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Literature summary for 7.1.1.2 extracted from
- Effect of pH on the steady state kinetics of bovine heart NADH:coenzyme Q oxidoreductase (2003), J. Bioenerg. Biomembr., 35, 419-425.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km-values for decylubiquinone are measured at pH-values 6.5 and 9.0 at different concentrations of the cosubstrate NADH. Km-values for NADH are measured at pH values 6.5, 7.0, 7.5, 8.0, 8.5 and 9.0 and at different concentrations of the cosubstrate decylubiquinone | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NADH + decylubiquinone | ordered sequential mechanism in which the order of substrate bindings and product release is: NADH, decylubiquinone, decylubiquinol, NAD+ | Bos taurus | NAD+ + decylubiquinol | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NADH:coenzyme Q oxidoreductase | - |
Bos taurus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
only NADH binding to the enzyme in pH-dependent. NADH binding to the free enzyme is accelerated by protonation of an amino acid (possibly His) | Bos taurus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Bos taurus | |
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Release 2023.1 (January 2023)
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