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Rational domain swaps reveal insights about chain length control by ketosynthase domains in fungal nonreducing polyketide synthases.

ABSTRACT: A facile genetic methodology in the filamentous fungus Aspergillus nidulans allowed exchange of the starter unit ACP transacylase (SAT) domain in the nonreduced polyketide synthase (NR-PKS) AfoE of the asperfuranone pathway with the SAT domains from 10 other NR-PKSs. The newly created hybrid with the NR-PKS AN3386 is able to accept a longer starter unit in place of the native substrate to create a novel aromatic polyketide in vivo.

SUBMITTER: Liu T

PROVIDER: S-EPMC3993715 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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Rational domain swaps reveal insights about chain length control by ketosynthase domains in fungal nonreducing polyketide synthases.

Liu Ting T Sanchez James F JF Chiang Yi-Ming YM Oakley Berl R BR Wang Clay C C CC

Organic letters 20140305 6

A facile genetic methodology in the filamentous fungus Aspergillus nidulans allowed exchange of the starter unit ACP transacylase (SAT) domain in the nonreduced polyketide synthase (NR-PKS) AfoE of the asperfuranone pathway with the SAT domains from 10 other NR-PKSs. The newly created hybrid with the NR-PKS AN3386 is able to accept a longer starter unit in place of the native substrate to create a novel aromatic polyketide in vivo. ...[more]

PMID: 24593241

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