GMP and IMP are competitive inhibitors of CMY-10, an extended-spectrum class C β-lactamase

Jung Hyun Na; Young Jun An; Sun Shin Cha

doi:10.1128/AAC.00098-17

GMP and IMP are competitive inhibitors of CMY-10, an extended-spectrum class C β-lactamase

Jung Hyun Na, Young Jun An, Sun Shin Cha

Department of Chemistry & Nanoscience

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Nucleotides were effective in inhibiting the class C β-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a K_i 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.

Original language	English
Article number	e00098
Journal	Antimicrobial Agents and Chemotherapy
Volume	61
Issue number	5
DOIs	https://doi.org/10.1128/AAC.00098-17
State	Published - May 2017

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Publisher Copyright:
Copyright © 2017 American Society for Microbiology. All Rights Reserved.

Keywords

Competitive inhibitor
GMP
IMP
β-lactamases

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abstract = "Nucleotides were effective in inhibiting the class C β-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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AU - Na, Jung Hyun

AU - An, Young Jun

AU - Cha, Sun Shin

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N2 - Nucleotides were effective in inhibiting the class C β-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.

AB - Nucleotides were effective in inhibiting the class C β-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.

KW - Competitive inhibitor

KW - GMP

KW - IMP

KW - β-lactamases

UR - https://www.scopus.com/pages/publications/85018186854

U2 - 10.1128/AAC.00098-17

DO - 10.1128/AAC.00098-17

M3 - Article

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AN - SCOPUS:85018186854

SN - 0066-4804

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JO - Antimicrobial Agents and Chemotherapy

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IS - 5

M1 - e00098

ER -

GMP and IMP are competitive inhibitors of CMY-10, an extended-spectrum class C β-lactamase

Abstract

Bibliographical note

Keywords

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