AI Article Synopsis
- * Noroxomaritidine reductase (NR) and Zt_SDR are SDRs with enhanced imine reduction potential compared to the keto-reducing Asparagus officinalis SDR (Ao_SDR), which has limited imine-reducing ability.
- * By modifying the active site of Ao_SDR and engineering another unrelated SDR (M77_SDR), researchers demonstrated that imine-reducing function can be introduced into SDRs
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7540013 | PMC |
| http://dx.doi.org/10.1002/cbic.202000233 | DOI Listing |
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