title: Engineering of an "unnatural" natural product by swapping polyketide synthase domains in Aspergillus nidulans.
abstract: An StcA-AfoE hybrid polyketide synthase (PKS), generated by swapping the AfoE (asperfuranone biosynthesis) SAT domain with the StcA (sterigmatocystin biosynthesis) SAT domian, produced a major new metabolite with the same chain length as the native AfoE product. Structure elucidation allowed us to propose a likely pathway, and feeding studies supported the hypothesis that the chain length of PKS metabolites may be under precise control of KS and PT domains.
authors.affiliation: Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, California 90089, United States.
authors.forename: Ting
authors.initials: T
authors.lastname: Liu
authors.forename: Yi-Ming
authors.initials: YM
authors.lastname: Chiang
authors.forename: Amber D
authors.initials: AD
authors.lastname: Somoza
authors.forename: Berl R
authors.initials: BR
authors.lastname: Oakley
authors.forename: Clay C C
authors.initials: CC
authors.lastname: Wang
mesh_terms: D001233:Aspergillus nidulans / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D001572:Benzofurans / Q000737:chemistry / Q000378:metabolism; D001688:Biological Products / Q000737:chemistry / Q000378:metabolism*; D048630:Polyketide Synthases / Q000235:genetics* / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary
chemical_list: D001572:Benzofurans; D001688:Biological Products; C552682:asperfuranone; D048630:Polyketide Synthases