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维罗纳气单胞菌温和生物变种中金属β-内酰胺酶ImiS的核苷酸和氨基酸序列

Nucleotide and amino acid sequences of the metallo-beta-lactamase, ImiS, from Aeromonas veronii bv. sobria.

作者信息

Walsh T R, Neville W A, Haran M H, Tolson D, Payne D J, Bateson J H, MacGowan A P, Bennett P M

机构信息

Bristol Centre for Antimicrobial Research and Evaluation, Department of Microbiology and Pathology, Medical School, University of Bristol, United Kingdom.

出版信息

Antimicrob Agents Chemother. 1998 Feb;42(2):436-9. doi: 10.1128/AAC.42.2.436.

DOI:10.1128/AAC.42.2.436
PMID:9527802
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC105430/
Abstract

The Aeromonas veronii bv. sobria metallo-beta-lactamase gene, imiS, was cloned. The imiS open reading frame extends for 762 bp and encodes a protein of 254 amino acids with a secreted modified protein of 227 amino acids and a predicted pI of 8.1. To confirm the predicted sequence, purified ImiS was digested and the resulting peptides were identified, yielding an identical sequence for ImiS, with 98% identity to CphA. Both possessed the putative active-site sequence Asn-Tyr-His-Thr-Asp at positions 88 to 92, which is unique to the Aeromonas metallo-beta-lactamases.

摘要

维罗纳气单胞菌温和生物变种的金属β-内酰胺酶基因imiS被克隆。imiS开放阅读框延伸762 bp,编码一个含254个氨基酸的蛋白质,其分泌型修饰蛋白含227个氨基酸,预测等电点为8.1。为确认预测序列,对纯化的ImiS进行酶切并鉴定所得肽段,结果显示ImiS序列与预测一致,与CphA的序列一致性为98%。两者在88至92位均具有推定的活性位点序列Asn-Tyr-His-Thr-Asp,这是气单胞菌金属β-内酰胺酶所特有的。

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