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
results (
results (Results
in table
6
26
61
11
38
Engineering
Engineering on EC 1.1.1.B3 - (S)-specific secondary alcohol dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
-
the enantiopreference oft he mutant is intermediate between wild type (S)-selectivity and (R)-selectivity
-
W288M
Geotrichum candidum NBRC 4597
-
the enantiopreference of the mutant enzyme is similar to wild type ((S)-selectivity)
-
W95L/N249Y
-
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
-
the mutant shows imperfect wild type stereoselectivity (S)
W110A/I86A
-
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
-
the mutant shows reversed stereoselectivity (R) compared to the wild type enzyme
additional information
-
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
-
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
-
