ArticleChembiochem : a European journal of chemical biology2020
Crossing the Border: From Keto- to Imine Reduction in Short-Chain Dehydrogenases/Reductases.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Computational analysis reveals temperature-induced stabilization of FAST-PETase.Computational and structural biotechnology journal · 2025Article
- One-Pot Biocatalytic Synthesis of Primary, Secondary, and Tertiary Amines with Two Stereocenters from α,β-Unsaturated Ketones Using Alkyl-Ammonium Formate.ACS catalysis · 2022Article
- Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Engineering of Thermostable β-Hydroxyacid Dehydrogenase for the Asymmetric Reduction of Imines.Chembiochem : a European journal of chemical biology · 2020Article
- Systematic Evaluation of Imine-Reducing Enzymes: Common Principles in Imine Reductases, β-Hydroxy Acid Dehydrogenases, and Short-Chain Dehydrogenases/ Reductases.Chembiochem : a European journal of chemical biology · 2020Article
- Crossing the Border: From Keto- to Imine Reduction in Short-Chain Dehydrogenases/Reductases.Chembiochem : a European journal of chemical biology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDRs) comprises numerous biocatalysts capable of C=O or C=C reduction. The highly homologous noroxomaritidine reductase (NR) from Narcissus sp. aff. pseudonarcissus and Zt_SDR from Zephyranthes treatiae, however, are SDRs with an extended imine substrate scope. Comparison with a similar SDR from Asparagus officinalis (Ao_SDR) exhibiting keto-reducing activity, yet negligible imine-reducing capability, and mining the Short-Chain Dehydrogenase/Reductase Engineering Database indicated that NR and Zt_SDR possess a unique active-site composition among SDRs. Adapting the active site of Ao_SDR accordingly improved its imine-reducing capability. By applying the same strategy, an unrelated SDR from Methylobacterium sp. 77 (M77_SDR) with distinct keto-reducing activity was engineered into a promiscuous enzyme with imine-reducing activity, thereby confirming that the ability to reduce imines can be rationally introduced into members of the "classical" SDR enzyme family. Thus, members of the SDR family could be a promising starting point for protein approaches to generate new imine-reducing enzymes.
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