Extended-spectrum properties of CMY-30, a Val211Gly mutant of CMY-2 cephalosporinase

Antimicrob Agents Chemother. 2009 Aug;53(8):3520-3. doi: 10.1128/AAC.00219-09. Epub 2009 May 26.

Abstract

CMY-30, a Val211Gly mutant of CMY-2 cephalosporinase, was derived by mutagenesis. The hydrolytic efficiency of CMY-30 against expanded-spectrum cephalosporins was higher than that of CMY-2 due to increased k(cat) values. Findings indicate a role of the Omega loop residue 211 in determining the substrate specificities of CMYs also corroborated by modeling studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aztreonam / metabolism
  • Ceftazidime / metabolism
  • Cephalosporins / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism
  • Protein Binding
  • Protein Structure, Secondary
  • beta-Lactamases* / chemistry
  • beta-Lactamases* / genetics
  • beta-Lactamases* / metabolism
  • beta-Lactams / metabolism

Substances

  • Cephalosporins
  • Escherichia coli Proteins
  • beta-Lactams
  • Ceftazidime
  • beta-lactamase CMY-2
  • beta-Lactamases
  • Aztreonam