Ostrovtsova S A, Strumilo S A
Laboratory of Enzymology and Biotechnology, Institute of Biochemistry, Academy of Sciences of the Byelorussian SSR, Grodno.
Biomed Biochim Acta. 1990;49(6):515-7.
Adenosine diphosphate (ADP) increases the activity of the highly purified 2-oxoglutarate dehydrogenase complex (OGDC) from human heart. The degree of activation is higher at low 2-oxoglutarate concentrations. The OGDC-catalyzed reaction rate versus ADP concentration curve is S-shaped at unsaturating substrate concentration. This is a catalytic attribute of cooperativity of the sites for binding of the allosteric effector ADP.
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