A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of ß-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization
A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of ß-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization
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一种新型 NADPH 依赖性醛还原酶，催化来自鲑色孢子酵母的 β-酮酸酯的不对称还原：纯化和表征
DOI：
10.1111/j.1574-6968.1990.tb03775.x
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发表时间：
1990
影响因子：
2.1
通讯作者：
T. Miyoshi
中科院分区：
文献类型：
--
作者：
H. Yamada;S. Shimizu;M. Kataoka;H. Sakai;T. Miyoshi
对黄色芽孢杆菌AKU 4429的NADPH依赖的乙醛还原酶(EC 1.1.1.2)进行了4步纯化，纯化倍数为23倍，总收率为11%，并用硫酸铵结晶了该酶。该酶对NADPH有严格的要求，不可逆地还原了一些醛，如对硝基苯甲醛、吡啶-3-醛和d-甘油醛。此外，还发现该酶催化4-卤代-3-氧代丁酸酯的立体专一性还原为相应的(R)-4-卤代-3-羟基丁酸酯，是化学合成L-肉碱的良好手性化合物。
NADPH-dependent aldehyde reductase (EC 1.1.1.2) was purified 23-fold with an overall yield of 11% from Sporobolomyces salmonicolor AKU 4429, in 4 steps and, by adding ammonium sulfate, the enzyme was crystallized. The enzyme has a strict requirement for NADPH and irrversibly reduces a number of aldehydes, such as p-nitrobenzaldehyde, pyridine-3-aldehyde and d-glyceraldehyde. Furthermore, it was found that the enzyme catalyses stereospecific reduction of 4-halo-3-oxobutanoate esters to the corresponding (R)-4-halo-3-hydroxybutanoate esters, which are promising chiral compounds for the chemical synthesis of l-carnitine.