title: GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C β-Lactamase.
abstract: Nucleotides were effective in inhibiting the class C β-lactamase CMY-10. IMP was the most potent competitive inhibitor, with aKivalue 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.
authors.affiliation: Department of Chemistry & Nano Science, Ewha Womans University, Seoul, Republic of Korea.
authors.forename: Jung-Hyun
authors.initials: JH
authors.lastname: Na
authors.affiliation: Marine Biotechnology Research Center, Korea Institute of Ocean Science and Technology (KIOST), Ansan, Republic of Korea.
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: An
authors.affiliation: Department of Chemistry & Nano Science, Ewha Womans University, Seoul, Republic of Korea chajung@ewha.ac.kr.
authors.forename: Sun-Shin
authors.initials: SS
authors.lastname: Cha
mesh_terms: D020134:Catalytic Domain / Q000502:physiology; D021902:Enterobacter aerogenes / Q000201:enzymology* / Q000235:genetics; D006157:Guanosine Monophosphate / Q000737:chemistry*; D007291:Inosine Monophosphate / Q000737:chemistry*; D008826:Microbial Sensitivity Tests; D065093:beta-Lactamase Inhibitors / Q000737:chemistry*; D001618:beta-Lactamases / Q000378:metabolism*
chemical_list: D065093:beta-Lactamase Inhibitors; D007291:Inosine Monophosphate; D006157:Guanosine Monophosphate; C491822:CMY-10 beta-lactamase; D001618:beta-Lactamases
keywords: GMP; IMP; competitive inhibitor; β-lactamases