Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage

Jesus Cortes, Kirsten H. Wiesmann, Gareth Roberts, Murray J. B. Brown, James Staunton, Peter F. Leadlay

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Macrocyclic polyketides exhibit an impressive range of medically useful activities, and there is great interest in manipulating the genes that govern their synthesis. The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain extension. The resulting mutant markedly accelerates formation of the predicted triketide lactone, compared to a control in which the repositioned domain is inactive. Repositioning of the cyclase should be generally useful for redirecting polyketide synthesis to obtain polyketides of specified chain lengths.
Original languageEnglish
Pages (from-to)1487-1489
Number of pages4
Issue number5216
Publication statusPublished - 9 Jun 1995


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