Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ethanol | presence of ethanol or isopropanol and alkalization of the medium sharply activates the NADH:p-NTF-reductase reaction, activity with ubiquinone is also activated | Saccharomyces cerevisiae | |
Isopropanol | presence of ethanol or isopropanol and alkalization of the medium sharply activates the NADH:p-NTF-reductase reaction, activity with ubiquinone is also activated | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | reaction kinetics at different pH values, overview | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | required | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P00330 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P00330 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Saccharomyces cerevisiae | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrotetrazolium violet + NADH + H+ | p-NTF, the tetrazolium contacts with NADH on the enzyme surface without intermediate carriers (the zinc in the active ADH site is not a electron carrier) and accepts electrons. Alcohols are not able to reduce p-NTF | Saccharomyces cerevisiae | a formazan + NAD+ | - |
? | |
4-nitrotetrazolium violet + NADH + H+ | p-NTF, the tetrazolium contacts with NADH on the enzyme surface without intermediate carriers (the zinc in the active ADH site is not a electron carrier) and accepts electrons. Alcohols are not able to reduce p-NTF | Saccharomyces cerevisiae ATCC 204508 | a formazan + NAD+ | - |
? | |
additional information | a quasi-vibrational process is detected with the use of HEPES buffer in the presence of alcohol: NADH is rapidly oxidized to NAD+ by ubiquinone and NAD+ is then slowly reduced to NADH by the alcohol. The NADH:ubiquinone-and alcohol:NAD+-reductase reactions are partially separated in time caused by considerable differences in the values of binding constants of NADH and NAD+ molecules | Saccharomyces cerevisiae | ? | - |
- |
|
additional information | a quasi-vibrational process is detected with the use of HEPES buffer in the presence of alcohol: NADH is rapidly oxidized to NAD+ by ubiquinone and NAD+ is then slowly reduced to NADH by the alcohol. The NADH:ubiquinone-and alcohol:NAD+-reductase reactions are partially separated in time caused by considerable differences in the values of binding constants of NADH and NAD+ molecules | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
ubiquinone + NADH + H+ | - |
Saccharomyces cerevisiae | ubiquinol + NAD+ | - |
? | |
ubiquinone + NADH + H+ | - |
Saccharomyces cerevisiae ATCC 204508 | ubiquinol + NAD+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADH | - |
Saccharomyces cerevisiae |
ADH1 | - |
Saccharomyces cerevisiae |
NADH:p-NTF-reductase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 9 | - |
Saccharomyces cerevisiae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 9 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Saccharomyces cerevisiae |