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
1.1.1.B3 (S)-specific secondary alcohol dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.1.1.B3 - (S)-specific secondary alcohol dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
W288L
the enantiopreference oft he mutant is intermediate between wild type (S)-selectivity and (R)-selectivity
W288M
the enantiopreference of the mutant enzyme is similar to wild type ((S)-selectivity)
W288L
Geotrichum candidum NBRC 4597
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the enantiopreference oft he mutant is intermediate between wild type (S)-selectivity and (R)-selectivity
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W288M
Geotrichum candidum NBRC 4597
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the enantiopreference of the mutant enzyme is similar to wild type ((S)-selectivity)
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W95L/N249Y
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the mutant exhibits higher activity but decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+ and NADH compared to the wild type enzyme, optimum pH is at about pH 8.6
I86A
W110A
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the mutant shows imperfect wild type stereoselectivity (S)
W110A/I86A
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the mutant enzyme is completely non-stereoselective for the reduction of 2-hexanone.Additionally, an extremely low level of stereoselectivity (i.e. from 10% to 24%) is observed for the reduction of aryl-aliphatic ketones and aliphatic ketones
additional information
I86A
site-directed mutagensis, the secondary alcohol dehydrogenase I86A mutant is stereospecific for (R)-alcohols instead of (S)-alcohols, in contrast to the wild-type enzyme, the mutation I86A allows large substituents to fit into the large pocket of I86ATeSADH, which corresponds to the small pocket in wild-type TeSADH, modeling of the stereopreference of TeSADH I86A
I86A
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the mutant shows reversed stereoselectivity (R) compared to the wild type enzyme
additional information
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covalent immobilization of the purified recombinant enzyme on different supports, i.e. on glyoxyl agarose, amino epoxy agarose, CNBr-activated sepharose, monoaminoethyl-N-ethylagarose-glutaraldehyde, monoaminoethyl-N-ethyl agarose, or polyethyleneimine agarose, immobilized enzyme activities, overview
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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covalent immobilization of the purified recombinant enzyme on different supports, i.e. on glyoxyl agarose, amino epoxy agarose, CNBr-activated sepharose, monoaminoethyl-N-ethylagarose-glutaraldehyde, monoaminoethyl-N-ethyl agarose, or polyethyleneimine agarose, immobilized enzyme activities, overview
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