Crystallization (Comment) | Organism |
---|---|
isozyme YADH-1, crystal structure analysis | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
D223G | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
D223G/G225R | nearly inactive mutant | Saccharomyces cerevisiae |
D49N | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
DELTAA200/A201L | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
E68Q | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
G204A | nearly inactive mutant | Saccharomyces cerevisiae |
G224I | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
G225R | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
H47R | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
H51E | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
H51Q | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
L203A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
L203A/T178S | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
M294L | increased activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
S198F | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
S269I | nearly inactive mutant | Saccharomyces cerevisiae |
T48A | inactive mutant | Saccharomyces cerevisiae |
T48C | inactive mutant | Saccharomyces cerevisiae |
T48S | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
T48S/T93A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
T48S/W57M/W93A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
W57L | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
W57M | slightly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
W93A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | wild-type and mutant forms of the 3 isozymes, steady-state kinetics, detailed kinetic analysis, at different pH values and temperatures | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | all isozymes, amino acid residues involved in zinc in binding are Cys46, Cys174, His67, Glu68, Asp49, and Thr48, binding mode | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
isozyme YADH-1, YADH-2, and YADH-3 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a primary alcohol + NAD+ = an aldehyde + NADH + H+ | detailed determination of the reaction and kinetic mechanisms, active site structure and determination of amino acid residues involved in catalysis, 3 isozymes | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-2-butanol + NAD+ | - |
Saccharomyces cerevisiae | 2-butanone + NADH | - |
r | |
allyl alcohol + NAD+ | - |
Saccharomyces cerevisiae | acrolein + NADH | - |
r | |
ethanol + NAD+ | - |
Saccharomyces cerevisiae | acetaldehyde + NADH | - |
r | |
ethylenglycol + NAD+ | - |
Saccharomyces cerevisiae | ? + NADH | - |
r | |
additional information | substrate specificity and stereospecificity, substrate binding pocket structure of the 3 isozymes, involving Met294, Trp57, and Trp93 | Saccharomyces cerevisiae | ? | - |
? | |
n-butanol + NAD+ | - |
Saccharomyces cerevisiae | n-butanal + NADH | - |
r | |
n-decanol + NAD+ | - |
Saccharomyces cerevisiae | n-decanal + NADH | - |
r | |
n-hexanol + NAD+ | - |
Saccharomyces cerevisiae | n-hexanal + NADH | - |
r | |
n-propanol + NAD+ | - |
Saccharomyces cerevisiae | n-propanal + NADH | - |
r | |
Tris + NAD+ | - |
Saccharomyces cerevisiae | ? + NADH | - |
r |
Synonyms | Comment | Organism |
---|---|---|
YADH | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 30 | assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | cofactor binding mode | Saccharomyces cerevisiae | |
NADH | cofactor binding mode | Saccharomyces cerevisiae |