Genes Encoding Enzymes Responsible for Biosynthesis of L-Lyxose and Attachment of Eurekanate during Avilamycin Biosynthesis
The oligosaccharide antibiotic avilamycin A is composed of a polyketide-derived dichloroisoeverninic acid moiety attached to a heptasaccharide chain consisting of six hexoses and one unusual pentose moiety. We describe the generation of mutant strains of the avilamycin producer defective in differen...
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| Veröffentlicht in: | Chemistry & biology 2005-10, Vol.12 (10), p.1137-1143 |
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| creator | Hofmann, Carsten Boll, Raija Heitmann, Björn Hauser, Gerd Dürr, Clemens Frerich, Anke Weitnauer, Gabriele Glaser, Steffen J. Bechthold, Andreas |
| description | The oligosaccharide antibiotic avilamycin A is composed of a polyketide-derived dichloroisoeverninic acid moiety attached to a heptasaccharide chain consisting of six hexoses and one unusual pentose moiety. We describe the generation of mutant strains of the avilamycin producer defective in different sugar biosynthetic genes. Inactivation of two genes (
aviD and
aviE2) resulted in the breakdown of the avilamycin biosynthesis. In contrast, avilamycin production was not influenced in an
aviP mutant. Inactivation of
aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue. Finally, AviE2 was expressed in
Escherichia coli and the gene product was characterized biochemically. AviE2 was shown to convert UDP-D-glucuronic acid to UDP-D-xylose, indicating that the pentose residue of avilamycin A is derived from D-glucose and not from D-ribose. Here we report a UDP-D-glucuronic acid decarboxylase in actinomycetes. |
| doi_str_mv | 10.1016/j.chembiol.2005.08.016 |
| format | Article |
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aviD and
aviE2) resulted in the breakdown of the avilamycin biosynthesis. In contrast, avilamycin production was not influenced in an
aviP mutant. Inactivation of
aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue. Finally, AviE2 was expressed in
Escherichia coli and the gene product was characterized biochemically. AviE2 was shown to convert UDP-D-glucuronic acid to UDP-D-xylose, indicating that the pentose residue of avilamycin A is derived from D-glucose and not from D-ribose. Here we report a UDP-D-glucuronic acid decarboxylase in actinomycetes.</description><identifier>ISSN: 1074-5521</identifier><identifier>EISSN: 1879-1301</identifier><identifier>DOI: 10.1016/j.chembiol.2005.08.016</identifier><identifier>PMID: 16242656</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Actinobacteria - enzymology ; Carbohydrate Sequence ; Carboxy-Lyases - biosynthesis ; Carboxy-Lyases - genetics ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Glucose - metabolism ; Molecular Sequence Data ; Molecular Structure ; Oligosaccharides - analysis ; Oligosaccharides - biosynthesis ; Oligosaccharides - metabolism ; Pentoses - biosynthesis</subject><ispartof>Chemistry & biology, 2005-10, Vol.12 (10), p.1137-1143</ispartof><rights>2005 Elsevier Ltd</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c414t-ec54d243143d963b76fe79f927e40bd59b6ffa7ccda3bd87f76657c4912503433</citedby><cites>FETCH-LOGICAL-c414t-ec54d243143d963b76fe79f927e40bd59b6ffa7ccda3bd87f76657c4912503433</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.chembiol.2005.08.016$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16242656$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hofmann, Carsten</creatorcontrib><creatorcontrib>Boll, Raija</creatorcontrib><creatorcontrib>Heitmann, Björn</creatorcontrib><creatorcontrib>Hauser, Gerd</creatorcontrib><creatorcontrib>Dürr, Clemens</creatorcontrib><creatorcontrib>Frerich, Anke</creatorcontrib><creatorcontrib>Weitnauer, Gabriele</creatorcontrib><creatorcontrib>Glaser, Steffen J.</creatorcontrib><creatorcontrib>Bechthold, Andreas</creatorcontrib><title>Genes Encoding Enzymes Responsible for Biosynthesis of L-Lyxose and Attachment of Eurekanate during Avilamycin Biosynthesis</title><title>Chemistry & biology</title><addtitle>Chem Biol</addtitle><description>The oligosaccharide antibiotic avilamycin A is composed of a polyketide-derived dichloroisoeverninic acid moiety attached to a heptasaccharide chain consisting of six hexoses and one unusual pentose moiety. We describe the generation of mutant strains of the avilamycin producer defective in different sugar biosynthetic genes. Inactivation of two genes (
aviD and
aviE2) resulted in the breakdown of the avilamycin biosynthesis. In contrast, avilamycin production was not influenced in an
aviP mutant. Inactivation of
aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue. Finally, AviE2 was expressed in
Escherichia coli and the gene product was characterized biochemically. AviE2 was shown to convert UDP-D-glucuronic acid to UDP-D-xylose, indicating that the pentose residue of avilamycin A is derived from D-glucose and not from D-ribose. 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aviD and
aviE2) resulted in the breakdown of the avilamycin biosynthesis. In contrast, avilamycin production was not influenced in an
aviP mutant. Inactivation of
aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue. Finally, AviE2 was expressed in
Escherichia coli and the gene product was characterized biochemically. AviE2 was shown to convert UDP-D-glucuronic acid to UDP-D-xylose, indicating that the pentose residue of avilamycin A is derived from D-glucose and not from D-ribose. Here we report a UDP-D-glucuronic acid decarboxylase in actinomycetes.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>16242656</pmid><doi>10.1016/j.chembiol.2005.08.016</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present); Free Full-Text Journals in Chemistry |
| subjects | Actinobacteria - enzymology Carbohydrate Sequence Carboxy-Lyases - biosynthesis Carboxy-Lyases - genetics Escherichia coli - enzymology Escherichia coli - genetics Glucose - metabolism Molecular Sequence Data Molecular Structure Oligosaccharides - analysis Oligosaccharides - biosynthesis Oligosaccharides - metabolism Pentoses - biosynthesis |
| title | Genes Encoding Enzymes Responsible for Biosynthesis of L-Lyxose and Attachment of Eurekanate during Avilamycin Biosynthesis |
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