title: 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.
authors.affiliation: Department of Pharmacology and Pharmaceutical Sciences, University of Southern California, School of Pharmacy , Los Angeles, California 90089, United States.
authors.forename: Ting
authors.initials: T
authors.lastname: Liu
authors.forename: James F
authors.initials: JF
authors.lastname: Sanchez
authors.forename: Yi-Ming
authors.initials: YM
authors.lastname: Chiang
authors.forename: Berl R
authors.initials: BR
authors.lastname: Oakley
authors.forename: Clay C C
authors.initials: CC
authors.lastname: Wang
mesh_terms: D000217:Acyltransferases / Q000378:metabolism; D001233:Aspergillus nidulans / Q000201:enzymology* / Q000235:genetics; D001572:Benzofurans; D015394:Molecular Structure; D048630:Polyketide Synthases / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D001572:Benzofurans; C552682:asperfuranone; D048630:Polyketide Synthases; D000217:Acyltransferases