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本文引用的文献

1
The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction.硫链丝菌素A色氨酸甲基转移酶TsrM催化一种依赖钴胺素(II)的甲基转移反应。
Nat Commun. 2015 Oct 12;6:8377. doi: 10.1038/ncomms9377.
2
Genomes to natural products PRediction Informatics for Secondary Metabolomes (PRISM).基因组到天然产物的次生代谢产物预测信息学(PRISM)。
Nucleic Acids Res. 2015 Nov 16;43(20):9645-62. doi: 10.1093/nar/gkv1012. Epub 2015 Oct 5.
3
Streptocollin, a Type IV Lanthipeptide Produced by Streptomyces collinus Tü 365.链霉菌素,由浅蓝链霉菌Tü 365产生的一种IV型羊毛硫肽。
Chembiochem. 2015 Dec;16(18):2615-23. doi: 10.1002/cbic.201500377. Epub 2015 Nov 6.
4
Chaxapeptin, a Lasso Peptide from Extremotolerant Streptomyces leeuwenhoekii Strain C58 from the Hyperarid Atacama Desert.查沙肽,一种源自超干旱阿塔卡马沙漠的耐极端环境李氏链霉菌菌株C58的套索肽。
J Org Chem. 2015 Oct 16;80(20):10252-60. doi: 10.1021/acs.joc.5b01878. Epub 2015 Sep 24.
5
Post-translational Introduction of D-Alanine into Ribosomally Synthesized Peptides by the Dehydroalanine Reductase NpnJ.脱氢丙氨酸还原酶NpnJ将D-丙氨酸进行翻译后引入核糖体合成的肽中。
J Am Chem Soc. 2015 Oct 7;137(39):12426-9. doi: 10.1021/jacs.5b05207. Epub 2015 Sep 24.
6
Characterization of Sviceucin from Streptomyces Provides Insight into Enzyme Exchangeability and Disulfide Bond Formation in Lasso Peptides.来自链霉菌的Sviceucin的特性研究为套索肽中的酶可交换性和二硫键形成提供了见解。
ACS Chem Biol. 2015 Nov 20;10(11):2641-9. doi: 10.1021/acschembio.5b00584. Epub 2015 Sep 21.
7
The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold.肠球菌溶血素合成酶具有意想不到的脂质激酶折叠结构。
Elife. 2015 Jul 30;4:e07607. doi: 10.7554/eLife.07607.
8
Pinensins: the first antifungal lantibiotics.松烯素:首个抗真菌的细菌素。
Angew Chem Int Ed Engl. 2015 Sep 14;54(38):11254-8. doi: 10.1002/anie.201500927. Epub 2015 Jul 24.
9
Thiopeptide Antibiotics Exhibit a Dual Mode of Action against Intracellular Pathogens by Affecting Both Host and Microbe.硫肽类抗生素通过影响宿主和微生物对细胞内病原体呈现双重作用模式。
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10
Tryptophan Lyase (NosL): Mechanistic Insights from Substrate Analogues and Mutagenesis.色氨酸裂解酶(NosL):来自底物类似物和诱变的机制见解
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核糖体合成和翻译后修饰肽天然产物生物合成逻辑的新见解。

New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.

机构信息

Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

出版信息

Cell Chem Biol. 2016 Jan 21;23(1):31-44. doi: 10.1016/j.chembiol.2015.11.012.

DOI:10.1016/j.chembiol.2015.11.012
PMID:26933734
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4779184/
Abstract

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a large group of structurally diverse natural products. Their biological activities and unique biosynthetic pathways have sparked a growing interest in RiPPs. Furthermore, the relatively low genetic complexity associated with RiPP biosynthesis makes them excellent candidates for synthetic biology applications. This Review highlights recent developments in the understanding of the biosynthesis of several bacterial RiPP family members, the use of the RiPP biosynthetic machinery for generating novel macrocyclic peptides, and the implementation of tools designed to guide the discovery and characterization of novel RiPPs.

摘要

核糖体合成和翻译后修饰肽(RiPPs)是一大类结构多样的天然产物。它们的生物活性和独特的生物合成途径引起了人们对 RiPPs 的日益关注。此外,与 RiPP 生物合成相关的遗传复杂性相对较低,这使得它们成为合成生物学应用的优秀候选者。本文综述了近年来对几种细菌 RiPP 家族成员生物合成的理解、利用 RiPP 生物合成机制生成新型大环肽,以及实施旨在指导新型 RiPP 发现和表征的工具方面的最新进展。