Thiopeptide Antibiotic Biosynthesis

Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis parad...

Full description

Saved in:
Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2009-09, Vol.48 (37), p.6770-6773
Main Authors: Arndt, Hans-Dieter, Schoof, Sebastian, Lu, Jin-Yong
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anti-Bacterial Agents - biosynthesis
Anti-Bacterial Agents - chemistry
antibiotics
biosynthesis
Genes, Bacterial
Molecular Sequence Data
Multigene Family
natural products
Peptide Biosynthesis
Peptides, Cyclic - biosynthesis
Peptides, Cyclic - chemistry
ribosomal peptides
Sequence Alignment
Sequence Homology, Amino Acid
Sulfhydryl Compounds - chemistry
thiopeptides
Thiostrepton - biosynthesis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343
cites cdi_FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343
container_end_page 6773
container_issue 37
container_start_page 6770
container_title Angewandte Chemie (International ed.)
container_volume 48
creator Arndt, Hans-Dieter
Schoof, Sebastian
Lu, Jin-Yong
description Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis paradigms and are expected to inspire future discoveries in the chemistry and biology of peptide natural products.
doi_str_mv 10.1002/anie.200901808
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_734019666</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>734019666</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343</originalsourceid><addsrcrecordid>eNqF0b1PwkAYBvCL0Qiiq6OSODgV76v3MSJBICE4AGG8XNu3cgq09kqU_942JejmdO_we57hOYRuCe4RjOmT3TnoUYw1JgqrM9QmISUBk5KdVzdnLJAqJC105f175ZXC4hK1iA6ZUBi30cNi7bIc8tIl0O3vShe5rHRx99ll_rAr1-Cdv0YXqd14uDm-HbR8GS4G42D6OpoM-tMg5lioIFFUWExFSEHy0KqYRYRTLgSAZRoiqRTwREc65TFhNg2V1imNtGQ8Ippx1kGPTW9eZJ978KXZOh_DZmN3kO29qSAmWghRyV4j4yLzvoDU5IXb2uJgCDb1LqbexZx2qQJ3x-p9tIXklx-HqIBuwJfbwOGfOtOfTYZ_y4Mm63wJ36esLT6MkEyGZjUbmflKUjVmwtT-vvGpzYx9K5w3yznFhGEipKj_7gczvoVS</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>734019666</pqid></control><display><type>article</type><title>Thiopeptide Antibiotic Biosynthesis</title><source>Wiley-Blackwell Read &amp; Publish Collection</source><creator>Arndt, Hans-Dieter ; Schoof, Sebastian ; Lu, Jin-Yong</creator><creatorcontrib>Arndt, Hans-Dieter ; Schoof, Sebastian ; Lu, Jin-Yong</creatorcontrib><description>Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis paradigms and are expected to inspire future discoveries in the chemistry and biology of peptide natural products.</description><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.200901808</identifier><identifier>PMID: 19536800</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>Amino Acid Sequence ; Anti-Bacterial Agents - biosynthesis ; Anti-Bacterial Agents - chemistry ; antibiotics ; biosynthesis ; Genes, Bacterial ; Molecular Sequence Data ; Multigene Family ; natural products ; Peptide Biosynthesis ; Peptides, Cyclic - biosynthesis ; Peptides, Cyclic - chemistry ; ribosomal peptides ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sulfhydryl Compounds - chemistry ; thiopeptides ; Thiostrepton - biosynthesis</subject><ispartof>Angewandte Chemie (International ed.), 2009-09, Vol.48 (37), p.6770-6773</ispartof><rights>Copyright © 2009 WILEY‐VCH Verlag GmbH &amp; Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343</citedby><cites>FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19536800$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arndt, Hans-Dieter</creatorcontrib><creatorcontrib>Schoof, Sebastian</creatorcontrib><creatorcontrib>Lu, Jin-Yong</creatorcontrib><title>Thiopeptide Antibiotic Biosynthesis</title><title>Angewandte Chemie (International ed.)</title><addtitle>Angewandte Chemie International Edition</addtitle><description>Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis paradigms and are expected to inspire future discoveries in the chemistry and biology of peptide natural products.</description><subject>Amino Acid Sequence</subject><subject>Anti-Bacterial Agents - biosynthesis</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>antibiotics</subject><subject>biosynthesis</subject><subject>Genes, Bacterial</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>natural products</subject><subject>Peptide Biosynthesis</subject><subject>Peptides, Cyclic - biosynthesis</subject><subject>Peptides, Cyclic - chemistry</subject><subject>ribosomal peptides</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sulfhydryl Compounds - chemistry</subject><subject>thiopeptides</subject><subject>Thiostrepton - biosynthesis</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqF0b1PwkAYBvCL0Qiiq6OSODgV76v3MSJBICE4AGG8XNu3cgq09kqU_942JejmdO_we57hOYRuCe4RjOmT3TnoUYw1JgqrM9QmISUBk5KdVzdnLJAqJC105f175ZXC4hK1iA6ZUBi30cNi7bIc8tIl0O3vShe5rHRx99ll_rAr1-Cdv0YXqd14uDm-HbR8GS4G42D6OpoM-tMg5lioIFFUWExFSEHy0KqYRYRTLgSAZRoiqRTwREc65TFhNg2V1imNtGQ8Ippx1kGPTW9eZJ978KXZOh_DZmN3kO29qSAmWghRyV4j4yLzvoDU5IXb2uJgCDb1LqbexZx2qQJ3x-p9tIXklx-HqIBuwJfbwOGfOtOfTYZ_y4Mm63wJ36esLT6MkEyGZjUbmflKUjVmwtT-vvGpzYx9K5w3yznFhGEipKj_7gczvoVS</recordid><startdate>20090901</startdate><enddate>20090901</enddate><creator>Arndt, Hans-Dieter</creator><creator>Schoof, Sebastian</creator><creator>Lu, Jin-Yong</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20090901</creationdate><title>Thiopeptide Antibiotic Biosynthesis</title><author>Arndt, Hans-Dieter ; Schoof, Sebastian ; Lu, Jin-Yong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Anti-Bacterial Agents - biosynthesis</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>antibiotics</topic><topic>biosynthesis</topic><topic>Genes, Bacterial</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>natural products</topic><topic>Peptide Biosynthesis</topic><topic>Peptides, Cyclic - biosynthesis</topic><topic>Peptides, Cyclic - chemistry</topic><topic>ribosomal peptides</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sulfhydryl Compounds - chemistry</topic><topic>thiopeptides</topic><topic>Thiostrepton - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arndt, Hans-Dieter</creatorcontrib><creatorcontrib>Schoof, Sebastian</creatorcontrib><creatorcontrib>Lu, Jin-Yong</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Angewandte Chemie (International ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arndt, Hans-Dieter</au><au>Schoof, Sebastian</au><au>Lu, Jin-Yong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thiopeptide Antibiotic Biosynthesis</atitle><jtitle>Angewandte Chemie (International ed.)</jtitle><addtitle>Angewandte Chemie International Edition</addtitle><date>2009-09-01</date><risdate>2009</risdate><volume>48</volume><issue>37</issue><spage>6770</spage><epage>6773</epage><pages>6770-6773</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>Tailors at work: The structurally intriguing thiopeptide antibiotic natural products have been conclusively and universally shown to be biosynthesized from genetically encoded linear precursor peptides by novel tailoring enzymes. These unique findings challenge previously accepted biosynthesis paradigms and are expected to inspire future discoveries in the chemistry and biology of peptide natural products.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>19536800</pmid><doi>10.1002/anie.200901808</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1433-7851
ispartof Angewandte Chemie (International ed.), 2009-09, Vol.48 (37), p.6770-6773
issn 1433-7851
1521-3773
language eng
recordid cdi_proquest_miscellaneous_734019666
source Wiley-Blackwell Read & Publish Collection
subjects Amino Acid Sequence
Anti-Bacterial Agents - biosynthesis
Anti-Bacterial Agents - chemistry
antibiotics
biosynthesis
Genes, Bacterial
Molecular Sequence Data
Multigene Family
natural products
Peptide Biosynthesis
Peptides, Cyclic - biosynthesis
Peptides, Cyclic - chemistry
ribosomal peptides
Sequence Alignment
Sequence Homology, Amino Acid
Sulfhydryl Compounds - chemistry
thiopeptides
Thiostrepton - biosynthesis
title Thiopeptide Antibiotic Biosynthesis
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T05%3A13%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Thiopeptide%20Antibiotic%20Biosynthesis&rft.jtitle=Angewandte%20Chemie%20(International%20ed.)&rft.au=Arndt,%20Hans-Dieter&rft.date=2009-09-01&rft.volume=48&rft.issue=37&rft.spage=6770&rft.epage=6773&rft.pages=6770-6773&rft.issn=1433-7851&rft.eissn=1521-3773&rft_id=info:doi/10.1002/anie.200901808&rft_dat=%3Cproquest_cross%3E734019666%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4068-d826a02652e745a8c3b142466eea39eb788e4d9b9f4c13af5899f2b9734b19343%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=734019666&rft_id=info:pmid/19536800&rfr_iscdi=true