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Literature summary extracted from
- The molybdenum cofactor enzyme mARC moonlighting or promiscuous enzyme? (2017), Biofactors, 43, 486-494 .
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.1 | additional information | plant nitrate reductase-dependent mARC activity, NOFNiR, can catalyze NO production from nitrite in the presence of millimolar concentrations of nitrate, which strongly inhibits the NO producing nitrite reductase activity of the nitrate reductase | Chlamydomonas reinhardtii |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.7.1.1 | cytoplasm | - |
Chlamydomonas reinhardtii | 5737 | - |
| 1.7.1.1 | cytoplasm | - |
Homo sapiens | 5737 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.1 | Fe2+ | heme | Chlamydomonas reinhardtii |  |
| 1.7.1.1 | Fe2+ | heme | Homo sapiens | |
| 1.7.1.1 | Molybdenum | present in the active center | Chlamydomonas reinhardtii | |
| 1.7.1.1 | Molybdenum | present in the active center | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.1.1 | additional information | Chlamydomonas reinhardtii | the nitrate reductase interacts with the crARC in Chlamydomonas reinhardtii | ? | - |
? | |
| 1.7.1.1 | nitrate + NADH + H+ | Chlamydomonas reinhardtii | - |
nitrite + NAD+ | - |
r | |
| 1.7.1.1 | nitrate + NADH + H+ | Homo sapiens | - |
nitrite + NAD+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.7.1.1 | Chlamydomonas reinhardtii | - |
- |
- |
| 1.7.1.1 | Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.1.1 | additional information | the nitrate reductase interacts with the crARC in Chlamydomonas reinhardtii | Chlamydomonas reinhardtii | ? | - |
? | |
| 1.7.1.1 | nitrate + NADH + H+ | - |
Chlamydomonas reinhardtii | nitrite + NAD+ | - |
r | |
| 1.7.1.1 | nitrate + NADH + H+ | - |
Homo sapiens | nitrite + NAD+ | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.7.1.1 | homodimer | each monomer folds into five functional domains. Three of these domains are involved in the binding of cofactors: the N-terminal Moco domain, the central cytochrome b5 heme domain and the C-terminal FAD domain. The other two domains are a dimerization and an NAD(P)H-binding domain. For dimerization, heme and FAD domains are connected by protease-sensitive sequences termed hinge-I and -II | Chlamydomonas reinhardtii |
| 1.7.1.1 | homodimer | each monomer folds into five functional domains. Three of these domains are involved in the binding of cofactors: the N-terminal Moco domain, the central cytochrome b5 heme domain and the C-terminal FAD domain. The other two domains are a dimerization and an NAD(P)H-binding domain. For dimerization, heme and FAD domains are connected by protease-sensitive sequences termed hinge-I and -II | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.7.1.1 | nitrate reductase | - |
Chlamydomonas reinhardtii |
| 1.7.1.1 | nitrate reductase | - |
Homo sapiens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.1.1 | cytochrome b5 | with heme, central domain | Chlamydomonas reinhardtii | |
| 1.7.1.1 | cytochrome b5 | with heme, central domain | Homo sapiens | |
| 1.7.1.1 | FAD | C-terminal domain | Chlamydomonas reinhardtii | |
| 1.7.1.1 | FAD | C-terminal domain | Homo sapiens | |
| 1.7.1.1 | molybdenum cofactor | N-terminal domain | Chlamydomonas reinhardtii | |
| 1.7.1.1 | molybdenum cofactor | N-terminal domain | Homo sapiens | |
| 1.7.1.1 | NADH | - |
Chlamydomonas reinhardtii | |
| 1.7.1.1 | NADH | - |
Homo sapiens | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.7.1.1 | Chlamydomonas reinhardtii | ammonium strongly downregulates nitrate reductase expression | down |
| 1.7.1.1 | Chlamydomonas reinhardtii | Chlamydomonas mARC and nitrate reductase NR are intimately connected at the level of transcription and activity | additional information |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.7.1.1 | evolution | the enzyme contains a cysteine ligand and two oxido-ligands, and is a member of the sulfite oxidase, SO, family, defined by the identity of the ligands bound to the Mo center | Chlamydomonas reinhardtii |
| 1.7.1.1 | evolution | the enzyme contains a cysteine ligand and two oxido-ligands, and is a member of the sulfite oxidase, SO, family, defined by the identity of the ligands bound to the Mo center | Homo sapiens |
| 1.7.1.1 | metabolism | the reductive NO production pathway uses nitrite as substrate for NO production and involves either the nitrate reductase enzyme, the plasma membrane-bound nitrite:NO reductase, or mitochondrial nitrite reduction | Homo sapiens |
| 1.7.1.1 | metabolism | the reductive NO production pathway uses nitrite as substrate for NO production and involves either the nitrate reductase enzyme, the plasma membrane-bound nitrite:NO reductase, or mitochondrial nitrite reduction. Plant nitrate reductase-dependent mARC activity, NOFNiR, can catalyze NO production from nitrite in the presence of millimolar concentrations of nitrate, which strongly inhibits the NO producing nitrite reductase activity of the nitrate reductase. Two molybdoenzymes, nitrate reductase NR and nitrate reductase-dependent mARC, are needed together for NO production in plants. The dual system NR and mARC is the major player for NO production in plants. This cytosolic NO synthesis is strictly dependent on the nitrate reductase-diaphorase activity, and independent of the Moco domain of nitrate reductase | Chlamydomonas reinhardtii |
| 1.7.1.1 | physiological function | the enzyme, instead of cytochrome b5 components, provides the electrons required for the reduction of nitrite to NO by amidoxime reducing component, i.e. crARC, or NO forming nitrite reductase, i.e. NOFNiR, respectively. Eukaryotic nitrate reductase is a cytoplasmic enzyme that catalyzes the reduction of nitrate to nitrite, which is the first step of nitrate assimilation in plants, algae and fungi. To synthesize NO from nitrite, nitrate reductase is able to substitute Cytb5 and Cytb5-R by mARC as acceptors of the electrons coming from NAD(P)H. NItrate reductase is playing a central role in plant biology by modulating the levels of NO | Chlamydomonas reinhardtii |
| 1.7.1.1 | physiological function | the enzyme, instead of cytochrome b5 components, provides the electrons required for the reduction of nitrite to NO by mitochondrial amidoxime reducing component, i.e. mARC, or NO forming nitrite reductase, i.e. NOFNiR, respectively. Eukaryotic nitrate reductase is a cytoplasmic enzyme that catalyzes the reduction of nitrate to nitrite, which is the first step of nitrate assimilation in plants, algae and fungi | Homo sapiens |
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Release 2023.1 (January 2023)
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