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Literature summary for 2.7.1.86 extracted from
- Orientation and reactivity of NADH kinase in proteoliposomes (1989), J. Biochem., 105, 922-926.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| acetate | maximal enhancement of activity, about 7fold is observed with 100 mM acetate, enzyme reconstituted in liposomes, maximal enhancement of solubilized enzyme with 400 mM acetate | Saccharomyces cerevisiae |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| phosphoenolpyruvate | 20 mM, 63% inhibition, reconstituted enzyme. Solubilized enzyme is inhibited 55% by 30 mM | Saccharomyces cerevisiae | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.027 | - |
NADH | NADH kinase reconstituted in liposomes | Saccharomyces cerevisiae | |
| 0.105 | - |
NADH | solubilized enzyme form | Saccharomyces cerevisiae | |
| 0.133 | - |
ATP | NADH kinase reconstituted in liposomes | Saccharomyces cerevisiae | |
| 2.1 | - |
ATP | solubilized enzyme form | Saccharomyces cerevisiae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
| Saccharomyces cerevisiae X2181-1A | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + NADH | - |
Saccharomyces cerevisiae | ADP + NADPH | - |
? | |
| ATP + NADH | - |
Saccharomyces cerevisiae X2181-1A | ADP + NADPH | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
NADH kinase reconstituted in liposomes | Saccharomyces cerevisiae |
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