Engineering of plant type III polyketide synthases

Toshiyuki Wakimoto, Hiroyuki Morita, Ikuro Abe*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

9 Scopus citations

Abstract

Members of the chalcone synthase superfamily of type III polyketide synthases (PKSs) catalyze iterative condensations of CoA thioesters to produce a variety of polyketide scaffolds with remarkable structural diversity and biological activities. The homodimeric type III PKSs share a common three-dimensional overall fold with a conserved Cys-His-Asn catalytic triad; notably, only a slight modification of the active site dramatically expands the catalytic repertoire of the enzymes. In addition, the enzymes exhibit extremely promiscuous substrate specificities, and accept a variety of nonphysiological substrates, making the type III PKSs an excellent platform for the further production of unnatural, novel polyketide scaffolds with promising biological activities. This chapter summarizes recent advances in the engineering of plant type III PKS enzymes in our laboratories, using approaches combining structure-based enzyme engineering and precursor-directed biosynthesis with rationally designed substrate analogs.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages337-358
Number of pages22
DOIs
StatePublished - 2012

Publication series

NameMethods in Enzymology
Volume515
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Chalcone synthase superfamily enzyme
  • Enzyme engineering
  • Polyketide synthase
  • Precursor-directed biosynthesis
  • Structure-based engineering
  • Unnatural natural product

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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