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EC Number
Amino acid exchange
activity with NADPH as cofactor decreased to about 50% of wild-type, activity with NADH strongly decreased
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
activity with NADH is decreased relative to Arg38Pro alone, but is higher than that of the wild-type enzyme
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
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
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
no activity with NADPH as cofactor
no activity with NADPH as cofactor, fourfold increase in activity with NADH
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
180% of wild-type activity
Results 1 - 10 of 12 > >>