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
Hauptverfasser:	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
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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