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Extended-spectrum properties of CMY-30, a Val211Gly mutant of CMY-2 cephalosporinase.
Kotsakis, Stathis D; Papagiannitsis, Costas C; Tzelepi, Eva; Tzouvelekis, Leonidas S; Miriagou, Vivi.
Afiliação
  • Kotsakis SD; Laboratory of Bacteriology, Hellenic Pasteur Institute, Vas. Sofias 127, Athens 11521, Greece.
Antimicrob Agents Chemother ; 53(8): 3520-3, 2009 Aug.
Article em En | MEDLINE | ID: mdl-19470510
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.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Beta-Lactamases / Cefalosporinas / Proteínas de Escherichia coli Idioma: En Ano de publicação: 2009 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Beta-Lactamases / Cefalosporinas / Proteínas de Escherichia coli Idioma: En Ano de publicação: 2009 Tipo de documento: Article