EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.4 | 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 |
1.1.1.4 | E221S/I222R | mutant with preference for NADPH as coenzyme | Saccharomyces cerevisiae |
1.1.1.4 | E221S/I222R/A223S | mutant with preference for NADPH as coenzyme | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.4 | 0.044 | - |
NADPH | mutant enzyme E221S/I222R | Saccharomyces cerevisiae | |
1.1.1.4 | 0.044 | - |
NADPH | mutant enzyme E221S/I222R/A223S | Saccharomyces cerevisiae | |
1.1.1.4 | 0.045 | - |
NADH | wild type enzyme | Saccharomyces cerevisiae | |
1.1.1.4 | 0.087 | - |
NADPH | mutant enzyme E221S | Saccharomyces cerevisiae | |
1.1.1.4 | 0.7 | - |
NADH | mutant enzyme E221S | Saccharomyces cerevisiae | |
1.1.1.4 | 3 | - |
(R)-acetoin | wild type enzyme | Saccharomyces cerevisiae | |
1.1.1.4 | 33 | - |
(R)-acetoin | mutant enzyme E221S/I222R/A223S | Saccharomyces cerevisiae | |
1.1.1.4 | 77 | - |
(R)-acetoin | mutant enzyme E221S/I222R | Saccharomyces cerevisiae | |
1.1.1.4 | 161 | - |
(R)-acetoin | mutant enzyme E221S | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.4 | Saccharomyces cerevisiae | P39714 | - |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.4 | 0.1 | - |
wild type enzyme, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 4.1 | - |
mutant enzyme E221S, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 4.8 | - |
mutant enzyme E221S/I222R, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 6.1 | - |
mutant enzyme E221S/I222R/A223S, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 13.7 | - |
mutant enzyme E221S, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 54.7 | - |
mutant enzyme E221S/I222R, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 92 | - |
wild type enzyme, using 1 mM NADH as cosubstrate | Saccharomyces cerevisiae |
1.1.1.4 | 93.2 | - |
mutant enzyme E221S/I222R/A223S, using 1 mM NADPH as cosubstrate | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.4 | (R)-acetoin + NADH + H+ | - |
Saccharomyces cerevisiae | (2R,3R)-butane-2,3-diol + NAD+ | - |
? | |
1.1.1.4 | (R)-acetoin + NADPH + H+ | wild type enzyme does not use NADPH as coenzyme | Saccharomyces cerevisiae | (2R,3R)-butane-2,3-diol + NADP+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.4 | (2R,3R)-2,3-butanediol dehydrogenase | - |
Saccharomyces cerevisiae |
1.1.1.4 | BDH1 | - |
Saccharomyces cerevisiae |
1.1.1.4 | NAD(H)-dependent 2,3-butanediol dehydrogenase | - |
Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.4 | NADH | - |
Saccharomyces cerevisiae |