1.1.1.B4: (R)-specific secondary alcohol dehydrogenase (NADH)
This is an abbreviated version!
For detailed information about (R)-specific secondary alcohol dehydrogenase (NADH), go to the full flat file.
Word Map on EC 1.1.1.B4
Reaction
Synonyms
(R)-1-phenylethanolsynthase, (R)-epinephrine dehydrogenase, ADH, ADH1, ADH2, ADHTt, carbonyl reductase, carbonyl reductase (NADH, specific for (S)-configuration of alcohol), CHY1186, CpCR, mLDH, More, RPES, SADH, SDR, secondary alcohol dehydrogenase, short chain dehydrogenase, short-chain NAD(H)-dependent alcohol dehydrogenase
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1.1.1.B4 (R)-specific secondary alcohol dehydrogenase (NADH)Advanced search results
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results (Engineering
Engineering on EC 1.1.1.B4 - (R)-specific secondary alcohol dehydrogenase (NADH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S154Y
mutant exhibits nearly 13fold, 5.4fold, and 2.3fold increase in kcat/Km value, kcat value, and specific activity toward 3,5-bis(trifluoromethyl)acetophenone
S154Y
-
mutant exhibits nearly 13fold, 5.4fold, and 2.3fold increase in kcat/Km value, kcat value, and specific activity toward 3,5-bis(trifluoromethyl)acetophenone
-
A90S
-
activity with NADPH as cofactor decreased to about 50% of wild-type, activity with NADH strongly decreased
G37D/R38P
-
activity with NADH is decreased relative to Arg38Pro alone, but is higher than that of the wild-type enzyme
R38P
-
no activity with NADPH as cofactor, fourfold increase in activity with NADH
V112D
-
no activity with NADPH as cofactor, strongly decreased activity with NADH
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
C295A
-
the mutant shows an increased size of the alkyl group which can bind in the substrate small pocket by one carbon atom compared to the wild-type enzyme
I86A
I86A/C295A
-
the mutant enzyme shows broadened substrate specificity for aryl ketones and broadened substrate specificity for meta-substituted, but not para-substituted, acetophenones compared to the wild-type enzyme. The increase of the substrate specificity of I86A/C295A SADH is accompanied by a decrease in the kcat/Km values of acetophenones, possibly due to the substrates fitting loosely inside the more open active site
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 altered substrate specificity and expands substrate specificity to include acetophenone, which is a very poor substrate for wild-type SADH, but also reverses the usual preferred stereochemistry to produce the anti-prelog R-product. I86A SADH exhibits limited reactivity with substituted acetophenones, fluorine being the only tolerable substituent
