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Abstract <p>Scientific investigations have increasingly focused on enzymaticmechanisms that scavenge reactive carbonyl species (RCS) in plants,motivated by the cytotoxic effects of these compounds, which can induceoxidative damage and even trigger programmed cell death. The α,β-doublebond reductase (DBR) that specifically reduces the C=C double bondof α,β-unsaturated aldehydes/ketones belongs to the medium-chaindehydrogenase/reductase superfamily (MDRs). DBRs from differentplants possess two identical domains: a nucleotide-binding domainwith a shared, conserved GXXS and A(G)XXGXXG motif, along with asubstrate-binding domain with active site residues. In vitro, DBRs catalyzethe reduction of a variety of substrates, including long-chain,short-chain, cyclic aliphatic compounds, as well as phenylpropanoidand phenylbutane aromatic compounds. DBRs are extensively involvedin the metabolic detoxification of RCS, which primarily improvestress resistance of the plants. DBRs have also been found to participatein the biosynthesis of several active compounds which exert uniquedefensive functions and pharmacological activities. In the realmof industrial synthetics, DBRs stand out as promising catalysts,capable of delivering a reduced chiral product with exceptionalyield and chemical purity. Phylogenetic analysis and the catalyticmechanism of DBRs are now poised to be interrogated using moderngenomic and bioinformatic approaches.</p>

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The α,β-Double Bond Reductases (DBRs): An Overview

  • 期刊论文

  • 发表日期：

    2025年5月1日

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  • Hongyang Zhu,
  • Yuemeng Ding,
  • Xue Sun,
  • Yifeng Wu

摘要

Abstract

Scientific investigations have increasingly focused on enzymaticmechanisms that scavenge reactive carbonyl species (RCS) in plants,motivated by the cytotoxic effects of these compounds, which can induceoxidative damage and even trigger programmed cell death. The α,β-doublebond reductase (DBR) that specifically reduces the C=C double bondof α,β-unsaturated aldehydes/ketones belongs to the medium-chaindehydrogenase/reductase superfamily (MDRs). DBRs from differentplants possess two identical domains: a nucleotide-binding domainwith a shared, conserved GXXS and A(G)XXGXXG motif, along with asubstrate-binding domain with active site residues. In vitro, DBRs catalyzethe reduction of a variety of substrates, including long-chain,short-chain, cyclic aliphatic compounds, as well as phenylpropanoidand phenylbutane aromatic compounds. DBRs are extensively involvedin the metabolic detoxification of RCS, which primarily improvestress resistance of the plants. DBRs have also been found to participatein the biosynthesis of several active compounds which exert uniquedefensive functions and pharmacological activities. In the realmof industrial synthetics, DBRs stand out as promising catalysts,capable of delivering a reduced chiral product with exceptionalyield and chemical purity. Phylogenetic analysis and the catalyticmechanism of DBRs are now poised to be interrogated using moderngenomic and bioinformatic approaches.