The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
Published 2015 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
Authors
Keywords
-
Journal
FEBS LETTERS
Volume 589, Issue 15, Pages 1802-1806
Publisher
Wiley
Online
2015-05-29
DOI
10.1016/j.febslet.2015.05.032
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Radical S-adenosylmethionine enzyme catalyzed thioether bond formation in sactipeptide biosynthesis
- (2013) Leif Flühe et al. CURRENT OPINION IN CHEMICAL BIOLOGY
- Two [4Fe-4S] Clusters Containing Radical SAM Enzyme SkfB Catalyze Thioether Bond Formation during the Maturation of the Sporulation Killing Factor
- (2013) Leif Flühe et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Distribution and Properties of the Genes Encoding the Biosynthesis of the Bacterial Cofactor, Pyrroloquinoline Quinone
- (2012) Yao-Qing Shen et al. BIOCHEMISTRY
- Biotin synthase: Insights into radical-mediated carbon–sulfur bond formation
- (2012) Corey J. Fugate et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- 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
- The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A
- (2012) Leif Flühe et al. Nature Chemical Biology
- The 3D Solution Structure of Thurincin H, a Bacteriocin with Four Sulfur to α-Carbon Crosslinks
- (2011) Clarissa S. Sit et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- 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
- The 3D Structure of Thuricin CD, a Two-Component Bacteriocin with Cysteine Sulfur to α-Carbon Cross-links
- (2011) Clarissa S. Sit et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily
- (2010) Stephen R. Wecksler et al. CHEMICAL COMMUNICATIONS
- CDD: a Conserved Domain Database for the functional annotation of proteins
- (2010) A. Marchler-Bauer et al. NUCLEIC ACIDS RESEARCH
- Imaging mass spectrometry of intraspecies metabolic exchange revealed the cannibalistic factors of Bacillus subtilis
- (2010) W.-T. Liu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile
- (2010) M. C. Rea et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Control of radical chemistry in the AdoMet radical enzymes
- (2009) Kaitlin S Duschene et al. CURRENT OPINION IN CHEMICAL BIOLOGY
- Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced byBacillus thuringiensisSF361
- (2009) Hyungjae Lee et al. FEMS MICROBIOLOGY LETTERS
- Isolation of a Variant of Subtilosin A with Hemolytic Activity
- (2009) T. Huang et al. JOURNAL OF BACTERIOLOGY
- The Radical SAM Superfamily
- (2008) Perry A. Frey et al. CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
- Site-directed, Ligase-Independent Mutagenesis (SLIM) for highly efficient mutagenesis of plasmids greater than 8kb
- (2008) Joyce Chiu et al. JOURNAL OF MICROBIOLOGICAL METHODS
- CDD: specific functional annotation with the Conserved Domain Database
- (2008) A. Marchler-Bauer et al. NUCLEIC ACIDS RESEARCH
- Spermicidal bacteriocins: Lacticin 3147 and subtilosin A
- (2007) Lara Silkin et al. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationPublish 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 More