EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.1 | isozyme YADH-1, crystal structure analysis | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.1 | D223G | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | D223G/G225R | nearly inactive mutant | Saccharomyces cerevisiae |
1.1.1.1 | D49N | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | DELTAA200/A201L | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | E68Q | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | G204A | nearly inactive mutant | Saccharomyces cerevisiae |
1.1.1.1 | G224I | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | G225R | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | H47R | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | H51E | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | H51Q | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | L203A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | L203A/T178S | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | M294L | increased activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | S198F | highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | S269I | nearly inactive mutant | Saccharomyces cerevisiae |
1.1.1.1 | T48A | inactive mutant | Saccharomyces cerevisiae |
1.1.1.1 | T48C | inactive mutant | Saccharomyces cerevisiae |
1.1.1.1 | T48S | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | T48S/T93A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | T48S/W57M/W93A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | W57L | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | W57M | slightly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
1.1.1.1 | W93A | reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.1 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.1 | Zn2+ | all isozymes, amino acid residues involved in zinc in binding are Cys46, Cys174, His67, Glu68, Asp49, and Thr48, binding mode | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.1 | Saccharomyces cerevisiae | - |
isozyme YADH-1, YADH-2, and YADH-3 | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.1.1 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.1 | (S)-2-butanol + NAD+ | - |
Saccharomyces cerevisiae | 2-butanone + NADH | - |
r | |
1.1.1.1 | allyl alcohol + NAD+ | - |
Saccharomyces cerevisiae | acrolein + NADH | - |
r | |
1.1.1.1 | ethanol + NAD+ | - |
Saccharomyces cerevisiae | acetaldehyde + NADH | - |
r | |
1.1.1.1 | ethylenglycol + NAD+ | - |
Saccharomyces cerevisiae | ? + NADH | - |
r | |
1.1.1.1 | additional information | substrate specificity and stereospecificity, substrate binding pocket structure of the 3 isozymes, involving Met294, Trp57, and Trp93 | Saccharomyces cerevisiae | ? | - |
? | |
1.1.1.1 | n-butanol + NAD+ | - |
Saccharomyces cerevisiae | n-butanal + NADH | - |
r | |
1.1.1.1 | n-decanol + NAD+ | - |
Saccharomyces cerevisiae | n-decanal + NADH | - |
r | |
1.1.1.1 | n-hexanol + NAD+ | - |
Saccharomyces cerevisiae | n-hexanal + NADH | - |
r | |
1.1.1.1 | n-propanol + NAD+ | - |
Saccharomyces cerevisiae | n-propanal + NADH | - |
r | |
1.1.1.1 | Tris + NAD+ | - |
Saccharomyces cerevisiae | ? + NADH | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.1 | YADH | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.1 | 25 | 30 | assay at | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.1 | NAD+ | cofactor binding mode | Saccharomyces cerevisiae | |
1.1.1.1 | NADH | cofactor binding mode | Saccharomyces cerevisiae |