ArticleProteins2014
Structural and functional studies of a trans-acyltransferase polyketide assembly line enzyme that catalyzes stereoselective α- and β-ketoreduction.
Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- KRstereo: Predicting β-Hydroxy Stereochemistry in Polyketides Using Protein Language Models.Journal of chemical information and modeling · 2026Article
- Characterization of the ketoreductase domain of pikromycin module 2.Chemical science · 2026Article
- Bioinformatic prediction of the stereoselectivity of modular polyketide synthase: an update of the sequence motifs in ketoreductase domain.Beilstein journal of organic chemistry · 2024Article
- Molecular basis for acyl carrier protein-ketoreductase interaction inChemical science · 2021Article
- Structural and Functional Studies of a gem-Dimethylating Methyltransferase from a trans-Acyltransferase Assembly Line.ACS chemical biology · 2018Article
- Natural products chemistry: The emerging trends and prospective goals.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018Article
- The modules of trans-acyltransferase assembly lines redefined with a central acyl carrier protein.Proteins · 2018Article
- Structural and Functional Studies of a Pyran Synthase Domain from a trans-Acyltransferase Assembly Line.ACS chemical biology · 2018Article
- Structural and Functional Trends in Dehydrating Bimodules from trans-Acyltransferase Polyketide Synthases.Structure (London, England : 1993) · 2017Article
- Polyketide stereocontrol: a study in chemical biology.Beilstein journal of organic chemistry · 2017Review
- Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase.ACS chemical biology · 2016Article
- Portability and Structure of the Four-Helix Bundle Docking Domains of trans-Acyltransferase Modular Polyketide Synthases.ACS chemical biology · 2016Article
- An unusual intramolecularTetrahedron · 2016Article
- The LINKS motif zippers trans-acyltransferase polyketide synthase assembly lines into a biosynthetic megacomplex.Journal of structural biology · 2016Article
- Stereocontrol within polyketide assembly lines.Natural product reports · 2016Review
- Substrate structure-activity relationships guide rational engineering of modular polyketide synthase ketoreductases.Chemical communications (Cambridge, England) · 2016Article
- The structural biology of biosynthetic megaenzymes.Nature chemical biology · 2015Review
- A double-hotdog with a new trick: structure and mechanism of the trans-acyltransferase polyketide synthase enoyl-isomerase.ACS chemical biology · 2014Article
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5 authors.
Funding
Abstract
While the cis-acyltransferase modular polyketide synthase assembly lines have largely been structurally dissected, enzymes from within the recently discovered trans-acyltransferase polyketide synthase assembly lines are just starting to be observed crystallographically. Here we examine the ketoreductase (KR) from the first polyketide synthase module of the bacillaene nonribosomal peptide synthetase/polyketide synthase at 2.35-Å resolution. This KR naturally reduces both α- and β-keto groups and is the only KR known to do so during the biosynthesis of a polyketide. The isolated KR not only reduced an N-acetylcysteamine-bound β-keto substrate to a D-β-hydroxy product, but also an N-acetylcysteamine-bound α-keto substrate to an L-α-hydroxy product. That the substrates must enter the active site from opposite directions to generate these stereochemistries suggests that the acyl-phosphopantetheine moiety is capable of accessing very different conformations despite being anchored to a serine residue of a docked acyl carrier protein. The features enabling stereocontrolled α-ketoreduction may not be extensive since a KR that naturally reduces a β-keto group within a cis-acyltransferase polyketide synthase was identified that performs a completely stereoselective reduction of the same α-keto substrate to generate the D-α-hydroxy product. A sequence analysis of trans-acyltransferase KRs reveals that a single residue, rather than a three-residue motif found in cis-acyltransferase KRs, is predictive of the orientation of the resulting β-hydroxyl group.
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