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Stability of Novel Siderophore Cephalosporin S-649266 against Clinically Relevant Carbapenemases.


ABSTRACT: To better understand the antibacterial activity of S-649266 against carbapenemase producers, its stability against clinically relevant carbapenemases was investigated. The catalytic efficiencies (kcat/Km) of IMP-1, VIM-2, and L1 for S-649266 were 0.0048, 0.0050, and 0.024 ?M(-1) s(-1), respectively, which were more than 260-fold lower than that for meropenem. Only slight hydrolysis of S-649266 against KPC-3 was observed. NDM-1 hydrolyzed meropenem 3-fold faster than S-649266 at 200 ?M.

SUBMITTER: Ito-Horiyama T 

PROVIDER: S-EPMC4914688 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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Stability of Novel Siderophore Cephalosporin S-649266 against Clinically Relevant Carbapenemases.

Ito-Horiyama Tsukasa T   Ishii Yoshikazu Y   Ito Akinobu A   Sato Takafumi T   Nakamura Rio R   Fukuhara Norio N   Tsuji Masakatsu M   Yamano Yoshinori Y   Yamaguchi Keizo K   Tateda Kazuhiro K  

Antimicrobial agents and chemotherapy 20160620 7


To better understand the antibacterial activity of S-649266 against carbapenemase producers, its stability against clinically relevant carbapenemases was investigated. The catalytic efficiencies (kcat/Km) of IMP-1, VIM-2, and L1 for S-649266 were 0.0048, 0.0050, and 0.024 μM(-1) s(-1), respectively, which were more than 260-fold lower than that for meropenem. Only slight hydrolysis of S-649266 against KPC-3 was observed. NDM-1 hydrolyzed meropenem 3-fold faster than S-649266 at 200 μM. ...[more]

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