Sequence of PSE-2 beta-lactamase | Zendy

Pentti Huovinen | Zendy; Saara Huovinen | Zendy; George A. Jacoby | Zendy

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Sequence of PSE-2 beta-lactamase

Author(s) -

Pentti Huovinen,

Saara 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.

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