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Literature summary extracted from
- Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase (2000), Eur. J. Biochem., 267, 1092-1099.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.13.9 | fusion protein with glutathione-S-transferase | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.9 | Cl- | 70% inhibition with 0.1 M NaCl or KCl, competitive with respect to NADPH and non-competitive with respect to L-kynurenine | Rattus norvegicus |  |
| 1.14.13.9 | pyridoxal | less potent than pyridoxal phosphate | Rattus norvegicus | |
| 1.14.13.9 | pyridoxal 5'-phosphate | non competitive inhibition | Rattus norvegicus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.13.9 | mitochondrial outer membrane | - |
Rattus norvegicus | 5741 | - |
| 1.14.13.9 | mitochondrion | - |
Rattus norvegicus | 5739 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.9 | 55000 | - |
SDS-PAGE | Rattus norvegicus |
| 1.14.13.9 | 55760 | - |
calculated from primary sequence | Rattus norvegicus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.9 | Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.13.9 | fusion protein with gluthatione-S-transferase | Rattus norvegicus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.13.9 | liver | - |
Rattus norvegicus | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.9 | 0.028 | - |
NADPH oxidase activity | Rattus norvegicus |
| 1.14.13.9 | 2 | - |
fusion protein with glutathione-S-transferase | Rattus norvegicus |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.14.13.9 | -80°C stable for 6 months | Rattus norvegicus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.9 | L-kynurenine + NADPH + O2 | - |
Rattus norvegicus | 3-hydroxy-L-kynurenine + NADP+ + H2O | - |
r | |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.9 | 37 | - |
stable for four hours | Rattus norvegicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.9 | 7.5 | - |
fusion protein with glutathione-S-transferase | Rattus norvegicus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.9 | 7 | 9 | about 50% of maximal activity at pH 7 and 9 | Rattus norvegicus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.9 | FAD | one molecule non-covalently bound FAD per molecule of enzyme | Rattus norvegicus | |
| 1.14.13.9 | NADH | less effective than NADPH | Rattus norvegicus | |
| 1.14.13.9 | NADPH | - |
Rattus norvegicus | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.9 | 0.19 | - |
pyridoxal 5'-phosphate | - |
Rattus norvegicus | |
| 1.14.13.9 | 1 | - |
pyridoxal | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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