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Literature summary extracted from

  • Lukacin, R.; Britsch, L.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.9 wild-type and mutant enzymes, expression in Escherichia coli Petunia x hybrida

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.9 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
1.14.11.9 H278Q mutant enzyme has no detectable enzyme activity Petunia x hybrida
1.14.11.9 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
1.14.11.9 R288K decrease in catalytic activity and a 5fold increase in Km-value for 2-oxoglutarate Petunia x hybrida
1.14.11.9 R288Q decrease in catalytic activity and a 160fold increase in Km-value for 2-oxoglutarate Petunia x hybrida

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.9 diethyldicarbonate ascorbate protects against inactivation Petunia x hybrida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.9 additional information
-
 additional information Km-values of mutant enzymes Petunia x hybrida
1.14.11.9 1.4
-
 2-oxoadipate
-
 Petunia x hybrida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.9 soluble
-
 Petunia x hybrida
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.9 Fe2+ required Petunia x hybrida
1.14.11.9 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.9 naringenin + 2-oxoglutarate + O2 Petunia x hybrida enzyme is involved in the biosynthesis of flavonoids, catechins, and anthocyanidins (2R,3R)-dihydrokaempferol + succinate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.9 Petunia x hybrida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.9
-
 Petunia x hybrida

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.11.9 additional information
-
-
 Petunia x hybrida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.9 (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
-
 ?
1.14.11.9 naringenin + 2-oxoadipate + O2
-
 Petunia x hybrida dihydrokaempferol + pentanedioate + CO2
-
 ?
1.14.11.9 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.9 additional information
-
 pH-optima of mutant enzymes Petunia x hybrida
1.14.11.9 6
-
 wild-type enzyme, and second lower optimum at pH 8.0 Petunia x hybrida