Single amino acid substitution between SHV-1 beta-lactamase and cefotaxime-hydrolyzing SHV-2 enzyme.
FEBS Lett
; 231(1): 217-20, 1988 Apr 11.
Article
em En
| MEDLINE
| ID: mdl-3129309
ABSTRACT
SHV-2 beta-lactamase was purified from an overproducing variant of a clinical isolate of Escherichia coli resistant to cefotaxime. Pure protein was digested by trypsin and Lys-C endoproteinase. Proteolytic peptides, isolated by reverse-phase HPLC, were submitted to manual Edman degradation and aligned by homology with the sequence of SHV-1 beta-lactamase. A putative amino acid sequence was deduced. Structural comparison revealed that SHV-2 differed from SHV-1 by only one amino acid, Gly----Ser, at position 213 of the mature protein.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Beta-Lactamases
/
Cefotaxima
/
Escherichia coli
/
Isoenzimas
Tipo de estudo:
Guideline
Idioma:
En
Ano de publicação:
1988
Tipo de documento:
Article