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Literature summary for 1.7.7.2 extracted from
- Nitrate reduction in Haloferax alexandrinus the case of assimilatory nitrate reductase (2017), Extremophiles, 21, 551-561 .
General Stability
| General Stability | Organism |
|---|---|
| enzyme requires high salt concentration for stability and activity | Haloferax alexandrinus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax alexandrinus | M0HXK1 | - |
- |
| Haloferax alexandrinus JCM 10717 | M0HXK1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Sepharose 4B, DEAE cellulose, Sephacryl S-300 chromatographies | Haloferax alexandrinus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.23 | - |
pH not specified in the publication, temperature not specified in the publication | Haloferax alexandrinus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme does not use electrons from either NADH or NADPH. Dithionite is not able to reduce nitrate in the absence of reduced methyl viologen | Haloferax alexandrinus | ? | - |
- |
 |
| additional information | enzyme does not use electrons from either NADH or NADPH. Dithionite is not able to reduce nitrate in the absence of reduced methyl viologen | Haloferax alexandrinus JCM 10717 | ? | - |
- |
|
| reduced methyl viologen + nitrate | - |
Haloferax alexandrinus | methyl viologen + nitrite | - |
? | |
| reduced methyl viologen + nitrate | - |
Haloferax alexandrinus JCM 10717 | methyl viologen + nitrite | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 72000, SDS-PAGE | Haloferax alexandrinus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| C452_13229 | - |
Haloferax alexandrinus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
- |
Haloferax alexandrinus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Fe-S center | presence of Fe-S clusters, with peak up to 450 nm in the fully reduced protein | Haloferax alexandrinus | |
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