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Comparative Study
. 1988 Apr 1;251(1):73-9.
doi: 10.1042/bj2510073.

Complete amino acid sequence of p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1)

M Barthélémy  1 , J Peduzzi, R Labia
Affiliations
Comparative Study

Complete amino acid sequence of p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1)

M Barthélémy et al. Biochem J. .

Abstract

The complete amino acid sequence of the p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1) was determined. The protein contains 265 residues. Peptides resulting from digestions with trypsin, Staphylococcus aureus V8 proteinase, chymotrypsin and Lys-C proteinase and cleavage with CNBr were separated and purified by using reverse-phase h.p.l.c. The amino acid sequence of each peptide was manually determined with the dimethylaminoazobenzene isothiocyanate/phenyl isothiocyanate double-coupling method. The primary structure of PIT-2 beta-lactamase was compared with those of two closely related enzymes, namely TEM-1 beta-lactamase and the beta-lactamase of Klebsiella pneumoniae strain LEN-1. The PIT-2 beta-lactamase amino acid sequence was strongly retained, with respectively 68% and 88% homology. Thus PIT-2 enzyme could represent an evolutionary step between a chromosomally encoded beta-lactamase and the plasmid-mediated TEM beta-lactamases.

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