Essential arginine residues for catalytic and regulatory functions of alpha-ketoglutarate dehydrogenase from pigeon breast muscle.
The number of arginine residues of pigeon breast muscle alpha-ketoglutarate dehydrogenase modified by 2,3-butanedione and 2,4-pentanedione was determined. It was shown that two of the 40 arginine residues in the enzyme monomer (Mr = 86,000) are accessible to the action of dicarbonyl compounds and are functionally significant. The protective effect of alpha-ketoglutarate and ADP against enzyme modification by 2,3-butanedione suggests the participation of alpha-ketoglutarate dehydrogenase arginine residues in the binding of substrate and allosteric activator, ADP.
D000818:Animals; D001120:Arginine / Q000032:analysis / Q000378:metabolism*; D002384:Catalysis; D010856:Columbidae / Q000378:metabolism*; D003931:Diacetyl / Q000494:pharmacology; D066298:In Vitro Techniques; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007700:Kinetics; D008239:Lysine / Q000032:analysis; D009132:Muscles / Q000201:enzymology*; D010422:Pentanones / Q000494:pharmacology
D010422:Pentanones; C008790:acetylacetone; D001120:Arginine; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex; D003931:Diacetyl; D008239:Lysine