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Literature summary for 1.14.14.81 extracted from

  • Seitz, C.; Ameres, S.; Forkmann, G.
    Identification of the molecular basis for the functional difference between flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase (2007), FEBS Lett., 581, 3429-3434.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type enzyme and chimeric mutants in yeast strain INVSc 1 microsomes Osteospermum hybrid cultivar

Protein Variants

Protein Variants Comment Organism
F484Y/S487T site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Osteospermum hybrid cultivar
F48Y site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Osteospermum hybrid cultivar
additional information generation of chimeric constructs consisting of cDNA fragments of Osteospermum hybrida F3'5'H and Gerbera hybrida F3'H, EC 1.14.13.21, overview Osteospermum hybrid cultivar
S487A site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Osteospermum hybrid cultivar
S487Y site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Osteospermum hybrid cultivar

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a cytochrome P450 enzyme Osteospermum hybrid cultivar

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
apigenin + [reduced NADPH-hemoprotein reductase] + O2 Osteospermum hybrid cultivar
-
?
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 Osteospermum hybrid cultivar
-
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
?
additional information Osteospermum hybrid cultivar substrate specificity of F3'H and the F3'5'H, flavonoid 3',5'-hydroxylase, EC 1.14.13.88, evolutionary derived from F3'H, is determined near the N-terminal end and the functional difference between these two enzymes near the C-terminal end, relatively few amino acids exchanges are required for the evolutionary extension of 3'- to 3',5'-hydroxylation activity, overview ?
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 Osteospermum hybrid cultivar
-
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Osteospermum hybrid cultivar Q304Q4
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activities of recombinant chimeric mutant enzymes, overview Osteospermum hybrid cultivar
0.0000026
-
recombinant wild-type F3'5'H Osteospermum hybrid cultivar

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
apigenin + [reduced NADPH-hemoprotein reductase] + O2
-
Osteospermum hybrid cultivar ?
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
Osteospermum hybrid cultivar dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 preferred substrate of the wild-type enzyme Osteospermum hybrid cultivar dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
?
additional information substrate specificity of F3'H and the F3'5'H, flavonoid 3',5'-hydroxylase, EC 1.14.13.88, evolutionary derived from F3'H, is determined near the N-terminal end and the functional difference between these two enzymes near the C-terminal end, relatively few amino acids exchanges are required for the evolutionary extension of 3'- to 3',5'-hydroxylation activity, overview Osteospermum hybrid cultivar ?
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
-
Osteospermum hybrid cultivar (2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
F3'5'H
-
Osteospermum hybrid cultivar
flavonoid 3',5'-hydroxylase
-
Osteospermum hybrid cultivar
More the enzyme belongs to the subfamilies CYP75A of the superfamily of cytochrome P450-dependent monooxygenases Osteospermum hybrid cultivar

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Osteospermum hybrid cultivar

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Osteospermum hybrid cultivar

Cofactor

Cofactor Comment Organism Structure
cytochrome P450 a cytochrome P450 enzyme Osteospermum hybrid cultivar