Purification and Properties of an Asymmetric Reduction Enzyme of 2-Methyl-3-oxobutyrate in Bakers Yeast
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概要
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The benzyl 2-methyl-3-hydroxybutyrate dehydrogenase was purified from the cells of bakers yeast by streptomycin treatment, Sephadex G-50 gel filtration, SP-Sephadex C-50 chromatography, and Toyopearl HW-60F gel filtration. The purified enzyme preparation was homogeneous and the molecular weight was about 31, 000 to 32, 000. The enzyme was NADPH-dependent and its maximum activity was at pH 7.0 and 45°C. It was stable between pH 6 and 9. The Km values at pH 7.0 were 0.42mM for benzyl 2-methyl-3-oxobutyrate (1) and 4.2mM for α-methyl β-hydroxy ester [syn-(2) and anti-(3)]. This enzyme reduced only benzyl 2-methyl-3-oxobutyrate (1) but had no effect on other synthetic substrates. The reduced products [syn-(2) and anti(3)] produced by the purified enzyme were identified by 400MHz NMR.
- 社団法人 日本農芸化学会の論文
著者
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HORIKOSHI KOKI
The Institute of Physical and Chemical Research
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AKITA HIROYUKI
The Institute of Physical and Chemical Research (Riken)
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OISHI Takeshi
The Institute of Physical and Chemical Research
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FURUICHI Akiya
The Institute of Physical and Chemical Research
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MATSUKURA(nee KOSHIJI)
The Institute of Physical and Chemical Research
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