拟南芥
氧化还原
灵敏度(控制系统)
表征(材料科学)
化学
醇脱氢酶
酒
生物
生物化学
材料科学
纳米技术
基因
有机化学
电子工程
突变体
工程类
作者
Maria Meloni,Jacopo Rossi,Silvia Fanti,Giacomo Carloni,Daniele Tedesco,Patrick Treffon,Luca Piccinini,Giuseppe Falini,Paolo Trost,Elizabeth Vierling,Francesco Licausi,Beatrice Giuntoli,Francesco Musiani,Simona Fermani,Mirko Zaffagnini
摘要
SUMMARY Alcohol dehydrogenases (ADHs) are a group of zinc‐binding enzymes belonging to the medium‐length dehydrogenase/reductase (MDR) protein superfamily. In plants, these enzymes fulfill important functions involving the reduction of toxic aldehydes to the corresponding alcohols (as well as catalyzing the reverse reaction, i.e., alcohol oxidation; ADH1) and the reduction of nitrosoglutathione (GSNO; ADH2/GSNOR). We investigated and compared the structural and biochemical properties of ADH1 and GSNOR from Arabidopsis thaliana . We expressed and purified ADH1 and GSNOR and determined two new structures, NADH‐ADH1 and apo‐GSNOR, thus completing the structural landscape of Arabidopsis ADHs in both apo‐ and holo‐forms. A structural comparison of these Arabidopsis ADHs revealed a high sequence conservation (59% identity) and a similar fold. In contrast, a striking dissimilarity was observed in the catalytic cavity supporting substrate specificity and accommodation. Consistently, ADH1 and GSNOR showed strict specificity for their substrates (ethanol and GSNO, respectively), although both enzymes had the ability to oxidize long‐chain alcohols, with ADH1 performing better than GSNOR. Both enzymes contain a high number of cysteines (12 and 15 out of 379 residues for ADH1 and GSNOR, respectively) and showed a significant and similar responsivity to thiol‐oxidizing agents, indicating that redox modifications may constitute a mechanism for controlling enzyme activity under both optimal growth and stress conditions.
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