Open AccessSequence of PSE-2 beta-lactamase
Author(s) -
Pentti Huovinen,
S Huovinen,
George A. Jacoby
Publication year - 1988
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.32.1.134
Subject(s) - carbenicillin , sequence (biology) , chemistry , beta lactamase , peptide sequence , hydrolysis , beta (programming language) , stereochemistry , enzyme , beta lactamase inhibitors , nucleotide , biochemistry , antibiotics , escherichia coli , ampicillin , computer science , gene , programming language
The nucleotide sequence of PSE-2 beta-lactamase, an enzyme that readily hydrolyzes both carbenicillin and oxacillin, has been determined. The deduced sequence of 266 amino acids contained 93 residues identical to those of OXA-2 beta-lactamase and the Ser-Thr-Phe-Lys tetrad also found in the active site of TEM-1 beta-lactamase.