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Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589.

作者信息

Sato Masaru, Kirimura Kohtaro, Kino Kuniki

机构信息

Department of Applied Chemistry, School of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo, Japan.

出版信息

Biosci Biotechnol Biochem. 2006 Nov;70(11):2790-2. doi: 10.1271/bbb.60307. Epub 2006 Nov 7.

DOI:10.1271/bbb.60307
PMID:17090922
Abstract

D-Alanine-D-alanine ligase (Ddl) and its mutants maintain the biosynthesis of peptidoglycan, and the substrate specificity of Ddls partially affects the resistance mechanism of vancomycin-resistant enterococci. Through investigation of Ddls, Ddl from Thermotoga maritima ATCC 43589 showed novel characteristics, vis. thermostability up to 90 degrees C and broad substrate specificity toward 15 D-amino acids, particularly D-alanine, D-cysteine, and D-serine, in that order.

摘要

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引用本文的文献

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Global Association between Thermophilicity and Vancomycin Susceptibility in Bacteria.细菌嗜热性与万古霉素敏感性之间的全球关联
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The elucidation of the structure of Thermotoga maritima peptidoglycan reveals two novel types of cross-link.
嗜热栖热菌肽聚糖结构的阐明揭示了两种新型交联类型。
J Biol Chem. 2009 Aug 14;284(33):21856-21862. doi: 10.1074/jbc.M109.034363. Epub 2009 Jun 19.