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Literature summary for 1.14.11.9 extracted from
- Identification of strictly conserved histidine and arginine residues as part of the active site in Petunia hybrida flavanone 3beta-hydroxylase (1997), Eur. J. Biochem., 249, 748-757.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| wild-type and mutant enzymes, expression in Escherichia coli | Petunia x hybrida |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H220Q | catalytic activity is reduced to about 0.15% of that of the wild-type enzyme. Slightly increased Km-value with respect to iron binding, as compared to the wild-type enzyme | Petunia x hybrida |
| H278Q | mutant enzyme has no detectable enzyme activity | Petunia x hybrida |
| N222N | catalytic activity is reduced to about 0.15% of that of the wild-type enzyme. Slightly increased Km-value with respect to iron binding, as compared to the wild-type enzyme | Petunia x hybrida |
| R288K | decrease in catalytic activity and a 5fold increase in Km-value for 2-oxoglutarate | Petunia x hybrida |
| R288Q | decrease in catalytic activity and a 160fold increase in Km-value for 2-oxoglutarate | Petunia x hybrida |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diethyldicarbonate | ascorbate protects against inactivation | Petunia x hybrida |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km-values of mutant enzymes | Petunia x hybrida | |
| 1.4 | - |
2-oxoadipate | - |
Petunia x hybrida | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Petunia x hybrida | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | required | Petunia x hybrida | |
| Iron | non-heme iron protein. His220, His278 and Asp222 constitute three of the possible ligands for iron binding in the active site of the enzyme | Petunia x hybrida | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| naringenin + 2-oxoglutarate + O2 | Petunia x hybrida | enzyme is involved in the biosynthesis of flavonoids, catechins, and anthocyanidins | (2R,3R)-dihydrokaempferol + succinate + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Petunia x hybrida | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Petunia x hybrida |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Petunia x hybrida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2S)-naringenin + 2-oxoglutarate + O2 | His220, His278 and Asp222 are part of the 2-oxoglutarate binding site | Petunia x hybrida | (2R,3R)-dihydrokaempferol + succinate + CO2 | - |
? | |
| naringenin + 2-oxoadipate + O2 | - |
Petunia x hybrida | dihydrokaempferol + pentanedioate + CO2 | - |
? | |
| naringenin + 2-oxoglutarate + O2 | enzyme is involved in the biosynthesis of flavonoids, catechins, and anthocyanidins | Petunia x hybrida | (2R,3R)-dihydrokaempferol + succinate + CO2 | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
pH-optima of mutant enzymes | Petunia x hybrida |
| 6 | - |
wild-type enzyme, and second lower optimum at pH 8.0 | Petunia x hybrida |
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