Protein Variants | Comment | Organism |
---|---|---|
E221S the | mutation produces a 170fold decrease in the Vm/Km with NADH because of a simultaneous 16fold increase in the Km value and an 11fold decrease in the Vm value, the mutation provides a positive effect on NADPH coenzyme specificity | Saccharomyces cerevisiae |
E221S/I222R | mutant with preference for NADPH as coenzyme | Saccharomyces cerevisiae |
E221S/I222R/A223S | mutant with preference for NADPH as coenzyme | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.044 | - |
NADPH | mutant enzyme E221S/I222R | Saccharomyces cerevisiae | |
0.044 | - |
NADPH | mutant enzyme E221S/I222R/A223S | Saccharomyces cerevisiae | |
0.045 | - |
NADH | wild type enzyme | Saccharomyces cerevisiae | |
0.087 | - |
NADPH | mutant enzyme E221S | Saccharomyces cerevisiae | |
0.7 | - |
NADH | mutant enzyme E221S | Saccharomyces cerevisiae | |
3 | - |
(R)-acetoin | wild type enzyme | Saccharomyces cerevisiae | |
33 | - |
(R)-acetoin | mutant enzyme E221S/I222R/A223S | Saccharomyces cerevisiae | |
77 | - |
(R)-acetoin | mutant enzyme E221S/I222R | Saccharomyces cerevisiae | |
161 | - |
(R)-acetoin | mutant enzyme E221S | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P39714 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.1 | - |
wild type enzyme, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
4.1 | - |
mutant enzyme E221S, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
4.8 | - |
mutant enzyme E221S/I222R, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
6.1 | - |
mutant enzyme E221S/I222R/A223S, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
13.7 | - |
mutant enzyme E221S, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
54.7 | - |
mutant enzyme E221S/I222R, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
92 | - |
wild type enzyme, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
93.2 | - |
mutant enzyme E221S/I222R/A223S, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-acetoin + NADH + H+ | - |
Saccharomyces cerevisiae | (2R,3R)-butane-2,3-diol + NAD+ | - |
? | |
(R)-acetoin + NADPH + H+ | wild type enzyme does not use NADPH as coenzyme | Saccharomyces cerevisiae | (2R,3R)-butane-2,3-diol + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
(2R,3R)-2,3-butanediol dehydrogenase | - |
Saccharomyces cerevisiae |
BDH1 | - |
Saccharomyces cerevisiae |
NAD(H)-dependent 2,3-butanediol dehydrogenase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Saccharomyces cerevisiae |