Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli.
Ethoxyformic anhydride was used to demonstrate the existence of a second important histidine in succinyl-CoA synthetase from Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important histidine per alpha beta catalytic unit. Data are presented suggesting that this residue and an important thiol group on the beta subunit (Collier, G., and Nishimura, J.S. (1978) J. Biol. Chem. 253, 4938-4943) interact with each other during catalysis. A mechanism of action involving these 2 residues is proposed for one of the partial reactions catalyzed by succinyl-CoA synthetase.
D001665:Binding Sites; D003066:Coenzyme A Ligases / Q000378:metabolism*; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D006639:Histidine; D007700:Kinetics; D010766:Phosphorylation; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet; D013389:Succinate-CoA Ligases / Q000378:metabolism*
D006639:Histidine; D003066:Coenzyme A Ligases; D013389:Succinate-CoA Ligases; D004047:Diethyl Pyrocarbonate