Active-site residue, domain and module swaps in modular polyketide synthases
Sequence comparisons of multiple acyltransferase (AT) domains from modular polyketide synthases (PKSs) have highlighted a correlation between a short sequence motif and the nature of the extender unit selected. When this motif was specifically altered in the bimodular model PKS DEBS1-TE of Saccharop...
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| Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2003-08, Vol.30 (8), p.489-494 |
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| container_title | Journal of industrial microbiology & biotechnology |
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| creator | DEL VECCHIO, Francesca PETKOVIC, Hrvoje KENDREW, Steven G LOW, Lindsey WILKINSON, Barrie LILL, Rachel CORTES, Jesus RUDD, Brian A. M STAUNTON, Jim LEADLAY, Peter F |
| description | Sequence comparisons of multiple acyltransferase (AT) domains from modular polyketide synthases (PKSs) have highlighted a correlation between a short sequence motif and the nature of the extender unit selected. When this motif was specifically altered in the bimodular model PKS DEBS1-TE of Saccharopolyspora erythraea, the products included triketide lactones in which acetate extension units had been incorporated instead of propionate units at the predicted positions. We also describe a cassette system for convenient construction of hybrid modular PKSs based on the tylosin PKS in Streptomyces fradiae and demonstrate its use in domain and module swaps. |
| doi_str_mv | 10.1007/s10295-003-0062-0 |
| format | Article |
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We also describe a cassette system for convenient construction of hybrid modular PKSs based on the tylosin PKS in Streptomyces fradiae and demonstrate its use in domain and module swaps.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-003-0062-0</identifier><identifier>PMID: 12811585</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Anti-Bacterial Agents - biosynthesis ; Bacteria ; Binding Sites ; Biological and medical sciences ; Biotechnology ; Erythromycin - biosynthesis ; Fundamental and applied biological sciences. 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| identifier | ISSN: 1367-5435 |
| ispartof | Journal of industrial microbiology & biotechnology, 2003-08, Vol.30 (8), p.489-494 |
| issn | 1367-5435 1476-5535 |
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| source | Oxford Journals Open Access Collection; MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Anti-Bacterial Agents - biosynthesis Bacteria Binding Sites Biological and medical sciences Biotechnology Erythromycin - biosynthesis Fundamental and applied biological sciences. Psychology Industrial Microbiology Microbiology Multienzyme Complexes - chemistry Multienzyme Complexes - genetics Multienzyme Complexes - metabolism Mutagenesis, Site-Directed Protein Structure, Tertiary Saccharopolyspora - enzymology Saccharopolyspora - genetics Saccharopolyspora erythraea Streptomyces - enzymology Streptomyces - genetics Streptomyces fradiae Tylosin - biosynthesis |
| title | Active-site residue, domain and module swaps in modular polyketide synthases |
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