4.5 Article Proceedings Paper

Active-site residue, domain and module swaps in modular polyketide synthases

期刊

出版社

SPRINGER HEIDELBERG
DOI: 10.1007/s10295-003-0062-0

关键词

polyketide synthase; Streptomyces fradiae; tylosin; Saccharopolyspora erythraea; erythromycin; acyltransferase; docking domain

资金

  1. NIAID NIH HHS [1 R43 AI47567-01] Funding Source: Medline

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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.

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