ENZYME entry: EC 1.18.6.2
| Accepted Name |
|---|
| Vanadium-dependent nitrogenase.
|
| Reaction catalysed |
|---|
| 12 reduced ferredoxin + 12 H(+) + N(2) + 40 ATP + 40 H(2)O <=> 12 oxidized ferredoxin + 3 H(2) + 2 NH(3) + 40 ADP + 40 phosphate |
| Cofactor(s) |
|---|
| Mg(2+).
|
| Comment(s) |
|---|
- This enzyme, originally isolated from the bacterium Azotobacter
vinelandii, is a complex of two components (namely dinitrogen
reductase and dinitrogenase).
- Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of
ATP, transfers an electron from ferredoxin to the dinitrogenase
component.
- Dinitrogenase is a vanadium-iron protein that reduces dinitrogen to
two molecules of ammonia in three successive two-electron reductions
via diazine and hydrazine.
- Compared with EC 1.18.6.1, this enzyme produces more dihydrogen and
consumes more ATP per dinitrogen molecule being reduced.
- Unlike EC 1.18.6.1, this enzyme can also use CO as substrate,
producing ethylene, ethane and propane.
|
| Cross-references |
|---|
| BRENDA | 1.18.6.2 |
| EC2PDB | 1.18.6.2 |
| ExplorEnz | 1.18.6.2 |
| PRIAM enzyme-specific profiles | 1.18.6.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.18.6.2 |
| IUBMB Enzyme Nomenclature | 1.18.6.2 |
| IntEnz | 1.18.6.2 |
| MEDLINE | Find literature relating to 1.18.6.2 |
| MetaCyc | 1.18.6.2 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.18.6.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.18.-.-
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