龙虾加夫基菌中的LD-羧肽酶活性。某些β-内酰胺抗生素对细胞壁结合肽聚糖形成作用的靶点。 - Suppr

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The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of certain beta-lactam antibiotics on the formation of wall-bound peptidoglycan.

作者信息

Hammes W P, Seidel H

出版信息

Eur J Biochem. 1978 Nov 15;91(2):509-15. doi: 10.1111/j.1432-1033.1978.tb12704.x.

DOI:10.1111/j.1432-1033.1978.tb12704.x

PMID:729580

Abstract

摘要

相似文献

The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of certain beta-lactam antibiotics on the formation of wall-bound peptidoglycan.龙虾加夫基菌中的LD-羧肽酶活性。某些β-内酰胺抗生素对细胞壁结合肽聚糖形成作用的靶点。

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引用本文的文献

Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.SxxK超家族酰基转移酶的生物化学和比较基因组学为分枝杆菌的矛盾现象提供了线索：存在对青霉素敏感的靶蛋白，但青霉素作为治疗剂却缺乏有效性。

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LD-carboxypeptidase activity in Escherichia coli. I. The LD-carboxypeptidase activity in ether treated cells.大肠杆菌中的亮氨酸脱氢酶羧肽酶活性。I. 经乙醚处理的细胞中的亮氨酸脱氢酶羧肽酶活性。

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Purification of a nocardicin A-sensitive LD-carboxypeptidase from Escherichia coli by affinity chromatography.通过亲和层析法从大肠杆菌中纯化对诺卡菌素A敏感的LD-羧肽酶。

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