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β-内酰胺抗生素与来自链霉菌R39的细胞外DD-羧肽酶-转肽酶之间的相互作用模式

Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase--transpeptidase from Streptomyces R39.

作者信息

Fuad N, Frère J M, Ghuysen J M, Duez C, Iwatsubo M

出版信息

Biochem J. 1976 Jun 1;155(3):623-9. doi: 10.1042/bj1550623.

DOI:10.1042/bj1550623
PMID:949323
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1172885/
Abstract

The exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39 is inhibited by beta-lactam antibiotics according to the same general scheme of reaction as the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. However, the values for the kinetic constants involved in the reaction are very different for the two enzymes and provide an explanation for the observation that the R39 enzyme is more sensitive to beta-lactam antibiotics than the R61 enzyme. Further, particular beta-lactams influence the kinetic constants to different extents depending on the source of the enzyme, so that a physical basis for the spectrum of antibiotic activity against particular enzyme systems is provided.

摘要

根据与链霉菌R61的胞外DD-羧肽酶-转肽酶相同的一般反应模式，链霉菌R39的胞外DD-羧肽酶-转肽酶受到β-内酰胺抗生素的抑制。然而，两种酶参与反应的动力学常数的值差异很大，这就解释了为什么R39酶比R61酶对β-内酰胺抗生素更敏感。此外，特定的β-内酰胺根据酶的来源不同程度地影响动力学常数，从而为针对特定酶系统的抗生素活性谱提供了物理基础。

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Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase--transpeptidase from Streptomyces R39.β-内酰胺抗生素与来自链霉菌R39的细胞外DD-羧肽酶-转肽酶之间的相互作用模式
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本文引用的文献

1
DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.链霉菌菌株R39、R61和K11中的DD-羧肽酶-转肽酶及β-内酰胺抗生素的杀伤位点
Antimicrob Agents Chemother. 1973 Feb;3(2):181-7. doi: 10.1128/AAC.3.2.181.
2
D-alanine carboxypeptidases of Bacillus stearothermophilus: solubilisation of particulate enzymes and mechanism of action of penicillin.嗜热脂肪芽孢杆菌的D-丙氨酸羧肽酶：颗粒酶的溶解及青霉素的作用机制
Biochim Biophys Acta. 1973 Apr 28;304(2):332-52. doi: 10.1016/0304-4165(73)90252-3.
3
Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.青霉素与细菌细胞的相互作用：青霉素结合蛋白和青霉素敏感酶。
Bacteriol Rev. 1974 Sep;38(3):291-335. doi: 10.1128/br.38.3.291-335.1974.
4
Binding of beta-lactam antibiotics to the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.β-内酰胺抗生素与链霉菌R39的胞外D-羧肽酶-转肽酶的结合。
Biochem J. 1974 Oct;143(1):241-9. doi: 10.1042/bj1430241.
5
Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.链霉菌R39胞外DD-羧肽酶-转肽酶的分子量、氨基酸组成及理化性质
Biochem J. 1974 Oct;143(1):233-40. doi: 10.1042/bj1430233.
6
Interaction between beta-lactam antibiotics and exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.β-内酰胺抗生素与链霉菌R61的胞外DD-羧肽酶-转肽酶之间的相互作用。
Eur J Biochem. 1974 Dec 16;50(1):203-14. doi: 10.1111/j.1432-1033.1974.tb03889.x.
7
D-alanine carboxypeptidase from Streptococcus faecalis.来自粪肠球菌的D-丙氨酸羧肽酶。
Biochem Biophys Res Commun. 1974 Apr 8;57(3):562-71. doi: 10.1016/0006-291x(74)90583-x.
8
D-alanine carboxypeptidase from Bacillus subtilis membranes. II. Interaction with penicillins and cephalosporins.来自枯草芽孢杆菌膜的D-丙氨酸羧肽酶。II. 与青霉素和头孢菌素的相互作用。
J Biol Chem. 1973 Oct 10;248(19):6767-71.
9
Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39.与链霉菌R61和R39的胞外DD-羧肽酶-转肽酶相互作用后苄青霉素的碎片化
Nature. 1975 Nov 13;258(5531):168-70. doi: 10.1038/258168a0.
10
Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics. A choice of models.来自链霉菌R61的胞外DD-羧肽酶-转肽酶与β-内酰胺抗生素之间相互作用的动力学。模型的选择。
Eur J Biochem. 1975 Sep 15;57(2):343-51. doi: 10.1111/j.1432-1033.1975.tb02307.x.