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GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C ß-Lactamase.
Na, Jung-Hyun; An, Young Jun; Cha, Sun-Shin.
Afiliação
  • Na JH; Department of Chemistry & Nano Science, Ewha Womans University, Seoul, Republic of Korea.
  • An YJ; Marine Biotechnology Research Center, Korea Institute of Ocean Science and Technology (KIOST), Ansan, Republic of Korea.
  • Cha SS; Department of Chemistry & Nano Science, Ewha Womans University, Seoul, Republic of Korea chajung@ewha.ac.kr.
Article em En | MEDLINE | ID: mdl-28242658
Nucleotides were effective in inhibiting the class C ß-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a Ki value of 16.2 µM. The crystal structure of CMY-10 complexed with GMP or IMP revealed that nucleotides fit into the R2 subsite of the active site with a unique vertical binding mode where the phosphate group at one terminus is deeply bound in the subsite and the base at the other terminus faces the solvent.
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Texto completo: 1 Coleções: 01-internacional Contexto em Saúde: 3_ND Base de dados: MEDLINE Assunto principal: Beta-Lactamases / Guanosina Monofosfato / Enterobacter aerogenes / Inibidores de beta-Lactamases / Inosina Monofosfato Idioma: En Revista: Antimicrob Agents Chemother Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Contexto em Saúde: 3_ND Base de dados: MEDLINE Assunto principal: Beta-Lactamases / Guanosina Monofosfato / Enterobacter aerogenes / Inibidores de beta-Lactamases / Inosina Monofosfato Idioma: En Revista: Antimicrob Agents Chemother Ano de publicação: 2017 Tipo de documento: Article