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嗜麦芽窄食单胞菌L-1金属β-内酰胺酶家族的分子异质性

Molecular heterogeneity of the L-1 metallo-beta-lactamase family from Stenotrophomonas maltophilia.

作者信息

Sanschagrin F, Dufresne J, Levesque R C

机构信息

Microbiologie Moléculaire et Génie des Protéines, Sciences de la Vie et de la Santé, Faculté de Médecine, Université Laval, Ste-Foy, Québec, Canada.

出版信息

Antimicrob Agents Chemother. 1998 May;42(5):1245-8. doi: 10.1128/AAC.42.5.1245.

DOI:10.1128/AAC.42.5.1245
PMID:9593158
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC105789/
Abstract

We have determined the nucleotide sequence of the blaS gene encoding the carbapenem-hydrolyzing L-1 beta-lactamase from Stenotrophomonas maltophilia GN12873. Analysis of the DNA and deduced amino acid sequences identified a product of 290 amino acids. Comparisons of the L-1 amino acid sequence with those of other zinc beta-lactamases showed 88.6% identity with the L-1 enzyme from S. maltophilia IID1275 and less than 20% identity with other class B metalloenzymes.

摘要

我们已经确定了编码嗜麦芽窄食单胞菌GN12873的碳青霉烯水解L-1β-内酰胺酶的blaS基因的核苷酸序列。对DNA和推导的氨基酸序列分析确定了一个由290个氨基酸组成的产物。将L-1氨基酸序列与其他锌β-内酰胺酶的序列进行比较，结果显示与嗜麦芽窄食单胞菌IID1275的L-1酶有88.6%的同一性，与其他B类金属酶的同一性低于20%。

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本文引用的文献

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Carbapenem-hydrolyzing beta-lactamases.碳青霉烯水解β-内酰胺酶
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