从两株不相关的铜绿假单胞菌菌株和一株木糖氧化产碱杆菌菌株中检测到一种变异金属β-内酰胺酶IMP-10。
Detection of a variant metallo-beta-lactamase, IMP-10, from two unrelated strains of Pseudomonas aeruginosa and an alcaligenes xylosoxidans strain.
作者信息
Iyobe Shizuko, Kusadokoro Haruko, Takahashi Ayako, Yomoda Sachie, Okubo Toyoji, Nakamura Akio, O'Hara Koji
机构信息
Laboratory of Drug Resistance in Bacteria, Gunma University School of Medicine, Maebashi, Japan.
出版信息
Antimicrob Agents Chemother. 2002 Jun;46(6):2014-6. doi: 10.1128/AAC.46.6.2014-2016.2002.
Abstract
The gene bla(IMP-10) of a variant metallo-beta-lactamase, IMP-10, had a single base replacement of G by T at nucleotide 145, which led to an amino acid alteration of Val49 to Phe compared to the IMP-1 enzyme, indicating that IMP-10 was a point mutation derivative of IMP-1. Highly purified enzymes revealed that IMP-10 was different from IMP-1 in its extremely low hydrolyzing activities for penicillins, such as benzylpenicillin, ampicillin, and piperacillin.
摘要
一种变异金属β-内酰胺酶IMP-10的基因bla(IMP-10)在核苷酸145处发生了单个碱基G被T替换的情况，与IMP-1酶相比，这导致第49位氨基酸由缬氨酸变为苯丙氨酸，表明IMP-10是IMP-1的点突变衍生物。高纯度酶显示，IMP-10与IMP-1不同，它对青霉素（如苄青霉素、氨苄青霉素和哌拉西林）的水解活性极低。
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