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Literature summary for 1.14.13.9 extracted from
- cDNA cloning, functional expression and characterization of kynurenine 3-hydroxylase of Anopheles stephensi (Diptera: Culicidae) (2002), Insect Mol. Biol., 11, 497-504.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| AsK3H, DNA and amino acid sequence determination and analysis, functional expression in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, membrane associated | Anopheles stephensi |
General Stability
| General Stability | Organism |
|---|---|
| purified recombinant enzyme is highly unstable, activity decreases directly after purification also at -80°C | Anopheles stephensi |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 60000 | - |
x * 60000, recombinant enzyme, SDS-PAGE | Anopheles stephensi |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-kynurenine + NADPH + O2 | Anopheles stephensi | the enzyme is not involved in regulation of 3-hydroxy-L-kynurenine level in vivo | 3-hydroxy-L-kynurenine + NADP+ + H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Anopheles stephensi | Q8ISJ5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Sf9 insect cells by solubilization with Triton X-100 and affinity chromatography | Anopheles stephensi |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| egg | - |
Anopheles stephensi | - |
| larva | - |
Anopheles stephensi | - |
| additional information | constitutive expression of the enzyme in all developmental stages from egg via larva and pupa to adult mosquito | Anopheles stephensi | - |
| pupa | - |
Anopheles stephensi | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.095 | - |
recombinant enzyme in crude Sf9 cell lysate | Anopheles stephensi |
| 0.866 | - |
purified recombinant enzyme | Anopheles stephensi |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -80°C, purified recombinant enzyme, not stable | Anopheles stephensi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-kynurenine + NADPH + O2 | - |
Anopheles stephensi | 3-hydroxy-L-kynurenine + NADP+ + H2O | - |
? | |
| L-kynurenine + NADPH + O2 | the enzyme is not involved in regulation of 3-hydroxy-L-kynurenine level in vivo | Anopheles stephensi | 3-hydroxy-L-kynurenine + NADP+ + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 60000, recombinant enzyme, SDS-PAGE | Anopheles stephensi |
| More | structural analysis | Anopheles stephensi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| K3H | - |
Anopheles stephensi |
| kynurenine 3-hydroxylase | - |
Anopheles stephensi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Anopheles stephensi |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | binding domain at the N-terminus comprising residues 23-166 | Anopheles stephensi | |
| NADPH | dependent on, the Gly-X-Gly-X-X-Gly motif, residues 27-32, and the hydrophobic amino acid residues at positions 23, 25, 36, 39, 46, and 48 are indispensable for correct folding of the beta1-alpha-beta2-structure of the dinucleotide binding domain | Anopheles stephensi | |
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