Any feedback?
Literature summary extracted from
- Influence of tungstate on the formation and activities of four reductases in Proteus mirabilis: identification of two new molybdo-enzymes: chlorate reductase and tetrathionate reductase (1979), FEBS Lett., 106, 43-46.
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.97.1.1 | Mo | molybdo-enzyme | Proteus mirabilis |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.97.1.1 | Proteus mirabilis | - |
enzyme formed during anaerobic growth without nitrate | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.97.1.1 | additional information | - |
- |
Proteus mirabilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.97.1.1 | chlorate + reduced electron acceptor | the only known substrate is chlorate | Proteus mirabilis | chlorite + H2O + oxidized electron acceptor | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.97.1.1 | molybdenum cofactor | molybdo-enzyme | Proteus mirabilis | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
