Engineering of Peptide Synthetases

Peptide synthetases are large enzymatic complexes that catalyze the synthesis of biologically active peptides in microorganisms and fungi and typically have an unusual structure and sequence. Peptide synthetases have recently been engineered to modify the substrate specificity to produce peptides of...

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Bibliographic Details
Published in:The Journal of biological chemistry 1997-10, Vol.272 (40), p.25304-25309
Main Authors: de Ferra, Francesca, Rodriguez, Francesco, Tortora, Ornella, Tosi, Claudio, Grandi, Guido
Format: Article
Language:English
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Summary:Peptide synthetases are large enzymatic complexes that catalyze the synthesis of biologically active peptides in microorganisms and fungi and typically have an unusual structure and sequence. Peptide synthetases have recently been engineered to modify the substrate specificity to produce peptides of a new sequence. In this study we show that surfactin synthetase can also be modified by moving the carboxyl-terminal intrinsic thioesterase region to the end of the internal amino acid binding domains, thus generating strains that produce new truncated peptides of the predicted sequence. Omission of the thioesterase domain results in nonproducing strains, thus showing the essential role of this region and the possibility of obtaining peptides of different lengths by genetic engineering. Secretion of the peptides depends on the presence of a functionalsfp gene.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.272.40.25304