一种来自亚特兰蒂斯 II 深海卤水湖的多极端嗜热醇脱氢酶。
A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool.
机构信息
KAUST Catalysis Center (KCC) King Abdullah University of Science and Technology (KAUST) Thuwal Saudi Arabia.
Center for Integrated Protein Science Munich at the Department of Chemistry Technical University of Munich (TUM) Garching Germany.
出版信息
FEBS Open Bio. 2018 Dec 18;9(2):194-205. doi: 10.1002/2211-5463.12557. eCollection 2019 Feb.
Abstract
Enzymes originating from hostile environments offer exceptional stability under industrial conditions and are therefore highly in demand. Using single-cell genome data, we identified the alcohol dehydrogenase (ADH) gene, , from the Atlantis II Deep Red Sea brine pool. ADH/A1a is highly active at elevated temperatures and high salt concentrations (optima at 70 °C and 4 m KCl) and withstands organic solvents. The polyextremophilic ADH/A1a exhibits a broad substrate scope including aliphatic and aromatic alcohols and is able to reduce cinnamyl-methyl-ketone and raspberry ketone in the reverse reaction, making it a possible candidate for the production of chiral compounds. Here, we report the affiliation of ADH/A1a to a rare enzyme family of microbial cinnamyl alcohol dehydrogenases and explain unique structural features for halo- and thermoadaptation.
摘要
来源于恶劣环境的酶在工业条件下具有非凡的稳定性，因此需求量很大。我们利用单细胞基因组数据，从亚特兰蒂斯 II 深海卤水湖中鉴定出了醇脱氢酶（ADH）基因 。ADH/A1a 在高温和高盐浓度下（最佳温度为 70°C 和 4 m KCl）高度活跃，并能耐受有机溶剂。多极端适应的 ADH/A1a 表现出广泛的底物范围，包括脂肪族和芳香族醇，并且能够在逆反应中还原肉桂基甲基酮和覆盆子酮，使其成为手性化合物生产的潜在候选物。在这里，我们将 ADH/A1a 与微生物肉桂醇脱氢酶的罕见酶家族联系起来，并解释了其对卤化物和热适应的独特结构特征。
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