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Results 1 - 10 of 12 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4A90S activity with NADPH as cofactor decreased to about 50% of wild-type, activity with NADH strongly decreased 711860
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4C295A 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 741784
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4G37D/R38P activity with NADH is decreased relative to Arg38Pro alone, but is higher than that of the wild-type enzyme 711860
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4I86A 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 723841
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4I86A 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 741784
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4I86A/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 741784
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4M140I no activity with NADPH as cofactor 711860
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4R38P no activity with NADPH as cofactor, fourfold increase in activity with NADH 711860
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4S154Y 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 -, 739942
Show all pathways known for 1.1.1.B4Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B4S154Y/L194I 180% of wild-type activity -, 739942
Results 1 - 10 of 12 > >>