Chemical modification of lysine and arginine residues of bovine heart 2-oxoglutarate dehydrogenase: effect on the enzyme activity and regulation.
Chemical modification of arginine and lysine residues of bovine heart 2-oxoglutarate dehydrogenase with phenylglyoxal and pyridoxal 5'-phosphate inactivated the enzyme, indicating the importance of these residues for the catalysis. Inactivation caused by pyridoxal 5'-phosphate was prevented in the presence of thiamine pyrophosphate and Mg2+ allowing the assumption that lysine residues participate in binding of the cofactor.
Institute of Biochemistry, National Academy of Sciences of Belarus, Grodno.
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Ostrovtsova
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000818:Animals; D001120:Arginine / Q000737:chemistry* / Q000502:physiology; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism* / Q000502:physiology; D007700:Kinetics; D008239:Lysine / Q000737:chemistry* / Q000502:physiology; D009206:Myocardium / Q000201:enzymology*; D010658:Phenylglyoxal / Q000494:pharmacology; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D013835:Thiamine Pyrophosphate / Q000378:metabolism; D013997:Time Factors
D004791:Enzyme Inhibitors; D011732:Pyridoxal Phosphate; D000244:Adenosine Diphosphate; D001120:Arginine; D007655:Ketoglutarate Dehydrogenase Complex; D008239:Lysine; D010658:Phenylglyoxal; D013835:Thiamine Pyrophosphate