ArticleChemical communications (Cambridge, England)2016
Substrate structure-activity relationships guide rational engineering of modular polyketide synthase ketoreductases.
Article in Chemical communications (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Distinct Acyl Carrier Protein Docking Sites Help Mediate the Opposite Stereoselectivities of A- and B-type Modular Polyketide Synthase Ketoreductases.Biochemistry · 2025Article
- Article
- Determination of Enantiomeric Excess and Diastereomeric Excess via Optical Methods. Application to α-methyl-β-hydroxy-carboxylic acids.Organic chemistry frontiers : an international journal of organic chemistry · 2023Article
- Ketoreductase Catalyzed (Dynamic) Kinetic Resolution for Biomanufacturing of Chiral Chemicals.Frontiers in bioengineering and biotechnology · 2022Review
- Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.Synthetic and systems biotechnology · 2020Review
- The urinary microbiome shows different bacterial genera in renal transplant recipients and non-transplant patients at time of acute kidney injury - a pilot study.BMC nephrology · 2020Article
- General chemoenzymatic route to two-stereocenter triketides employing assembly line ketoreductases.Chemical communications (Cambridge, England) · 2019Article
- Modular type I polyketide synthase acyl carrier protein domains share a common N-terminally extended fold.Scientific reports · 2019Article
- Substrate-bound structures of a ketoreductase from amphotericin modular polyketide synthase.Journal of structural biology · 2018Article
- Engineering modular polyketide synthases for production of biofuels and industrial chemicals.Current opinion in biotechnology · 2018Review
- Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates.Chemical communications (Cambridge, England) · 2017Article
- Engineered polyketides: Synergy between protein and host level engineering.Synthetic and systems biotechnology · 2017Review
- Structural and Functional Trends in Dehydrating Bimodules from trans-Acyltransferase Polyketide Synthases.Structure (London, England : 1993) · 2017Article
- Mechanism and Stereochemistry of Polyketide Chain Elongation and Methyl Group Epimerization in Polyether Biosynthesis.Journal of the American Chemical Society · 2017Article
- Towards Precision Engineering of Canonical Polyketide Synthase Domains: Recent Advances and Future Prospects.Molecules (Basel, Switzerland) · 2017Review
- Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates.The Journal of antibiotics · 2016Article
- Insights into polyketide biosynthesis gained from repurposing antibiotic-producing polyketide synthases to produce fuels and chemicals.The Journal of antibiotics · 2016Review
- Molecular Genetic Characterization of an Anthrabenzoxocinones Gene Cluster in Streptomyces Sp. FJS31-2 for the Biosynthesis of BE-24566B and Zunyimycin Ale.Molecules (Basel, Switzerland) · 2016Article
- Epimerase and Reductase Activities of Polyketide Synthase Ketoreductase Domains Utilize the Same Conserved Tyrosine and Serine Residues.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Modular polyketide synthase ketoreductases can set two chiral centers through a single reduction. To probe the basis of stereocontrol, a structure-activity relationship study was performed with three α-methyl, β-ketothioester substrates and four ketoreductases. Since interactions with the β-ketoacyl moiety were found to be most critical, residues implicated in contacting this moiety were mutated. Two mutations were sufficient to completely reverse the stereoselectivity of the model ketoreductase EryKR1, converting it from an enzyme that generates (2S,3R)-products into one that yields (2S,3S)-products.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.