Evidence for involvement of arginyl residue at the catalytic site of penicillin acylase from Escherichia coli.
Incubation of penicillin acylase from Escherichia coli with phenylglyoxal or 2,3-butanedione results in enzyme inactivation. Both benzylpenicillin and phenylacetate protect the enzyme against the inactivation, indicating the presence of arginine at or near the catalytic site. The reactions follow pseudofirst order kinetics and the inactivation kinetics indicate the presence of a single essential arginine moiety.
Prabhune
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AA
Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
Sivaraman
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H
D001120:Arginine; D001665:Binding Sites; D003931:Diacetyl / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D010399:Penicillin Amidase / Q000378:metabolism*; D010400:Penicillin G / Q000494:pharmacology; D010648:Phenylacetates / Q000494:pharmacology; D010658:Phenylglyoxal / Q000494:pharmacology
D010648:Phenylacetates; D001120:Arginine; D010399:Penicillin Amidase; C025136:phenylacetic acid; D003931:Diacetyl; D010658:Phenylglyoxal; D010400:Penicillin G