ArticleProtein engineering, design & selection : PEDS2016
Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes.
Article in Protein engineering, design & selection : PEDS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
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- Directed evolution of phosphite dehydrogenase to cycle noncanonical redox cofactors via universal growth selection platform.Nature communications · 2022Article
- The catalytic mechanism of the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2).PLoS computational biology · 2022Article
- Structural and Biochemical Analysis of the Furan Aldehyde Reductase YugJ fromInternational journal of molecular sciences · 2022Article
- Highly efficient libraries design for saturation mutagenesis.Synthetic biology (Oxford, England) · 2022Article
- Structural Rearrangements of a Dodecameric Ketol-Acid Reductoisomerase Isolated from a Marine Thermophilic Methanogen.Biomolecules · 2021Article
- "NAD-display": Ultrahigh-Throughput in Vitro Screening of NAD(H) Dehydrogenases Using Bead Display and Flow Cytometry.Angewandte Chemie (International ed. in English) · 2021Article
- Altered Cofactor Preference of Thermostable StDAPDH by a Single Mutation at K159.International journal of molecular sciences · 2020Article
- On the evolution of protein-adenine binding.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Discovery and Biochemical Characterization of a Methanol Dehydrogenase FromFrontiers in bioengineering and biotechnology · 2020Article
- Design and in vitro realization of carbon-conserving photorespiration.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Pyridine Nucleotide Coenzyme Specificity ofFrontiers in microbiology · 2018Article
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- A Simple Combinatorial Codon Mutagenesis Method for Targeted Protein Engineering.ACS synthetic biology · 2017Article
- A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases.ACS synthetic biology · 2017Article
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4 authors.
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Abstract
NAD(P)H-dependent enzymes are ubiquitous in metabolism and cellular processes and are also of great interest for pharmaceutical and industrial applications. Here, we present a structure-guided enzyme engineering strategy for improving catalytic properties of NAD(P)H-dependent enzymes toward native or native-like reactions using mutations to the enzyme's adenine-binding pocket, distal to the site of catalysis. Screening single-site saturation mutagenesis libraries identified mutations that increased catalytic efficiency up to 10-fold in 7 out of 10 enzymes. The enzymes improved in this study represent three different cofactor-binding folds (Rossmann, DHQS-like, and FAD/NAD binding) and utilize both NADH and NADPH. Structural and biochemical analyses show that the improved activities are accompanied by minimal changes in other properties (cooperativity, thermostability, pH optimum, uncoupling), and initial tests on two enzymes (ScADH6 and EcFucO) show improved functionality in Escherichia coli.
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