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Related Experiment Video

Updated: Jun 24, 2026

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

Novel type III polyketide synthases from Aloe arborescens.

Yuusuke Mizuuchi¹, She-Po Shi, Kiyofumi Wanibuchi

¹School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.

The FEBS Journal

|April 7, 2009

Summary

Researchers identified novel enzymes in Aloe arborescens, revealing the enzymatic pathways for key pharmaceutical compounds like aloesin and aloenin. This study elucidates the biosynthesis of important polyketides in medicinal plants.

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A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

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From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

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A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

Published on: October 4, 2019

Area of Science:

Biochemistry
Plant Science
Molecular Biology

Background:

Aloe arborescens produces valuable aromatic polyketides, including aloenin, aloesin, and barbaloin.
Understanding the biosynthesis of these compounds is crucial for pharmaceutical applications.

Purpose of the Study:

To identify and characterize novel type III polyketide synthases (PKS3, PKS4, PKS5) from Aloe arborescens.
To elucidate the enzymatic mechanisms underlying the production of pharmaceutically important polyketides.

Main Methods:

cDNA library screening to clone and sequence novel PKS enzymes.
Recombinant expression of PKS4 and PKS5 in Escherichia coli.
Site-directed mutagenesis of PKS3 to investigate active-site residue function.

Main Results:

PKS4 and PKS5 function as octaketide synthases, producing SEK4/SEK4b, potentially involved in barbaloin biosynthesis.
PKS3 is a multifunctional enzyme producing aloesone (aloesin precursor), a hexaketide pyrone (aloenin precursor), and other novel polyketides.
The active-site residue A207 in PKS3 plays a critical role in determining polyketide chain length.

Conclusions:

This is the first report of enzymatic formation of aloesin and aloenin precursors by wild-type PKS from Aloe arborescens.
The identified enzymes and their mechanisms provide insights into the biosynthesis of important medicinal compounds.
Enzyme engineering via mutagenesis can alter PKS product specificity, offering potential for novel compound discovery.