title: The Botrytis cinerea type III polyketide synthase shows unprecedented high catalytic efficiency toward long chain acyl-CoAs.
abstract: BPKS from Botrytis cinerea is a novel type III polyketide synthase that accepts C(4)-C(18) aliphatic acyl-CoAs and benzoyl-CoA as the starters to form pyrones, resorcylic acids and resorcinols through sequential condensation with malonyl-CoA. The catalytic efficiency (k(cat)/K(m)) of BPKS was 2.8 × 10(5) s(-1) M(-1) for palmitoyl-CoA, the highest ever reported. Substrate docking analyses addressed the unique features of BPKS such as its high activity and high specificity toward long chain acyl-CoAs.
authors.affiliation: Department of Chemical Engineering, Konkuk University, Seoul 143-701, Korea.
authors.forename: Marimuthu
authors.initials: M
authors.lastname: Jeya
authors.forename: Tae-Su
authors.initials: TS
authors.lastname: Kim
authors.forename: Manish Kumar
authors.initials: MK
authors.lastname: Tiwari
authors.forename: Jinglin
authors.initials: J
authors.lastname: Li
authors.forename: Huimin
authors.initials: H
authors.lastname: Zhao
authors.forename: Jung-Kul
authors.initials: JK
authors.lastname: Lee
mesh_terms: D000214:Acyl Coenzyme A / Q000378:metabolism*; D020171:Botrytis / Q000201:enzymology*; D002384:Catalysis; D005656:Fungal Proteins / Q000378:metabolism*; D048630:Polyketide Synthases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000214:Acyl Coenzyme A; D005656:Fungal Proteins; D048630:Polyketide Synthases