1.1.1.B3: (S)-specific secondary alcohol dehydrogenase
This is an abbreviated version!
For detailed information about (S)-specific secondary alcohol dehydrogenase, go to the full flat file.
Reaction
Synonyms
(S)-1-phenylethanol dehydrogenase, (S)-1-phenylethanolsynthase, acetophenone reductase, ADH, ADH-A, ADH1, ADH2, ADHTt, APRD, carbonyl reductase (NADH, specific for (S)-configuration of alcohol), CRII, More, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent ADH, PED, S-ADH, SADH, Scr2, SDR, short chain dehydrogenase, short-chain NAD(H)-dependent alcohol dehydrogenase, SOU1, SPES, TtADH
ECTree
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Application
Application on EC 1.1.1.B3 - (S)-specific secondary alcohol dehydrogenase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
synthesis
synthesis
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production of ethyl (R)-4-chloro-3-hydroxybutanoate using whole recombinant cells of Escherichia coli and 2-propanol as an energy source to regenerate NADH. Yield reaches 36.6 g/l with purity of more than 99% enantiomeric excess and 95.2% conversion
synthesis
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synthesis of (R)-1,3-butanediol from its racemate by stereoselective oxidation of the (S)-isomer using (S)-specific secondary alcohol dehydrogenase in whole recombinant Escherichia coli cells. Yield of the (R)-product reaches 72.6 g/l, with a molar recovery yield of 48.4% and an optical purity of 95% enantiomeric excess
synthesis
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the enzyme is useful in production of chiral compounds for organic synthesis
synthesis
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the immobilized enzyme is utilized in the asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%
synthesis
synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate in Escherichia coli. Coexpression of carbonyl reductase CRII and a glucose dehydrogenase gives an activity of 15 U/mg protein using ethyl 4-chloro-3-oxobutanoate as a substrate in a water/butyl acetate system. The transformants give a molar yield of 91%, and an optical purity of the (S)-isomer of more than 99% enantiomeric excess
synthesis
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the enzyme can be used for stereospecific interconversion of (R)-1-phenylethanol and (S)-1-phenylethanol via the oxoform together with the (R)-specific secondary alcohol dehydrogenase using whole cells as biocatalysts that include the required cofactor regenration system, method, overview. Optically pure secondary alcohols are widely used in pharmaceuticals, flavors, agricultural chemicals and specialty materials
synthesis
the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, the activity is 6.2 U/mg. Using two coexisting recombinant Escherichia coli strains, in which a strain expressing glucose dehydrogenase is used as an NADPH regenerator. An optical purity of 99% (e.e.) and a maximum yield of 1240 mM (S)-4-chloro-3-hydroxybutanoate are obtained, and highest turnover number of 53900 can be achieved without adding extra NADP+/NADPH
synthesis
using recombinant Scr2 in an aqueous-organic solvent system with a substrate fed-batch strategy and a final substrate concentration of 1 M, a yield of 95.3% and e.e. of 99% is obtained after 6-h reaction
synthesis
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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the enzyme is useful in production of chiral compounds for organic synthesis
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synthesis
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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the immobilized enzyme is utilized in the asymmetric reduction of acetophenone to produce (S)-1-phenylethanol, with an enantiomeric excess of more than 99%
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synthesis
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the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, the activity is 6.2 U/mg. Using two coexisting recombinant Escherichia coli strains, in which a strain expressing glucose dehydrogenase is used as an NADPH regenerator. An optical purity of 99% (e.e.) and a maximum yield of 1240 mM (S)-4-chloro-3-hydroxybutanoate are obtained, and highest turnover number of 53900 can be achieved without adding extra NADP+/NADPH
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synthesis
Rhodotorula sp. AS2.2241
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the enzyme can be used for stereospecific interconversion of (R)-1-phenylethanol and (S)-1-phenylethanol via the oxoform together with the (R)-specific secondary alcohol dehydrogenase using whole cells as biocatalysts that include the required cofactor regenration system, method, overview. Optically pure secondary alcohols are widely used in pharmaceuticals, flavors, agricultural chemicals and specialty materials
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