PMID: 1218078Nov 1, 1975Paper

The amino acid sequence of Staphylococcus aureus penicillinase

The Biochemical Journal
R P Ambler

Abstract

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.

Citations

Jan 1, 1985·Critical Reviews in Microbiology·J M Frère, B Joris
Jun 26, 2008·Journal of Theoretical Biology·James T MurphyMarc Devocelle
Jul 1, 1980·European Journal of Biochemistry·M D JonesB F Clark
Jul 6, 2013·Journal of Infection and Chemotherapy : Official Journal of the Japan Society of Chemotherapy·Karen Bush
Jun 25, 2010·The Journal of Antimicrobial Chemotherapy·Richard Sykes
Apr 1, 1992·Journal of Molecular Evolution·R Kirby
Oct 4, 2015·Microbiology·Elizabeth A MuellerPatrick M Schlievert
Apr 1, 1979·International Journal of Peptide and Protein Research·P C Moews, J R Knox
Jun 27, 2007·Antimicrobial Agents and Chemotherapy·Anne Marie QueenanKaren Bush
Feb 20, 2020·Antimicrobial Agents and Chemotherapy·Lina P CarvajalJinnethe Reyes

Related Concepts

Amides
Molecular Sieve Chromatography
Ion-Exchange Chromatography Procedure
Cyanogen Bromide
Electrophoresis, Starch Gel
Exopenicillinase
Peptide Hydrolases
Staphylococcus aureus
Tetranitromethane

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