| Structural highlights
Function
BLC10_KLEAE Class C beta-lactamase which confers resistance to penicillins and cephalosporins (PubMed:15383166). Has benzylpenicillin-, ceftazidime-, nitrocefin- and imipenem-hydrolyzing activity (PubMed:16677302, PubMed:28242658).[1] [2] [3]
Publication Abstract from PubMed
Nucleotides were effective in inhibiting the class C beta-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a Ki value of 16.2 muM. 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.
GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase.,Na JH, An YJ, Cha SS Antimicrob Agents Chemother. 2017 Apr 24;61(5). pii: e00098-17. doi:, 10.1128/AAC.00098-17. Print 2017 May. PMID:28242658[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee JH, Jung HI, Jung JH, Park JS, Ahn JB, Jeong SH, Jeong BC, Lee JH, Lee SH. Dissemination of transferable AmpC-type beta-lactamase (CMY-10) in a Korean hospital. Microb Drug Resist. 2004 Fall;10(3):224-30. PMID:15383166 doi:10.1089/mdr.2004.10.224
- ↑ Kim JY, Jung HI, An YJ, Lee JH, Kim SJ, Jeong SH, Lee KJ, Suh PG, Lee HS, Lee SH, Cha SS. Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase. Mol Microbiol. 2006 May;60(4):907-16. PMID:16677302 doi:10.1111/j.1365-2958.2006.05146.x
- ↑ Na JH, An YJ, Cha SS. GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase. Antimicrob Agents Chemother. 2017 Apr 24;61(5). pii: e00098-17. doi:, 10.1128/AAC.00098-17. Print 2017 May. PMID:28242658 doi:https://dx.doi.org/10.1128/AAC.00098-17
- ↑ Na JH, An YJ, Cha SS. GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase. Antimicrob Agents Chemother. 2017 Apr 24;61(5). pii: e00098-17. doi:, 10.1128/AAC.00098-17. Print 2017 May. PMID:28242658 doi:https://dx.doi.org/10.1128/AAC.00098-17
|