Single amino acid substitution between SHV-1 beta-lactamase and cefotaxime-hydrolyzing SHV-2 enzyme

FEBS Lett. 1988 Apr 11;231(1):217-20. doi: 10.1016/0014-5793(88)80734-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cefotaxime / metabolism*
  • Escherichia coli / enzymology*
  • Glycine
  • Isoenzymes / genetics*
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism
  • Molecular Sequence Data
  • Serine
  • beta-Lactamases / genetics*
  • beta-Lactamases / isolation & purification
  • beta-Lactamases / metabolism


  • Isoenzymes
  • Serine
  • beta-Lactamases
  • Cefotaxime
  • Glycine