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头孢匹林对生长中的枯草芽孢杆菌细胞中D-丙氨酸羧肽酶形成的影响。

Effect of cephapirin on formation of D-alanine carboxypeptidase in growing Bacillus subtilis cells.

作者信息

White J S, Astill M, Lawrence P J

出版信息

Antimicrob Agents Chemother. 1979 Feb;15(2):204-8. doi: 10.1128/AAC.15.2.204.

DOI:10.1128/AAC.15.2.204
PMID:106774
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC352633/
Abstract

Cephapirin was utilized to examine the interaction of beta-lactam antibiotics with growing Bacillus subtilis cells and the biological effects simultaneously produced. Saturation binding and quantitative cell death were observed at the cephapirin concentration of 0.1 mug/ml. Cephapirin bound to all penicillin-binding proteins except the d-alanine carboxypeptidase. A specific [(14)C]benzylpenicillin-binding assay was developed for the d-alanine carboxypeptidase. At the lowest saturating concentration of antibiotic (0.1 mug/ml), cephapirin inhibited formation of the d-alanine carboxypeptidase. Upon incubation with cephapirin, 18% of the membranous d-alanine carboxypeptidase was released into the media. The data suggest that beta-lactam antibiotics may affect the formation of bacterial cytoplasmic membranes in addition to their effect on cell wall synthesis.

摘要

头孢匹林被用于研究β-内酰胺类抗生素与生长中的枯草芽孢杆菌细胞的相互作用以及同时产生的生物学效应。在头孢匹林浓度为0.1微克/毫升时观察到饱和结合和定量细胞死亡。头孢匹林与除d-丙氨酸羧肽酶之外的所有青霉素结合蛋白结合。针对d-丙氨酸羧肽酶开发了一种特异性的[(14)C]苄青霉素结合测定法。在最低饱和抗生素浓度(0.1微克/毫升)下,头孢匹林抑制d-丙氨酸羧肽酶的形成。与头孢匹林孵育后,18%的膜结合d-丙氨酸羧肽酶释放到培养基中。数据表明,β-内酰胺类抗生素除了影响细胞壁合成外,还可能影响细菌细胞质膜的形成。

相似文献

1
Effect of cephapirin on formation of D-alanine carboxypeptidase in growing Bacillus subtilis cells.头孢匹林对生长中的枯草芽孢杆菌细胞中D-丙氨酸羧肽酶形成的影响。
Antimicrob Agents Chemother. 1979 Feb;15(2):204-8. doi: 10.1128/AAC.15.2.204.
2
The formation of functional penicillin-binding proteins.功能性青霉素结合蛋白的形成。
J Biol Chem. 1975 Aug 25;250(16):6578-85.
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Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and sequence homology to beta-lactamases.来自枯草芽孢杆菌青霉素敏感型D-丙氨酸羧肽酶的活性位点肽序列。青霉素作用机制及与β-内酰胺酶的序列同源性。
J Biol Chem. 1980 May 10;255(9):3964-76.
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Linear, uncross-linked peptidoglycan secreted by penicillin-treated Bacillus subtilis. Isolation and characterization as a substrate for penicillin-sensitive D-alanine carboxypeptidases.由青霉素处理的枯草芽孢杆菌分泌的线性、未交联肽聚糖。作为青霉素敏感的D-丙氨酸羧肽酶底物的分离与特性鉴定。
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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.
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Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.青霉素作用机制:青霉素和底物在两种细菌D-丙氨酸羧肽酶中与同一个活性位点丝氨酸共价结合。
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Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis.青霉素和头孢菌素对D-丙氨酸羧肽酶的失活作用在枯草芽孢杆菌中并不致命。
Proc Natl Acad Sci U S A. 1971 Nov;68(11):2814-7. doi: 10.1073/pnas.68.11.2814.
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A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking D-alanine carboxypeptidase IA.一种青霉素结合蛋白5有缺陷且缺乏D-丙氨酸羧肽酶IA的大肠杆菌突变体。
J Bacteriol. 1980 Jul;143(1):531-4. doi: 10.1128/jb.143.1.531-534.1980.
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Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.从枯草芽孢杆菌的D-丙氨酸羧肽酶中分离青霉素结合肽。
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12. doi: 10.1073/pnas.74.3.1009.

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本文引用的文献

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Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
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Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44.大肠杆菌K12菌株44中参与细胞壁肽交联的酶对氨苄青霉素和头孢菌素的敏感性。
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Five penicillin-binding components occur in Bacillus subtilis membranes.枯草芽孢杆菌膜中存在五种青霉素结合成分。
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Penicillin: reversible inhibition of forespore septum development in Bacillus megaterium cells.青霉素:对巨大芽孢杆菌细胞中前芽孢隔膜发育的可逆抑制作用。
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