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Related Experiment Video

Updated: Apr 24, 2026

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes T&#252;6028
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Fungal type III polyketide synthases.

Makoto Hashimoto1, Takamasa Nonaka, Isao Fujii

  • 1Iwate Medical University, School of Pharmacy, Japan. ifujii@iwate-med.ac.jp.

Natural Product Reports
|September 4, 2014
PubMed
Summary

Fungal type III polyketide synthases (PKSs) are less abundant but play critical roles. Research highlights their functional analysis and substrate specificities, revealing new enzyme activities.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Mycology

Background:

  • Fungal type III polyketide synthases (PKSs) are less common than type I PKSs but possess crucial biological functions.
  • The discovery of fungal type III PKS genes began in 2005 with Aspergillus oryzae, leading to identification in various fungal genomes.
  • This review focuses on the literature from 2005 to 2014 concerning fungal type III PKSs.

Purpose of the Study:

  • To summarize the functional analysis of fungal type III PKSs.
  • To review studies on specific fungal type III PKS enzymes, including Neurospora crassa ORAS, Aspergillus niger AnPKS, Botrytis cinerea BPKS, and Aspergillus oryzae CsyA and CsyB.
  • To discuss the substrate specificity and catalytic mechanisms of these enzymes.

Main Methods:

  • Literature review of fungal type III PKS research published between 2005 and 2014.

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  • Functional analysis of selected fungal type III PKS enzymes.
  • In vitro enzymatic assays using recombinant proteins to determine substrate and product specificities.
  • Homology modeling to investigate enzyme structure-function relationships.

    • Main Results:

    • Functional analysis of several fungal type III PKSs has been reported, primarily through in vitro studies.
    • The starter and product specificities of these enzymes have been elucidated.
    • Aspergillus oryzae CsyB was identified as a novel type III PKS catalyzing the condensation of two β-keto fatty acyl-CoAs.
    • Homology modeling suggests that the acyl binding tunnel and active site cavity are critical for fungal type III PKS function.

    Conclusions:

    • Fungal type III PKSs, despite their lower abundance, exhibit diverse functions and specificities.
    • The characterization of enzymes like CsyB expands the known repertoire of type III PKS catalytic activities.
    • Structural insights from homology modeling underscore the importance of active site architecture in determining the function of fungal type III PKSs.