Iterative polyketide biosynthesis by modular polyketide synthases in bacteria

Modular polyketide synthases (type I PKSs) in bacteria are responsible for synthesizing a significant percentage of bioactive natural products. This group of synthases has a characteristic modular organization, and each module within a PKS carries out one cycle of polyketide chain elongation; thus e...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2016-01, Vol.100 (2), p.541-557
Main Authors: Chen, Haotong, Du, Liangcheng
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analysis
Bacteria
Bacteria - enzymology
Bacteria - metabolism
Bacterial proteins
bioactive properties
Biological Products - metabolism
Biomedical and Life Sciences
Biosynthesis
Biosynthetic Pathways
Biotechnology
Carbon
Engineering
Health aspects
Life Sciences
Metabolites
Microbial Genetics and Genomics
Microbiology
Mini-Review
Natural products
Observations
Phylogenetics
polyketide synthases
Polyketide Synthases - metabolism
Polyketides
Polyketides - metabolism
Polypeptides
Secondary Metabolism
Studies
Substrate Specificity
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Summary:Modular polyketide synthases (type I PKSs) in bacteria are responsible for synthesizing a significant percentage of bioactive natural products. This group of synthases has a characteristic modular organization, and each module within a PKS carries out one cycle of polyketide chain elongation; thus each module is non-iterative in function. It was possible to predict the basic structure of a polyketide product from the module organization of the PKSs, since there generally existed a co-linearity between the number of modules and the number of chain elongations. However, more and more bacterial modular PKSs fail to conform to the canonical rules, and a particularly noteworthy group of non-canonical PKSs is the bacterial iterative type I PKSs. This review covers recent examples of iteratively used modular PKSs in bacteria. These non-canonical PKSs give rise to a large array of natural products with impressive structural diversity. The molecular mechanism behind the iterations is often unclear, presenting a new challenge to the rational engineering of these PKSs with the goal of generating new natural products. Structural elucidation of these synthase complexes and better understanding of potential PKS-PKS interactions as well as PKS-substrate recognition may provide new prospects and inspirations for the discovery and engineering of new bioactive polyketides.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-015-7093-0