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来自铜绿假单胞菌的DD-羧肽酶和肽聚糖转肽酶。

DD-carboxypeptidase and peptidoglycan transpeptidase from Pseudomonas aeruginosa.

作者信息

Presslitz J E, Ray V A

出版信息

Antimicrob Agents Chemother. 1975 May;7(5):578-81. doi: 10.1128/AAC.7.5.578.

Abstract

Peptidoglycan transpeptidase and dd-carboxypeptidase have been detected in isolated membranes of Pseudomonas aeruginosa. Cephalosporins and penicillins fail to inhibit the transpeptidase at concentrations as high as 100 mug/ml. dd-Carboxypeptidase, on the other hand, is sensitive to inhibition by beta-lactam antibiotics. The presence of dimethyl sulfoxide in the reaction mixture results in a twofold stimulation of peptidoglycan formation, whereas dd-carboxypeptidase is inhibited approximately 30%. Maximum stimulation of transpeptidase occurs in the presence of both dimethyl sulfoxide and a beta-lactum antibiotic. This is in sharp contrast to the transpeptidase from Escherichia coli, which is sensitive to inhibition by penicillins and cephalosporins.

摘要

在铜绿假单胞菌的分离膜中已检测到肽聚糖转肽酶和D-羧肽酶。头孢菌素和青霉素在高达100μg/ml的浓度下无法抑制转肽酶。另一方面,D-羧肽酶对β-内酰胺抗生素的抑制敏感。反应混合物中存在二甲基亚砜会使肽聚糖形成受到两倍的刺激,而D-羧肽酶则被抑制约30%。转肽酶在二甲基亚砜和β-内酰胺抗生素同时存在的情况下受到最大刺激。这与大肠杆菌的转肽酶形成鲜明对比,后者对青霉素和头孢菌素的抑制敏感。

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Mode of action of a structurally novel beta-lactam.一种结构新颖的β-内酰胺的作用模式。
Antimicrob Agents Chemother. 1978 Jul;14(1):144-50. doi: 10.1128/AAC.14.1.144.

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