对从枯草芽孢杆菌膜中纯化的青霉素敏感的D-丙氨酸羧肽酶进行有限的蛋白酶解。通过切割COOH末端膜锚产生活性水溶性片段。 - Suppr

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超能文献

Limited proteolysis of the penicillin-sensitive D-alanine carboxypeptidase purified from Bacillus subtilis membranes. Active water-soluble fragments generated by cleavage of a COOH-terminal membrane anchor.

作者信息

Waxman D J, Strominger J L

出版信息

J Biol Chem. 1981 Feb 25;256(4):2059-66.

PMID:6780558

Abstract

摘要

相似文献

Limited proteolysis of the penicillin-sensitive D-alanine carboxypeptidase purified from Bacillus subtilis membranes. Active water-soluble fragments generated by cleavage of a COOH-terminal membrane anchor.对从枯草芽孢杆菌膜中纯化的青霉素敏感的D-丙氨酸羧肽酶进行有限的蛋白酶解。通过切割COOH末端膜锚产生活性水溶性片段。

J Biol Chem. 1981 Feb 25;256(4):2059-66.

Cleavage of a COOH-terminal hydrophobic region from D-alanine carboxypeptidase, a penicillin-sensitive bacterial membrane enzyme. Characterization of active, water-soluble fragments.从D-丙氨酸羧肽酶（一种对青霉素敏感的细菌膜酶）上切割COOH末端疏水区域。活性水溶性片段的表征。

J Biol Chem. 1979 Jun 10;254(11):4863-75.

Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two Bacilli.从两种芽孢杆菌中纯化得到的一种青霉素敏感酶的COOH末端膜状片段的一级结构。

J Biol Chem. 1981 Feb 25;256(4):2067-77.

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.

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。

Proc Natl Acad Sci U S A. 1979 Jun;76(6):2730-4. doi: 10.1073/pnas.76.6.2730.

Proceedings: The molecular mechanism of action of beta-lactam antibiotics: the solution of an apparent paradox.会议论文：β-内酰胺类抗生素的分子作用机制：一个明显悖论的解决方案

Arch Int Physiol Biochim. 1975 Feb;83(1):184-6.

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。

J Biol Chem. 1980 Dec 10;255(23):11577-87.

The mechanism of action of penicillin. Penicillin acylates the active site of Bacillus stearothermophilus D-alanine carboxypeptidase.青霉素的作用机制。青霉素使嗜热脂肪芽孢杆菌D - 丙氨酸羧肽酶的活性位点发生酰化。

J Biol Chem. 1980 May 10;255(9):3977-86.

The sporulation-specific penicillin-binding protein 5a from Bacillus subtilis is a DD-carboxypeptidase in vitro.来自枯草芽孢杆菌的孢子形成特异性青霉素结合蛋白5a在体外是一种DD-羧肽酶。

Biochem J. 1985 Sep 15;230(3):825-8. doi: 10.1042/bj2300825.

Synthesis of peptidoglycan by high molecular weight penicillin-binding proteins of Bacillus subtilis and Bacillus stearothermophilus.枯草芽孢杆菌和嗜热脂肪芽孢杆菌的高分子量青霉素结合蛋白合成肽聚糖。

J Biol Chem. 1984 Feb 10;259(3):1483-90.

引用本文的文献

A statistical investigation of amphiphilic properties of C-terminally anchored peptidases.C末端锚定肽酶两亲性特性的统计研究。

Eur Biophys J. 2003 Nov;32(7):589-98. doi: 10.1007/s00249-003-0302-2. Epub 2003 Apr 30.

Domain organization of penicillin-binding protein 5 from Escherichia coli analysed by C-terminal truncation.通过C末端截短分析大肠杆菌青霉素结合蛋白5的结构域组织。

Biochem J. 1993 Jan 15;289 ( Pt 2)(Pt 2):593-8.

Stability and synthesis of the penicillin-binding proteins during sporulation.芽孢形成过程中青霉素结合蛋白的稳定性与合成

J Bacteriol. 1983 Nov;156(2):545-51. doi: 10.1128/jb.156.2.545-551.1983.

DNA sequence of the Escherichia coli tonB gene.大肠杆菌tonB基因的DNA序列。

Proc Natl Acad Sci U S A. 1983 Sep;80(17):5235-9. doi: 10.1073/pnas.80.17.5235.

A prokaryotic membrane anchor sequence: carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane.一种原核生物膜锚定序列：噬菌体f1基因III蛋白的羧基末端将其保留在膜中。

Proc Natl Acad Sci U S A. 1982 Sep;79(17):5200-4. doi: 10.1073/pnas.79.17.5200.

Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali.用碱提取的平肠球菌（屎肠球菌）ATCC 9790细胞壁相关DD-羧肽酶的性质

J Bacteriol. 1990 Jul;172(7):3718-24. doi: 10.1128/jb.172.7.3718-3724.1990.

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