title: Role of protein subunits in Proteus rettgeri penicillin G acylase.
abstract: Penicillin G acylase from Proteus rettgeri is an 80,000- to 90,000-dalton enzyme composed of two nonidentical subunits. Both subunits were required for enzymatic activity. The 65,000-dalton beta subunit contained a phenylmethylsulfonyl fluoride-sensitive residue required for enzymatic activity, and the 24,500-dalton alpha subunit contained the domain that imparts specificity for the penicillin side chain.
mesh_terms: D000581:Amidohydrolases / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D010399:Penicillin Amidase / Q000302:isolation & purification* / Q000378:metabolism; D011511:Proteus / Q000201:enzymology*
chemical_list: D046911:Macromolecular Substances; D000581:Amidohydrolases; D010399:Penicillin Amidase