Highly enantioselective reduction of carbonyl compounds using a reductase purified from bakers' yeast

被引:38
作者
Ema, T [1 ]
Sugiyama, Y [1 ]
Fukumoto, M [1 ]
Moriya, H [1 ]
Cui, JN [1 ]
Sakai, T [1 ]
Utaka, M [1 ]
机构
[1] Okayama Univ, Fac Engn, Dept Appl Chem, Okayama 700, Japan
关键词
D O I
10.1021/jo980165e
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
An NADPH-dependent reductase that shows reducing activity for 1-chloro-2-hexanone has been purified from bakers' yeast. SDS-PAGE and gel filtration suggested that the purified reductase is a monomeric enzyme with a molecular weight of ca. 37 kDa. Asymmetric reduction of several carbonyl compounds using the purified reductase has been carried out. 1-Chloro-2-hexanone, 1-acetoxy-2-heptanone, methyl acetoacetate, ethyl pyruvate, 1-chloro-2,4-pentanedione, and 2,4-hexanedione were reduced to the corresponding alcohols with high enantiomeric purities (>98% ee). The reductase showed high specificity constants (k(cat)/K-m = 10(3)-10(5) s(-1) M-1) and relatively low Michaelis constants (K-m= 10(-4)-10(-3) M) for all the substrates examined.
引用
收藏
页码:4996 / 5000
页数:5
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