Shigeru Kawano

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A novel (R)-specific alcohol dehydrogenase (AFPDH) produced by Candida maris IFO10003 was purified to homogeneity by ammonium sulfate fractionation, DEAE-Toyopearl, and Phenyl-Toyopearl, and characterized. The relative molecular mass of the native enzyme was found to be 59,900 by gel filtration, and that of the subunit was estimated to be 28,900 on(More)
5-((R)-1-Hydroxyethyl)-furo[2,3-c]pyridine ((R)-FPH) is a useful chiral building block in the synthesis of pharmaceuticals. An NADH-dependent alcohol dehydrogenase (AFPDH) isolated from Candida maris catalyzed the reduction of 5-acetylfuro[2,3-c]pyridine (AFP) to (R)-FPH with 100% enantiomeric excess. The gene encoding AFPDH was cloned and sequenced. The(More)
Pseudomonas fluorescens KNK08-18, showing (S)-selective transaminase activity, was isolated from soil by an enrichment culture method using (S)-7-methoxy-2-aminotetraline as the main nitrogen source. A transaminase was purified from the strain to homogeneity in seven steps. The relative mass of the enzyme was estimated to be 53 kDa on SDS-polyacrylamide gel(More)
The microbial enantioselective reduction of acetylpyridine derivatives was studied. Many microorganisms were found to reduce 5-acetylfuro[2,3-c]pyridine (AFP) to (S)-5-(1-hydroxyethyl)furo[2,3-c]-pyridine (FPH). Candida maris IFO10003 reduced AFP to (R)-FPH with high enantioselectivity. The microbial reduction reaction was optimized. The aeration conditions(More)
An efficient chemo-enzymatic procedure for the synthesis of (R)-3-hydroxypentanenitrile (1) with over 99% enantiomeric excess using two enzymatic reactions was successfully established. Initial enantioselective enzymatic reduction of 3-oxopentanenitrile with reductase S1 gave (R)-1 with an 81.5% ee which was then converted to (R)-1-(cyanomethyl) propyl(More)
Norcoclaurine synthase (NCS) catalyzes the stereoselective Pictet-Spengler reaction between dopamine and 4-hydroxyphenylacetaldehyde as the first step of benzylisoquinoline alkaloid synthesis in plants. Recent studies suggested that NCS shows relatively relaxed substrate specificity toward aldehydes, and thus, the enzyme can serve as a tool to synthesize(More)