Authors

V I Bunik¹, O A Buneeva, V S Gomazkova

Affiliation

¹ Department of Biochemistry, Moscow State University, USSR.

PMID: 2117555
DOI: 10.1016/0014-5793(90)81166-l

Abstract

Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed.

MeSH terms

Allosteric Regulation
Animals
Columbidae
Diethyl Pyrocarbonate / pharmacology
Ketoglutarate Dehydrogenase Complex / metabolism*
Ketone Oxidoreductases / metabolism*
Macromolecular Substances
Muscles / enzymology
NAD / metabolism*
Oxidation-Reduction
Protein Conformation
Sulfhydryl Compounds
Thioctic Acid / analogs & derivatives*
Thioctic Acid / metabolism

Substances

Macromolecular Substances
Sulfhydryl Compounds
NAD
Thioctic Acid
dihydrolipoic acid
Ketone Oxidoreductases
Ketoglutarate Dehydrogenase Complex
Diethyl Pyrocarbonate