ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural and evolutionary relationships of "AT-less" type I polyketide synthase ketosynthases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 67 citations in OpenAlex.
- Research progress of glutarimide-containing polyketides: Structures, bioactivities and their biosynthesis.Pharmaceutical science advances · 2025Review
- Plug-and-play engineering of modular polyketide synthases.Nature chemical biology · 2025Article
- Gene conversion-associated successive engineering of modular polyketide synthases.Communications chemistry · 2025Article
- Modular polyketide synthase ketosynthases collaborate with upstream dehydratases to install double bonds.Chemical communications (Cambridge, England) · 2024Article
- Structure and Mechanisms of Assembly-Line Polyketide Synthases.Annual review of biochemistry · 2024Review
- Evolution-guided engineering ofScience (New York, N.Y.) · 2024Article
- Structure of a modular polyketide synthase reducing region.Structure (London, England : 1993) · 2023Article
- Acinetobacter type VI secretion system comprises a non-canonical membrane complex.PLoS pathogens · 2023Article
- Crosstalk between primary and secondary metabolism: Interconnected fatty acid and polyketide biosynthesis in prokaryotes.Bioorganic & medicinal chemistry letters · 2023Review
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- Insights into azalomycin F assembly-line contribute to evolution-guided polyketide synthase engineering and identification of intermodular recognition.Nature communications · 2023Article
- Programmed Iteration Controls the Assembly of the Nonanoic Acid Side Chain of the Antibiotic Mupirocin.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Programmed Iteration Controls the Assembly of the Nonanoic Acid Side Chain of the Antibiotic Mupirocin.Angewandte Chemie (International ed. in English) · 2022Article
- Enzymatic assembly of the salinosporamide γ-lactam-β-lactone anticancer warhead.Nature chemical biology · 2022Article
- HowACS chemical biology · 2021Article
- Initiating polyketide biosynthesis by on-line methyl esterification.Nature communications · 2021Article
- Biosynthesis Gene Cluster and Oxazole Ring Formation Enzyme for Inthomycins inApplied and environmental microbiology · 2020Article
- Unique features of the ketosynthase domain in a nonribosomal peptide synthetase-polyketide synthase hybrid enzyme, tenuazonic acid synthetase 1.The Journal of biological chemistry · 2020Article
- Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.Synthetic and systems biotechnology · 2020Review
- Unraveling the iterative type I polyketide synthases hidden inProceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
Abstract
Acyltransferase (AT)-less type I polyketide synthases (PKSs) break the type I PKS paradigm. They lack the integrated AT domains within their modules and instead use a discrete AT that acts in trans, whereas a type I PKS module minimally contains AT, acyl carrier protein (ACP), and ketosynthase (KS) domains. Structures of canonical type I PKS KS-AT didomains reveal structured linkers that connect the two domains. AT-less type I PKS KSs have remnants of these linkers, which have been hypothesized to be AT docking domains. Natural products produced by AT-less type I PKSs are very complex because of an increased representation of unique modifying domains. AT-less type I PKS KSs possess substrate specificity and fall into phylogenetic clades that correlate with their substrates, whereas canonical type I PKS KSs are monophyletic. We have solved crystal structures of seven AT-less type I PKS KS domains that represent various sequence clusters, revealing insight into the large structural and subtle amino acid residue differences that lead to unique active site topologies and substrate specificities. One set of structures represents a larger group of KS domains from both canonical and AT-less type I PKSs that accept amino acid-containing substrates. One structure has a partial AT-domain, revealing the structural consequences of a type I PKS KS evolving into an AT-less type I PKS KS. These structures highlight the structural diversity within the AT-less type I PKS KS family, and most important, provide a unique opportunity to study the molecular evolution of substrate specificity within the type I PKSs.
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