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Biochemical Characterization of the Subclass B3 Metallo-β-Lactamase PJM-1 from Pseudoxanthomonas japonensis.


ABSTRACT: Biochemical properties of the novel subclass B3 metallo-β-lactamase (MBL) PJM-1 expressed in Pseudoxanthomonas japonensis, which is often isolated from the environment, were determined. The 906-bp blaPJM-1 gene in P. japonensis is a species-specific MBL gene, and PJM, with 301 predicted amino acids, has 81.8% amino acid identity with AIM-1. In this study, PJM-1 was recombinantly expressed and purified. PJM-1 showed a low catalytic activity against ceftazidime and cefepime, and it was strongly inhibited by EDTA.

SUBMITTER: Yamada K 

PROVIDER: S-EPMC9487579 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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Biochemical Characterization of the Subclass B3 Metallo-β-Lactamase PJM-1 from Pseudoxanthomonas japonensis.

Yamada Kageto K   Ishii Yoshikazu Y   Tateda Kazuhiro K  

Antimicrobial agents and chemotherapy 20220809 9


Biochemical properties of the novel subclass B3 metallo-β-lactamase (MBL) PJM-1 expressed in Pseudoxanthomonas japonensis, which is often isolated from the environment, were determined. The 906-bp <i>bla</i><sub>PJM-1</sub> gene in <i>P. japonensis</i> is a species-specific MBL gene, and PJM, with 301 predicted amino acids, has 81.8% amino acid identity with AIM-1. In this study, PJM-1 was recombinantly expressed and purified. PJM-1 showed a low catalytic activity against ceftazidime and cefepim  ...[more]

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