Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall
Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall
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DOI：
10.1016/j.femsle.2005.08.009
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发表时间：
2005-10-15
影响因子：
2.1
通讯作者：
Markiewicz, Z
中科院分区：
文献类型：
--
作者：
Korsak, D;Vollmer, W;Markiewicz, Z
我们报告了青霉素结合蛋白 5 (PBP5) 结构基因 lmo2754 的克隆。我们还描述了 PBP5 的酶活性并表征了缺乏该活性的突变体。纯化的 PBP5 具有 DD-羧肽酶活性，可去除胞壁质五肽侧链的末端 D-丙氨酸残基。与二聚五肽化合物相比，它对低分子量单体五肽底物表现出更高的活性。类似地，PBP5 优先裂解高分子量胞壁质中存在的单体五肽。构建了缺乏功能性 PBP5 的单核细胞增生李斯特氏菌突变体。突变体的细胞是有活力的，表明该蛋白质对于生长是必需的，但生长较慢并且细胞壁增厚。 (C) 2005 年欧洲微生物学会联合会。由 Elsevier B.V. 出版。保留所有权利。
We report on the cloning of the structural gene for penicillin-binding protein 5 (PBP5), lmo2754. We also describe the enzymatic activity of PBP5 and characterize a mutant lacking this activity. Purified PBP5 has DD-carboxypeptidase activity, removing the terminal D-alanine residue from murein pentapeptide side chains. It shows higher activity against low molecular weight monomeric pentapeptide substrates compared to dimeric pentapeptide compound. Similarly, PBP5 preferentially cleaves monomeric pentapeptides present in high-molecular weight murein sacculi. A Listeria monocytogenes mutant lacking functional PBP5 was constructed. Cells of the mutant are viable, showing that the protein is dispensable for growth, but grow slower and have thickened cell walls. (C) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.