The amino acid sequence of Staphylococcus aureus penicillinase.
The amino acid sequence of the penicillinase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) from Staphylococcus aureus strain PC1 was determined. The protein consists of a single polypeptide chain of 257 residues, and the sequence was determined by characterization of tryptic, chymotryptic, peptic and CNBr peptides, with some additional evidence from thermolysin and S. aureus proteinase peptides. A mistake in the preliminary report of the sequence is corrected; residues 113-116 are now thought to be -Lys-Lys-Val-Lys- rather than -Lys-Val-Lys-Lys-. Detailed evidence for the amino acid sequence has been deposited as Supplementary Publication SUP 50056 (91 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.
D000577:Amides / Q000032:analysis; D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D003488:Cyanogen Bromide; D004592:Electrophoresis, Starch Gel; D010405:Penicillinase / Q000032:analysis* / Q000302:isolation & purification; D010447:Peptide Hydrolases; D013211:Staphylococcus aureus / Q000201:enzymology*; D013774:Tetranitromethane
D000577:Amides; D003470:Culture Media; D010447:Peptide Hydrolases; D010405:Penicillinase; D013774:Tetranitromethane; D003488:Cyanogen Bromide