The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2+) enzyme.

Suppr

超能文献

作者信息

Dideberg O, Joris B, Frere J M, Ghuysen J M, Weber G, Robaye R, Delbrouck J M, Roelandts I

出版信息

FEBS Lett. 1980 Aug 11;117(1):215-8. doi: 10.1016/0014-5793(80)80948-3.

DOI:10.1016/0014-5793(80)80948-3

PMID:7409167

Abstract

摘要

相似文献

The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2+) enzyme.

FEBS Lett. 1980 Aug 11;117(1):215-8. doi: 10.1016/0014-5793(80)80948-3.

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.

The exocellular beta-lactamase of Streptomyces albus G. Purification, properties and comparison with the exocellular DD-carboxypeptidase.白色链霉菌G的胞外β-内酰胺酶。纯化、性质及与胞外DD-羧肽酶的比较。

Biochem J. 1981 Jan 1;193(1):75-82. doi: 10.1042/bj1930075.

On the DD-carboxypeptidase enzyme system of Streptomyces strain K15.关于链霉菌K15菌株的DD-羧肽酶酶系统。

Eur J Biochem. 1981 Apr;115(3):579-84. doi: 10.1111/j.1432-1033.1981.tb06242.x.

Fragmentation of penicillin catalysed by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces strain r61. Isotopic study of hydrogen fixation on carbon 6.

FEBS Lett. 1978 Apr 1;88(1):147-50. doi: 10.1016/0014-5793(78)80628-0.

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.

The peptidoglycan crosslinking enzyme system in Streptomyces strains R61, K15 and rimosus.

Eur J Biochem. 1977 Nov 15;81(1):19-28. doi: 10.1111/j.1432-1033.1977.tb11922.x.

The 4.5 A resolution structure analysis of the exocellular DD-carboxypeptidase of Streptomyces albus G.

FEBS Lett. 1980 Aug 11;117(1):212-4. doi: 10.1016/0014-5793(80)80947-1.

Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxy-peptidase-transpeptidase from Streptomyces R61.

FEBS Lett. 1976 Nov;70(1):257-60. doi: 10.1016/0014-5793(76)80770-3.

Chemical modifications of the active site of Streptomyces R61 DD-carboxypeptidase.

Eur J Biochem. 1981 Mar 16;115(1):53-7. doi: 10.1111/j.1432-1033.1981.tb06196.x.

引用本文的文献

Characterization of VldE (Spr1875), a Pneumococcal Two-State l,d-Endopeptidase with a Four-Zinc Cluster in the Active Site.VldE（Spr1875）的特性研究，一种肺炎球菌双态L,D-内肽酶，其活性位点含有四锌簇。

ACS Catal. 2024 Dec 11;14(24):18786-18798. doi: 10.1021/acscatal.4c05090. eCollection 2024 Dec 20.

Neisseria gonorrhoeae penicillin-binding protein 3 demonstrates a pronounced preference for N(epsilon)-acylated substrates.淋病奈瑟菌青霉素结合蛋白3对N（ε）-酰化底物表现出明显的偏好。

Biochemistry. 2009 Jun 23;48(24):5731-7. doi: 10.1021/bi9003099.

Molecular cloning, sequence analysis, and characterization of a penicillin-resistant DD-carboxypeptidase of Myxococcus xanthus.

J Bacteriol. 1999 Aug;181(15):4696-9. doi: 10.1128/JB.181.15.4696-4699.1999.

Antibiotic resistance in pathogenic and producing bacteria, with special reference to beta-lactam antibiotics.致病细菌和产抗生素细菌中的抗生素耐药性，特别提及β-内酰胺类抗生素。

Microbiol Rev. 1981 Dec;45(4):591-619. doi: 10.1128/mr.45.4.591-619.1981.

Interactions between non-classical beta-lactam compounds and the beta-lactamases of Actinomadura R39 and Streptomyces albus G.非经典β-内酰胺化合物与马杜拉放线菌R39和白色链霉菌G的β-内酰胺酶之间的相互作用

Biochem J. 1981 Oct 1;199(1):137-43. doi: 10.1042/bj1990137.

Biochem J. 1981 Jan 1;193(1):75-82. doi: 10.1042/bj1930075.

Active-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G.针对白色链霉菌G含锌D-丙氨酰-D-丙氨酸裂解羧肽酶活性位点的抑制剂

Biochem J. 1984 May 1;219(3):763-72. doi: 10.1042/bj2190763.

Interaction between non-classical beta-lactam compounds and the Zn2+-containing G and serine R61 and R39 D-alanyl-D-alanine peptidases.非经典β-内酰胺化合物与含锌的G型和丝氨酸R61及R39 D-丙氨酰-D-丙氨酸肽酶之间的相互作用。

Biochem J. 1981 Oct 1;199(1):129-36. doi: 10.1042/bj1990129.

文献AI研究员

20分钟写一篇综述，助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型，支持多种主流文档格式。

立即体验