从日本假单胞菌中分离的 B3 型金属β-内酰胺酶 PJM-1 的生化特性研究。
Biochemical Characterization of the Subclass B3 Metallo-β-Lactamase PJM-1 from Pseudoxanthomonas japonensis.
机构信息
Department of Microbiology and Infectious Disease, Toho University School of Medicine, Ota-ku, Tokyo, Japan.
出版信息
Antimicrob Agents Chemother. 2022 Sep 20;66(9):e0069122. doi: 10.1128/aac.00691-22. Epub 2022 Aug 9.
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 gene in 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.
摘要
新型 B3 金属β-内酰胺酶（MBL）PJM-1 在经常从环境中分离到的日本假单胞菌中的表达产物的生化特性已被确定。 基因中的 906bp 为种特异性 MBL 基因，PJM-1 具有 301 个预测的氨基酸，与 AIM-1 具有 81.8%的氨基酸同一性。 在本研究中，PJM-1 被重组表达和纯化。 PJM-1 对头孢他啶和头孢吡肟的催化活性较低，并且被 EDTA 强烈抑制。
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