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Literature summary for 1.1.5.10 extracted from
- Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase (1969), Biochem. J., 115, 55-64.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| oxalate | - |
Oryctolagus cuniculus |  |
| oxaloacetate | - |
Oryctolagus cuniculus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Oryctolagus cuniculus | 5739 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 95000 | - |
combination of gel filtration data and the sedimentation coefficient | Oryctolagus cuniculus |
| 102000 | - |
gel filtration | Oryctolagus cuniculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | cortex | Oryctolagus cuniculus | - |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, 50 mM Tris-chloride buffer, pH 8-0, in the dark, stable for several weeks | Oryctolagus cuniculus |
| 4°C, as a precipitate in 32% (w/v) ammonium sulfate solution in 50 mM Tris-chloride buffer, pH 8.0, stable for several months | Oryctolagus cuniculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-lactate + oxidized 2,6-dichloroindophenol | - |
Oryctolagus cuniculus | pyruvate + reduced 2,6-dichloroindophenol | - |
? | |
| D-lactate + ubiquinone | the rate with 0.06 mM ubiquinone is 72% of the rate with 2,6-dichloroindophenol | Oryctolagus cuniculus | pyruvate + ubiquinol | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (R)-2-hydroxy acid dehydrogenase | - |
Oryctolagus cuniculus |
| (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase | - |
Oryctolagus cuniculus |
| D-lactate dehydrogenase | ambiguous | Oryctolagus cuniculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Oryctolagus cuniculus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
pH 5.5-10, 30 min, stable | Oryctolagus cuniculus |
| 62 | - |
pH 7.3, activity decreases by 79% in 10 min, in the presence of 1 mM oxalate the decrease is 5% | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.6 | - |
assay at | Oryctolagus cuniculus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4.8 | - |
20°C, 30 min, stable above pH 10.5 or below pH 4.8 | Oryctolagus cuniculus |
| 5.5 | 10 | 20°C, 30 min, stable | Oryctolagus cuniculus |
| 7.3 | - |
unstable above 55°C | Oryctolagus cuniculus |
| 10.5 | - |
20°C, 30 min, stable above pH 10.5 or below pH 4.8 | Oryctolagus cuniculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the purified enzyme has a spectrum typical of a flavoprotein. The change induced in the spectrum on addition of D-malate or D-lactate suggests the formation of a flavin semiquinone. Flavin can be removed by treatment with acid ammonium sulfate, and activity can be restored to the inactive apoenzyme by addition of FAD, but not of FMN or riboflavin | Oryctolagus cuniculus | |
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Release 2023.1 (January 2023)
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