ArticleACS synthetic biology2017
A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases.
Article in ACS synthetic biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- A cofactor-promiscuous HMGR from the Lyme disease pathogen illuminates diversity in bacterial isoprenoid biosynthesis.Protein science : a publication of the Protein Society · 2026Article
- A cofactor-promiscuous HMGR from the Lyme disease pathogen illuminates diversity in bacterial isoprenoid biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Expanding the cofactor range of aldehyde reductase YqhD by mutating key amino acids.Biotechnology letters · 2026Article
- Structural and evolutionary dissection of NADPH-binding motifs in NADPH-preferring ene-reductases.Protein science : a publication of the Protein Society · 2026Article
- Monooxygenase-dehydrogenase cascade for sustained enzymatic remediation of TMA in salmon protein hydrolysates.Applied and environmental microbiology · 2026Article
- The role of AdhE mutations inJournal of bacteriology · 2025Article
- MACAW: a method for semi-automatic detection of errors in genome-scale metabolic models.Genome biology · 2025Article
- Cofactor engineering for improved production of 2,4-dihydroxybutyric acid via the synthetic homoserine pathway.Frontiers in bioengineering and biotechnology · 2025Article
- The role of AdhE on ethanol tolerance and production in Clostridium thermocellum.The Journal of biological chemistry · 2024Article
- A refined picture of the native amine dehydrogenase family revealed by extensive biodiversity screening.Nature communications · 2024Article
- Changing the Electron Acceptor Specificity ofInternational journal of molecular sciences · 2023Article
- Network-wide thermodynamic constraints shape NAD(P)H cofactor specificity of biochemical reactions.Nature communications · 2023Article
- Going Full Circle with Organocatalysis and Biocatalysis: The Latent Potential of Cofactor Mimics in Asymmetric Synthesis.The Journal of organic chemistry · 2023Review
- A primer to directed evolution: current methodologies and future directions.RSC chemical biology · 2023Review
- Logistic Regression-Guided Identification of Cofactor Specificity-Contributing Residues in Enzyme with Sequence Datasets Partitioned by Catalytic Properties.ACS synthetic biology · 2022Article
- Insertions and deletions mediated functional divergence of Rossmann fold enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Orthogonal glycolytic pathway enables directed evolution of noncanonical cofactor oxidase.Nature communications · 2022Article
- Engineering Isopropanol Dehydrogenase for Efficient Regeneration of Nicotinamide Cofactors.Applied and environmental microbiology · 2022Article
- Protein cost minimization promotes the emergence of coenzyme redundancy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Rossmann-toolbox: a deep learning-based protocol for the prediction and design of cofactor specificity in Rossmann fold proteins.Briefings in bioinformatics · 2022Article
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Authors and funding
6 authors.
Funding
Abstract
The ability to control enzymatic nicotinamide cofactor utilization is critical for engineering efficient metabolic pathways. However, the complex interactions that determine cofactor-binding preference render this engineering particularly challenging. Physics-based models have been insufficiently accurate and blind directed evolution methods too inefficient to be widely adopted. Building on a comprehensive survey of previous studies and our own prior engineering successes, we present a structure-guided, semirational strategy for reversing enzymatic nicotinamide cofactor specificity. This heuristic-based approach leverages the diversity and sensitivity of catalytically productive cofactor binding geometries to limit the problem to an experimentally tractable scale. We demonstrate the efficacy of this strategy by inverting the cofactor specificity of four structurally diverse NADP-dependent enzymes: glyoxylate reductase, cinnamyl alcohol dehydrogenase, xylose reductase, and iron-containing alcohol dehydrogenase. The analytical components of this approach have been fully automated and are available in the form of an easy-to-use web tool: Cofactor Specificity Reversal-Structural Analysis and Library Design (CSR-SALAD).
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