C-o bond formation by polyketide synthases

Academic Article

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Overview

authors

• Kwon, H. J.
• Smith, W. C.
• Scharon, A. J.
• Hwang, S. H.
• Kurth, M. J.
• Shen, Ben

publication date

• August 2002

journal

• Science  Journal

abstract

• Polyketide synthases (PKSs) assemble the polyketide carbon backbone by sequential decarboxylative condensation of acyl coenzyme A (CoA) precursors, and the C-C bond-forming step in this process is catalyzed by the beta-ketoacyl synthase (KS) domain or subunit. Genetic and biochemical characterization of the nonactin biosynthesis gene cluster from Streptomyces griseus revealed two KSs, NonJ and NonK, that are highly homologous to known KSs but catalyze sequential condensation of the acyl CoA substrates by forming C-O rather than C-C bonds. This chemistry can be used in PKS engineering to increase the scope and diversity of polyketide biosynthesis.

subject areas

• 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
• Acyl Coenzyme A
• Amino Acid Sequence
• Binding Sites
• Catalysis
• Chromatography, High Pressure Liquid
• Genes, Bacterial
• Macrolides
• Molecular Sequence Data
• Multienzyme Complexes
• Multigene Family
• Mutation
• Protein Engineering
• Protein Subunits
• Sequence Alignment
• Spectrometry, Mass, Electrospray Ionization
• Streptomyces
• Streptomyces griseus
• Transformation, Bacterial

Identity

International Standard Serial Number (ISSN)

• 0036-8075

Digital Object Identifier (DOI)

• 10.1126/science.1073175

PubMed ID

• 12193782

Additional Document Info

start page

• 1327

end page

• 1330

volume

• 297

issue

• 5585