醛还原酶
立体专一性
醛
化学
立体化学
等电点
对映体过量
辅因子
酶
还原酶
催化作用
对映选择合成
有机化学
作者
Keiko Kita,Koh-ichi Nakase,Hideshi Yanase,Michihiko Kataoka,Sakayu Shimizu
出处
期刊:Journal of Molecular Catalysis B-enzymatic
[Elsevier]
日期:1999-03-01
卷期号:6 (3): 305-313
被引量:42
标识
DOI:10.1016/s1381-1177(98)00108-8
摘要
New aldehyde reductases (AR), ARII and ARIII, which reduce ethyl 4-chloro-3-oxobutanoate (4-COBE) to ethyl 4-chloro-3-hydroxybutanoate (CHBE), with NADPH as a cofactor, were purified from Sporobolomyces salmonicolor AKU4429. The two enzymes were different from another aldehyde reductase (ARI) which had already been purified and characterized [Yamada et al., FEMS Microbiol. Lett., 70 (1990) 45; Kataoka et al., Biochim. Biophys. Acta, 1122 (1992) 57]. ARII catalyzed the stereospecific reduction of 4-COBE to (S)-CHBE (92.7% enantiomeric excess (e.e.)). In contrast, ARIII reduced 4-COBE to (R)-CHBE (38.4% e.e.). ARII was characterized further, and reduced aliphatic and aromatic aldehydes, as well as carbonyl compounds, such as camphorquinone, but did not accept aldose as a substrate. The enzyme is a monomer protein with a relative molecular mass of 34,000. Its isoelectric point is 5.0. The NH2-terminal amino acid sequence of ARII is different from that of ARI, which catalyzes the stereospecific reduction of 4-COBE to (R)-CHBE (100% e.e.).
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