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Single amino acid substitution between SHV‐1 β‐lactamase and cefotaxime‐hydrolyzing SHV‐2 enzyme
Author(s) -
Barthélémy Michel,
Péduzzi Jean,
Ben Yaghlane Hasna,
Labia Roger
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80734-8
Subject(s) - edman degradation , cefotaxime , peptide sequence , escherichia coli , biochemistry , biology , enzyme , amino acid , trypsin , microbiology and biotechnology , antibiotics , gene
SHV‐2 β‐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 β‐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.