[Role of amino acid arginine residues of bacterial formate dehydrogenase].
Inactivation of NAD-dependent formate dehydrogenase by butandione-2,3 has been studied. The inactivation is shown to be due to specific modification of the arginine residues. The enzyme activity is completely abolished by modification of 17 arginine residues per enzyme molecule. Native formate dehydrogenase contains 50 arginine residues. The dependences of the enzyme inactivation rate on butandione and substrate concentrations and the pH profile of the inactivation have been investigated. Coenzymes (but not formate) protect the enzyme against inactivation. The enzyme activity is completely retained upon formation of a binary E-NAD complex and a ternary E-NAD-azide complex. Protection of one arginine residue per enzyme subunit is observed under formation of a ternary enzyme--inhibitor complex. The fole of the arginine residue in coenzyme binding is discussed.
D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001120:Arginine; D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D002074:Butanones / Q000494:pharmacology*; D003931:Diacetyl / Q000494:pharmacology*; D005560:Formate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D011485:Protein Binding
D000596:Amino Acids; D002074:Butanones; D001120:Arginine; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D003931:Diacetyl
Izuchenie roli aminokislotnykh ostatkov arginina bakterial'noĭ formiatdegidrogenazy.