Demonstration That the RadicalS-Adenosylmethionine (SAM) Enzyme PqqE Catalyzesde NovoCarbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD
出版年份 2016 全文链接
标题
Demonstration That the RadicalS-Adenosylmethionine (SAM) Enzyme PqqE Catalyzesde NovoCarbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD
作者
关键词
-
出版物
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 17, Pages 8877-8884
出版商
American Society for Biochemistry & Molecular Biology (ASBMB)
发表日期
2016-03-10
DOI
10.1074/jbc.c115.699918
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Chemical and Biological Reduction of the Radical SAM Enzyme CPH4 Synthase
- (2015) Nathan A. Bruender et al. BIOCHEMISTRY
- Mössbauer spectroscopy of Fe/S proteins
- (2015) Maria-Eirini Pandelia et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
- (2015) Beata M. Wieckowski et al. FEBS LETTERS
- PqqE fromMethylobacterium extorquensAM1: a radicalS-adenosyl-l-methionine enzyme with an unusual tolerance to oxygen
- (2015) Natsaran Saichana et al. JOURNAL OF BIOCHEMISTRY
- PqqD Is a Novel Peptide Chaperone That Forms a Ternary Complex with the RadicalS-Adenosylmethionine Protein PqqE in the Pyrroloquinoline Quinone Biosynthetic Pathway
- (2015) John A. Latham et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Leading the way to RiPPs
- (2015) A James Link Nature Chemical Biology
- A prevalent peptide-binding domain guides ribosomal natural product biosynthesis
- (2015) Brandon J Burkhart et al. Nature Chemical Biology
- Structure and biosynthesis of a macrocyclic peptide containing an unprecedented lysine-to-tryptophan crosslink
- (2015) Kelsey R. Schramma et al. Nature Chemistry
- Radical S-Adenosylmethionine Enzymes
- (2014) Joan B. Broderick et al. CHEMICAL REVIEWS
- SPASM and Twitch Domains inS-Adenosylmethionine (SAM) Radical Enzymes
- (2014) Tsehai A. J. Grell et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Multistep, Eight-Electron Oxidation Catalyzed by the Cofactorless Oxidase, PqqC: Identification of Chemical Intermediates and Their Dependence on Molecular Oxygen
- (2013) Florence Bonnot et al. BIOCHEMISTRY
- Intrigues and Intricacies of the Biosynthetic Pathways for the Enzymatic Quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ
- (2013) Judith P. Klinman et al. CHEMICAL REVIEWS
- X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification
- (2013) P. J. Goldman et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Distribution and Properties of the Genes Encoding the Biosynthesis of the Bacterial Cofactor, Pyrroloquinoline Quinone
- (2012) Yao-Qing Shen et al. BIOCHEMISTRY
- Emerging themes in radical SAM chemistry
- (2012) Krista A Shisler et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature
- (2012) Paul G. Arnison et al. NATURAL PRODUCT REPORTS
- Biological Systems Discovery In Silico: Radical S-Adenosylmethionine Protein Families and Their Target Peptides for Posttranslational Modification
- (2011) D. H. Haft et al. JOURNAL OF BACTERIOLOGY
- A “Radical Dance” in Thiamin Biosynthesis: Mechanistic Analysis of the Bacterial Hydroxymethylpyrimidine Phosphate Synthase
- (2010) Abhishek Chatterjee et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Pyrroloquinoline Quinone Biogenesis: Demonstration That PqqE fromKlebsiella pneumoniaeIs a RadicalS-Adenosyl-l-methionine Enzyme
- (2009) Stephen R. Wecksler et al. BIOCHEMISTRY
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreFind the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
Search