Biosynthesis of the erythromycin macrolactone and a rational approach for producing hybrid macrolides
The three eryA genes involved in the formation of the polyketide portion of the macrolide antibiotic erythromycin in Saccharopolyspora erythraea, appear to be organized in a single transcriptional unit on the basis of the results of gene disruption experiments. An insertion sequence-like element of...
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| Veröffentlicht in: | Gene 1992-06, Vol.115 (1), p.97-103 |
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| container_title | Gene |
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| creator | Donadio, Stefano Staver, Michael J. McAlpine, James B. Swanson, Susan J. Katz, Leonard |
| description | The three
eryA genes involved in the formation of the polyketide portion of the macrolide antibiotic erythromycin in
Saccharopolyspora erythraea, appear to be organized in a single transcriptional unit on the basis of the results of gene disruption experiments. An insertion sequence-like element of lower G + C content separates
eryAI from
eryAII. The organization of the enzymatic domains present in the
eryA-encoded multifunctional polypeptides, determined by computer-assisted analysis, is presented. This has enabled the determination of a putative dehydratase domain. A rational approach for producing novel macrolides by introducing selected changes in polyketide synthase genes is outlined. The isolation of a lactone intermediate resulting from an early synthesis step in macrolactone formation is also presented. |
| doi_str_mv | 10.1016/0378-1119(92)90546-2 |
| format | Article |
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Saccharopolyspora erythraea, appear to be organized in a single transcriptional unit on the basis of the results of gene disruption experiments. An insertion sequence-like element of lower G + C content separates
eryAI from
eryAII. The organization of the enzymatic domains present in the
eryA-encoded multifunctional polypeptides, determined by computer-assisted analysis, is presented. This has enabled the determination of a putative dehydratase domain. A rational approach for producing novel macrolides by introducing selected changes in polyketide synthase genes is outlined. The isolation of a lactone intermediate resulting from an early synthesis step in macrolactone formation is also presented.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/0378-1119(92)90546-2</identifier><identifier>PMID: 1612455</identifier><identifier>CODEN: GENED6</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Amino Acid Sequence ; antibiotics ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Erythromycin - biosynthesis ; fatty acid synthase ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; genetic engineering ; Genetic Engineering - methods ; Genetics ; Microbiology ; Molecular Sequence Data ; Multienzyme Complexes - genetics ; polyketide synthase ; Saccharopolyspora ; Saccharopolyspora - genetics ; Saccharopolyspora erythraea ; Streptomyces</subject><ispartof>Gene, 1992-06, Vol.115 (1), p.97-103</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-c1b3f1c577e04ec17ddabbda5edea5ca9f293030d6620e29506615d7d5e315a33</citedby><cites>FETCH-LOGICAL-c417t-c1b3f1c577e04ec17ddabbda5edea5ca9f293030d6620e29506615d7d5e315a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0378-1119(92)90546-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>309,310,314,780,784,789,790,3550,23930,23931,25140,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5336385$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1612455$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Donadio, Stefano</creatorcontrib><creatorcontrib>Staver, Michael J.</creatorcontrib><creatorcontrib>McAlpine, James B.</creatorcontrib><creatorcontrib>Swanson, Susan J.</creatorcontrib><creatorcontrib>Katz, Leonard</creatorcontrib><title>Biosynthesis of the erythromycin macrolactone and a rational approach for producing hybrid macrolides</title><title>Gene</title><addtitle>Gene</addtitle><description>The three
eryA genes involved in the formation of the polyketide portion of the macrolide antibiotic erythromycin in
Saccharopolyspora erythraea, appear to be organized in a single transcriptional unit on the basis of the results of gene disruption experiments. An insertion sequence-like element of lower G + C content separates
eryAI from
eryAII. The organization of the enzymatic domains present in the
eryA-encoded multifunctional polypeptides, determined by computer-assisted analysis, is presented. This has enabled the determination of a putative dehydratase domain. A rational approach for producing novel macrolides by introducing selected changes in polyketide synthase genes is outlined. The isolation of a lactone intermediate resulting from an early synthesis step in macrolactone formation is also presented.</description><subject>Amino Acid Sequence</subject><subject>antibiotics</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Erythromycin - biosynthesis</subject><subject>fatty acid synthase</subject><subject>Fundamental and applied biological sciences. 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eryA genes involved in the formation of the polyketide portion of the macrolide antibiotic erythromycin in
Saccharopolyspora erythraea, appear to be organized in a single transcriptional unit on the basis of the results of gene disruption experiments. An insertion sequence-like element of lower G + C content separates
eryAI from
eryAII. The organization of the enzymatic domains present in the
eryA-encoded multifunctional polypeptides, determined by computer-assisted analysis, is presented. This has enabled the determination of a putative dehydratase domain. A rational approach for producing novel macrolides by introducing selected changes in polyketide synthase genes is outlined. The isolation of a lactone intermediate resulting from an early synthesis step in macrolactone formation is also presented.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>1612455</pmid><doi>10.1016/0378-1119(92)90546-2</doi><tpages>7</tpages></addata></record> |
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| ispartof | Gene, 1992-06, Vol.115 (1), p.97-103 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence antibiotics Bacteriology Base Sequence Biological and medical sciences Erythromycin - biosynthesis fatty acid synthase Fundamental and applied biological sciences. Psychology Genes, Bacterial genetic engineering Genetic Engineering - methods Genetics Microbiology Molecular Sequence Data Multienzyme Complexes - genetics polyketide synthase Saccharopolyspora Saccharopolyspora - genetics Saccharopolyspora erythraea Streptomyces |
| title | Biosynthesis of the erythromycin macrolactone and a rational approach for producing hybrid macrolides |
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