title: Studies on the biosynthesis of epothilones: the PKS and Epothilone C/D monooxygenase.
abstract: Nonproducer mutants support the assumption that epothilones A and B are synthesized by the same polyketide synthase (PKS). The endproducts of the PKS, epothilones C and D, compete for the active site of a constitutively synthesized monooxygenase which is regulated by product inhibition. The postulated C-13 hydroxy-epothilones as direct precursors of epothilones C and D were not detected.
authors: GBF, Gesellschaft für Biotechnologische Forschung mbH, Abteilung Naturstoffbiologie, Braunschweig, Germany. kge@gbf.de
authors: K
authors: K
authors: Gerth
authors: H
authors: H
authors: Steinmetz
authors: G
authors: G
authors: Höfle
authors: H
authors: H
authors: Reichenbach
mesh_terms: D001665:Binding Sites; D034261:Epothilones; D004852:Epoxy Compounds / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009154:Mutation; D010105:Oxygenases / Q000378:metabolism*; D020560:Proteobacteria / Q000235:genetics / Q000378:metabolism; D013844:Thiazoles / Q000378:metabolism*
chemical_list: D034261:Epothilones; D004852:Epoxy Compounds; D009097:Multienzyme Complexes; D013844:Thiazoles; C093787:epothilone A; D010105:Oxygenases; C424924:epothilone C-D monooxygenase; C093788:epothilone B