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Literature summary for 1.7.1.1 extracted from
- Limited proteolysis of the nitrate reductase from spinach leaves (1988), J. Biol. Chem., 263, 19684-19689.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Molybdenum | molybdenum, heme and FAD components are localized in distinct domains which are covalently linked by exposed hinge regions. The molybdenum domain appears to be important in the maintenance of subunit interactions in the enzyme complex | Spinacia oleracea |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Spinacia oleracea | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Spinacia oleracea | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrate + NADH | - |
Spinacia oleracea | nitrite + NAD+ + H2O | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | molybdenum, heme and FAD components are localized in distinct domains which are covalently linked by exposed hinge regions | Spinacia oleracea | |
| heme | molybdenum, heme and FAD components are localized in distinct domains which are covalently linked by exposed hinge regions | Spinacia oleracea | |
| NADH | - |
Spinacia oleracea | |
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Release 2023.1 (January 2023)
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