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Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis
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Awodi, U. R., Ronan, Jade L., Masschelein, Joleen, Emmanuel de los Santos, L. C. and Challis, Gregory L. (2017) Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis. Chemical Science, 8 (1). pp. 411-415. doi:10.1039/C6SC02803A ISSN 2041-6520.
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Official URL: http://dx.doi.org/10.1039/C6SC02803A
Abstract
Actinobacteria produce a variety of polyketide alkaloids with unusual structures. Recently, it was shown that a type I modular polyketide synthase (PKS) is involved in the assembly of coelimycin P1, a polyketide alkaloid produced by Streptomyces coelicolor M145. However, the mechanisms for converting the product of the PKS to coelimycin P1 remain to be elucidated. Here we show that the C-terminal thioester reductase (TR) domain of the PKS and an ω-transaminase are responsible for release of the polyketide chain as an aldehyde and its subsequent reductive amination. Bioinformatics analyses identified numerous gene clusters in actinobacterial genomes that encode modular PKSs with a C-terminal TR domain and a homolog of the ω-transaminase. These are predicted to direct the biosynthesis of both known and novel polyketide alkaloids, suggesting that reductive chain release and transamination constitutes a conserved mechanism for the biosynthesis of such metabolites.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QP Physiology | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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Library of Congress Subject Headings (LCSH): | Polyketides -- Synthesis, Biosynthesis | ||||||||
Journal or Publication Title: | Chemical Science | ||||||||
Publisher: | Royal Society of Chemistry | ||||||||
ISSN: | 2041-6520 | ||||||||
Official Date: | 2017 | ||||||||
Dates: |
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Volume: | 8 | ||||||||
Number: | 1 | ||||||||
Page Range: | pp. 411-415 | ||||||||
DOI: | 10.1039/C6SC02803A | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||
Date of first compliant deposit: | 5 April 2017 | ||||||||
Date of first compliant Open Access: | 7 April 2017 | ||||||||
Funder: | University of Warwick Chancellor’s Interational Scholarship, University of Warwick Chancellor's Scholarship, Marie Curie Individual Fellowship, Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||||||
Grant number: | 656067 (Marie Curie Individual Fellowship), BB/K002341/1, BB/L502017/1, BB/M017982/1 (BBSRC) |
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