Muheim A, Waldner R, Sanglard D, Reiser J, Schoemaker H E, Leisola M S
Department of Biotechnology, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Eur J Biochem. 1991 Jan 30;195(2):369-75. doi: 10.1111/j.1432-1033.1991.tb15715.x.
An intracellular aryl-alcohol dehydrogenase (previously referred to as aryl-aldehyde reductase) was purified from the white-rot fungus Phanerochaete chrysosporium. The enzyme reduced veratraldehyde to veratryl alcohol using NADPH as a cofactor. Other aromatic benzaldehydes were also reduced, but not aromatic ketones. Methoxy-substituted rings were better substrates than hydroxylated ones. The enzyme was also able to reduce a dimeric aldehyde (4-benzyloxy-3-methoxybenzaldehyde). The highest reduction rate was measured when 3,5-dimethoxybenzaldehyde was used as a substrate. On SDS/PAGE the purified enzyme showed one major band with a molecular mass of 47 kDa, whereas gel filtration suggested a molecular mass of 280 kDa. Polyclonal antibodies raised against the gel purified 47-kDa protein were able to immunoprecipitate the aryl-alcohol dehydrogenase indicating that its activity possibly resides entirely in this protein fragment. The pI of the enzyme was 5.2 and it was most active at pH 6.1. The aryl-alcohol dehydrogenase was partially inhibited by typical oxidoreductase inhibitors.
从白腐真菌黄孢原毛平革菌中纯化出一种细胞内芳基醇脱氢酶（以前称为芳基醛还原酶）。该酶以NADPH作为辅因子，将藜芦醛还原为藜芦醇。其他芳香族苯甲醛也能被还原，但芳香族酮不能。甲氧基取代的环比羟基化的环是更好的底物。该酶还能够还原一种二聚醛（4-苄氧基-3-甲氧基苯甲醛）。以3,5-二甲氧基苯甲醛为底物时，测得的还原速率最高。在SDS/PAGE上，纯化后的酶显示出一条主要条带，分子量为47 kDa，而凝胶过滤表明分子量为280 kDa。针对凝胶纯化的47 kDa蛋白产生的多克隆抗体能够免疫沉淀芳基醇脱氢酶，这表明其活性可能完全存在于该蛋白片段中。该酶的pI为5.2，在pH 6.1时活性最高。芳基醇脱氢酶受到典型氧化还原酶抑制剂的部分抑制。
