大肠杆菌细胞壁肽聚糖合成过程中的两种不同转肽反应。
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
作者信息
Kraus W, Höltje J V
出版信息
J Bacteriol. 1987 Jul;169(7):3099-103. doi: 10.1128/jb.169.7.3099-3103.1987.
Abstract
Murein synthesized in ether-permeabilized cells of Escherichia coli deficient in individual penicillin-binding proteins (PBPs) and in the presence of certain beta-lactam antibiotics was analyzed by high-pressure liquid chromatography separation of the muramidase split products. PBP 1b was found to to be the major murein synthesizing activity that was poorly compensated for by PBP 1a. A PBP 2 mutant as well as mecillinam-inhibited cells showed increased activity in the formation of oligomeric muropeptides as well as UDP-muramylpeptidyl-linked muropeptides, the reaction products of transpeptidation, bypassing the lipid intermediate. In contrast, penicillin G and furazlocillin severely inhibited these reactions but stimulated normal dimer production. It is concluded that two distinct transpeptidases exist in E. coli: one, highly sensitive to penicillin G and furazlocillin, catalyzes the formation of hyper-cross-linked muropeptides, and a second one, quite resistant to these antibiotics, synthesizes muropeptide dimers.
摘要
在存在某些β-内酰胺抗生素的情况下，对缺乏单个青霉素结合蛋白（PBPs）的大肠杆菌经乙醚通透化处理的细胞中合成的胞壁质，通过对溶菌酶裂解产物进行高压液相色谱分离来分析。发现PBP 1b是主要的胞壁质合成活性，PBP 1a对其补偿作用较差。PBP 2突变体以及被美西林抑制的细胞在形成寡聚肽聚糖以及UDP-胞壁酰肽基连接的肽聚糖（转肽反应产物）方面表现出增加的活性，绕过了脂质中间体。相反，青霉素G和呋脲苄青霉素严重抑制这些反应，但刺激正常二聚体的产生。得出的结论是，大肠杆菌中存在两种不同的转肽酶：一种对青霉素G和呋脲苄青霉素高度敏感，催化高度交联的肽聚糖的形成；另一种对这些抗生素相当耐药，合成肽聚糖二聚体。
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本文引用的文献
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Formation of hyper-crosslinked peptidoglycan with multiple crosslinkages by a penicillin-binding protein, 1A, of Escherichia coli.大肠杆菌青霉素结合蛋白1A形成具有多个交联的超交联肽聚糖。
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Molecular divergence of a major peptidoglycan synthetase with transglycosylase-transpeptidase activities in Escherichia coli --- penicillin-binding protein 1Bs.大肠杆菌中具有转糖基酶-转肽酶活性的主要肽聚糖合成酶——青霉素结合蛋白1Bs的分子差异
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