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Information on EC 1.14.14.81 - flavanoid 3',5'-hydroxylase
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1.14.14.81 flavanoid 3',5'-hydroxylaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in plants. The 3',5'-dihydroxyflavanone is formed via the 3'-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4'-trihydroxyflavanone (naringenin) at either the 3' position to form eriodictyol or at both the 3' and 5' positions to form 5,7,3',4',5'-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3',4'-pentahydroxyflavanone (taxifolin) at the 5' position, forming ampelopsin.
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Word Map
- 1.14.14.81
- anthocyanins
-
3\'-hydroxylase
- delphinidin
- flavonols
- dihydroflavonols
-
4-reductase
-
berry
- petunia
- cyanidin
-
b-ring
-
delphinidin-based
- pelargonidin
- gentian
-
leucoanthocyanidins
-
3',5'-hydroxylated
- malvidin
- 3-o-glucosyltransferase
- dihydrokaempferol
-
flavan-3-ols
- cyp75b
- petunidin
-
f3\'hs
-
co-pigment
- nutrition
-
red-skinned
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
f3'5'h, flavonoid 3',5'-hydroxylase, flavonoid 3'5'-hydroxylase, flavonoid 3'5' hydroxylase, cyp75a, cyp75a31, f3',5'h, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.14.13.88
-
-
formerly
-
F3',5'H
F3'5'H
flavonoid 3',5'-hydroxylase
additional information
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
Nierembergia sp.
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the subfamilies CYP75A of the superfamily of cytochrome P450-dependent monooxygenases
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3'-hydroxyflavanone + [reduced NADPH-hemoprotein reductase] + O2 = a 3',5'-dihydroxyflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
(1b)
-
-
-
a flavanone + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = a 3',5'-dihydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
overall reaction
-
-
-
a flavanone + [reduced NADPH-hemoprotein reductase] + O2 = a 3'-hydroxyflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
flavanone,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3',5'-dihydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in plants. The 3',5'-dihydroxyflavanone is formed via the 3'-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4'-trihydroxyflavanone (naringenin) at either the 3' position to form eriodictyol or at both the 3' and 5' positions to form 5,7,3',4',5'-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3',4'-pentahydroxyflavanone (taxifolin) at the 5' position, forming ampelopsin.
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CAS REGISTRY NUMBER
COMMENTARY
94047-23-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
2,3-(trans)-(+)-catechin + [reduced NADPH-hemoprotein reductase] + O2
2,3-(trans)-(+)-gallocatechin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
5,7,3',4'-tetrahydroxyflavanone + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
5,7,4'-trihydroxyflavanone + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4'-tetrahydroxyflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
5-deoxyleucopelargonidin + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
apigenin + [reduced NADPH-hemoprotein reductase] + O2
tricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
3',5'-dihydroxy-dihydrokaempferol + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
5'-hydroxydihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
kaempferol + [reduced NADPH-hemoprotein reductase] + O2
myricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
leucocyanidin + [reduced NADPH-hemoprotein reductase] + O2
leucodelphinidin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + [reduced NADPH-hemoprotein reductase] + O2
(2S)-eriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Nierembergia sp.
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(2S)-naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
Nierembergia sp.
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
overall reaction
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
overall reaction
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Nierembergia sp.
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
preferred substrate of the wild-type enzyme
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
overall reaction
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Viola sp.
-
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Viola sp.
-
leads to synthesis of delphinidin
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
5'-hydroxydihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
5'-hydroxydihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Nierembergia sp.
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + [reduced NADPH-hemoprotein reductase] + O2
(2S)-eriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
naringenin + [reduced NADPH-hemoprotein reductase] + O2
(2S)-eriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for blue or purple flowers
-
-
?
additional information
?
-
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for blue or purple flowers
-
-
?
additional information
?
-
the enzyme is the key enzyme for delphinidin biosynthesis in the flavonoid biosynthetic pathway, biosynthesis of colour pigments, overview
-
-
?
additional information
?
-
-
the enzyme is the key enzyme for delphinidin biosynthesis in the flavonoid biosynthetic pathway, biosynthesis of colour pigments, overview
-
-
?
additional information
?
-
-
the enzyme is the key enzyme for delphinidin biosynthesis in the flavonoid biosynthetic pathway, biosynthesis of colour pigments, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
Nierembergia sp.
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
Nierembergia sp.
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
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
-
-
?
additional information
?
-
the enzyme is involved in biosynthesis of delphinidin-derived anthocyanins which are responsible for the rose to lilac flower colours of the petals, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the 3',5'-hydroxylation of dihydroflavonols, the precursors of purple anthocyanins
-
-
?
additional information
?
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for blue or purple flowers
-
-
?
additional information
?
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for the expression of blue or purple flower color. Pigment composition analysis of transgenic plants suggests that the F3'5'H transgene not only creates or inhibits the biosynthetic pathway to 3',5'-hydroxylated anthocyanins but switches the pathway to 3',5'-hydroxylated or 3'-hydroxylated anthocyanins
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
-
enzyme is involved in anthocyanin biosynthesis. When expressed as a transgene in the red-skinned cultivar Desiree changes tuber skin color from red to purple
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, 3',5'-hydroxylation, 3',4'-hydroxylation and 3',4',5'-hydroxylation occurs, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme hydroxylates a broad range of flavonoid substrates in vitro, overview
-
-
?
additional information
?
-
the enzyme is involved in the biosynthetic pathway of delphinidin-based anthocyanins, as well as of the flavonols quercetin and myricetin and procyanidin and prodelphinidin, correlation of enzyme expression pattern and flavonoid composition, flavonoid composition in organs of Vitis vinifera, flavonoid biosynthetic pathways, overview
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
transcriptional regulation of the enzyme in fruits, the enzyme is expressed after flowering, when proanthocyanidins are synthesized, accumulation of hydroxylated anthocyaniins in grape berries, flavonoid biosynthetic pathways, overview
-
-
?
additional information
?
-
-
transcriptional regulation of the enzyme in fruits, the enzyme is expressed after flowering, when proanthocyanidins are synthesized, accumulation of hydroxylated anthocyaniins in grape berries, flavonoid biosynthetic pathways, overview
-
-
?
additional information
?
-
-
flavonoid pathway during berry development, anthocyanin synthesis takes place mainly in postveraison, detailed overview, metabolite and expression profiling
-
-
?
additional information
?
-
-
the enzyme is a key enzyme in colour variation of the grape berry conforming to a peculiar pattern of genotype-specific expression of the whole set of anthocyanin genes in a direct transcript-metabolite phenotype relationship, the enzyme is involved in anthocyanin composition, colour intensity and colour hue of grapes at berry maturity, overview
-
-
?
additional information
?
-
-
the hydroxylase is responsible for the hydroxylation of the 5' position on the B ring of the flavonoid skeleton
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-(trans)-(+)-catechin + [reduced NADPH-hemoprotein reductase] + O2
2,3-(trans)-(+)-gallocatechin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
3',5'-dihydroxy-dihydrokaempferol + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
5'-hydroxydihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
leucocyanidin + [reduced NADPH-hemoprotein reductase] + O2
leucodelphinidin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
naringenin + [reduced NADPH-hemoprotein reductase] + O2
(2S)-eriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
apigenin + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
overall reaction
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
overall reaction
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
overall reaction
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
Viola sp.
-
leads to synthesis of delphinidin
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydrokaempferol + [reduced NADPH-hemoprotein reductase] + O2
dihydroquercetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
dihydroquercetin + [reduced NADPH-hemoprotein reductase] + O2
dihydromyricetin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(2S)-5,7,3',4',5'-pentahydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
naringenin + [reduced NADPH-hemoprotein reductase] + O2
(2S)-eriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
naringenin + [reduced NADPH-hemoprotein reductase] + O2
(2S)-eriodictyol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for blue or purple flowers
-
-
?
additional information
?
-
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for blue or purple flowers
-
-
?
additional information
?
-
the enzyme is the key enzyme for delphinidin biosynthesis in the flavonoid biosynthetic pathway, biosynthesis of colour pigments, overview
-
-
?
additional information
?
-
-
the enzyme is the key enzyme for delphinidin biosynthesis in the flavonoid biosynthetic pathway, biosynthesis of colour pigments, overview
-
-
?
additional information
?
-
-
the enzyme is the key enzyme for delphinidin biosynthesis in the flavonoid biosynthetic pathway, biosynthesis of colour pigments, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
Nierembergia sp.
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
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
-
-
?
additional information
?
-
the enzyme is involved in biosynthesis of delphinidin-derived anthocyanins which are responsible for the rose to lilac flower colours of the petals, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the 3',5'-hydroxylation of dihydroflavonols, the precursors of purple anthocyanins
-
-
?
additional information
?
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for blue or purple flowers
-
-
?
additional information
?
-
key enzyme in the synthesis of 3',5'-hydroxylated anthocyanins, which are generally required for the expression of blue or purple flower color. Pigment composition analysis of transgenic plants suggests that the F3'5'H transgene not only creates or inhibits the biosynthetic pathway to 3',5'-hydroxylated anthocyanins but switches the pathway to 3',5'-hydroxylated or 3'-hydroxylated anthocyanins
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
-
enzyme is involved in anthocyanin biosynthesis. When expressed as a transgene in the red-skinned cultivar Desiree changes tuber skin color from red to purple
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the hydroxylation pattern of the B-ring of flavonoids is determined by the activity of the flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, flavonoid biosynthesis pathways, overview
-
-
?
additional information
?
-
the enzyme is involved in the biosynthetic pathway of delphinidin-based anthocyanins, as well as of the flavonols quercetin and myricetin and procyanidin and prodelphinidin, correlation of enzyme expression pattern and flavonoid composition, flavonoid composition in organs of Vitis vinifera, flavonoid biosynthetic pathways, overview
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-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
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?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
the enzyme plays a role in the phenyl-propanoid pathway and the biosynthesis of cyanidin- and delphinidin-based anthocyanin pigments in the socalled red cultivars of grapevine, metabolic profiling and colour variations, overview, the enzyme is responsible for flavonoid accumulation in tissues
-
-
?
additional information
?
-
transcriptional regulation of the enzyme in fruits, the enzyme is expressed after flowering, when proanthocyanidins are synthesized, accumulation of hydroxylated anthocyaniins in grape berries, flavonoid biosynthetic pathways, overview
-
-
?
additional information
?
-
-
transcriptional regulation of the enzyme in fruits, the enzyme is expressed after flowering, when proanthocyanidins are synthesized, accumulation of hydroxylated anthocyaniins in grape berries, flavonoid biosynthetic pathways, overview
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-
?
additional information
?
-
-
flavonoid pathway during berry development, anthocyanin synthesis takes place mainly in postveraison, detailed overview, metabolite and expression profiling
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-
?
additional information
?
-
-
the enzyme is a key enzyme in colour variation of the grape berry conforming to a peculiar pattern of genotype-specific expression of the whole set of anthocyanin genes in a direct transcript-metabolite phenotype relationship, the enzyme is involved in anthocyanin composition, colour intensity and colour hue of grapes at berry maturity, overview
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b5
expression of cytchrome b5 in grape berries is correlated to enzyme expression during fruit development phases, overview
-
cytochrome P450
-
inhibition by a polyclonal antibody that inhibits higher plant NADPH-cytochrome p450 reductase is consistent with the suggestion that flavonoid 3',5'-hydroxylase is a monooxygenase consisting of cytochrome p450 and a NADPH-cytochrome P-450 reductase
-
cytochrome P450
the enzyme is a member of the cytochrome P450 family
-
cytochrome P450
the enzyme is a member of the cytochrome P450 family
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RNAi
reduces transcript levels, thus affecting flower color, acylated delphinidins (dominating in the wild-type) including gentiodelphin are decreased to 12.0% while non-acylated delphinidins are increased to 66.0 and 69.7% (15.2% in wild-type) of total anthocyanins in two transformed strains (clone 1 lilac, clone 15 pale blue)
-
additional information
-
a polyclonal antibody that inhibits higher plant NADPH-cytochrome p450 reductase inhibits the flavonoid 3',5'-hydroxylase. No effect by diethylpyrocarbonate or phenylmethylsulfonyl fluoride
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
transcriptional induction of the enzyme is temporally coordinated with the beginning of anthocyanin biosynthesis, the expression being 50fold higher in red berries versus green berries
-
additional information
transcriptional induction of the enzyme is temporally coordinated with the beginning of anthocyanin biosynthesis, the expression being 50fold higher in red berries versus green berries
-
additional information
transcriptional induction of the enzyme is temporally coordinated with the beginning of anthocyanin biosynthesis, the expression being 50fold higher in red berries versus green berries
-
additional information
transcriptional induction of the enzyme is temporally coordinated with the beginning of anthocyanin biosynthesis, the expression being 50fold higher in red berries versus green berries
-
additional information
transcriptional induction of the enzyme is temporally coordinated with the beginning of anthocyanin biosynthesis, the expression being 50fold higher in red berries versus green berries
-
additional information
-
drought stress leads to upregulation of the enzyme and of total anthocyanin biosynthesis in berries from dehydrated plants, the anthocyanin composition is enriched in more hydroxylated and more methoxylated derivatives, metabolite profiling, overview
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additional information
-
water deficits increase total anthocyanin contents and highly upregulate the enzyme expression, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Gallocatechin biosynthesis via a flavonoid 3',5'-hydroxylase is a defense response in Norway spruce against infection by the bark beetle-associated sap-staining fungus Endoconidiophora polonica.
Iron Deficiencies
Iron deficiency stimulates anthocyanin accumulation in grapevine apical leaves.
Mycoses
Gallocatechin biosynthesis via a flavonoid 3',5'-hydroxylase is a defense response in Norway spruce against infection by the bark beetle-associated sap-staining fungus Endoconidiophora polonica.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
activities of recombinant chimeric mutant enzymes, overview
additional information
F3'5'H activity in ray floret enzyme extracts of 3 developmental stages, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. pubilimba, crossings of cv. Yingshuan, from C. sinensis var. sinenesis, and cv. Beiyue Danzhu
UniProt
brenda
crossings of cv. Yingshuan and cv. Beiyue Danzhu from C. sinensis var. pubilimba
UniProt
brenda
Gentiana triflora x Gentiana scabra cultivar Albireo, ornamental gentian plant
UniProt
brenda
diploid potato clone W5281.2, female parent/purple tuber skin/genotype Ii RR Pp
-
-
brenda
fragment; cv. red cultivar Cabernet Sauvignon
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
F3'5'H activity in ray floret enzyme extracts of 3 developmental stages, overview
brenda
-
expressed in tuber skin only in presence of the anthocyanin regulatory locus I
brenda
additional information
very high expression level in red young leaves and red-purple flower buds
brenda
-
activity varies with the development of flowers, peaking immediately prior to and during anthesis, but is absent in mature flowers
brenda
weak expression at stages 1-3 of bud development
brenda
wild-type fruit accumulates proanthocyanidin (condensed tannins) during development
brenda
berry skin of young and small, at the pre-veraison stage, and ripe fruits
brenda
berry skin, transcriptional regulation of the enzyme, onset of expression after flowering, low expression at the onset of ripening, high expression after veraison concomitant with the accumulation of 3'- and 3',5'-hydroxylated anthocyanins, overview
brenda
-
quantitative expression analysis of the enzyme at different developmental stages in correlation to the anthocyanidin profile, overview
brenda
-
upregulation of expression during development in berry skin, accumulation of cyanidin-based anthocyanins and delphinidin-based anthocyanins
brenda
very high expression level in red young leaves and red-purple flower buds
brenda
apex, apical leaflet, reddish pigmented shoot tips
brenda
-
low expression in developing grape leaf, low level of delphinidin-based anthocyanins, accumulation of cyanidin-based anthocyanins (consistent in green-yellow-, purple-, and black-colored skin cultivars)
brenda
additional information
CYP75A31 real-time PCR expression analysis in the vegetative tomato plant parts
brenda
additional information
-
CYP75A31 real-time PCR expression analysis in the vegetative tomato plant parts
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
identification of 202 tea accessions with 120 single nucleotide polymorphisms (SNPs) at F3'5'H locus, genotyping
evolution
identification of 202 tea accessions with 120 single nucleotide polymorphisms (SNPs) at F3'5'H locus, genotyping
evolution
-
the F3'5'H gene in Phalaenopsis has a relatively large evolutionary distance to other plant F3'5'Hs
malfunction
functional SNP allelic variants within F3'5'H governing the ratio of di/tri-hydroxylated catechins and catechin contents
malfunction
functional SNP allelic variants within F3'5'H governing the ratio of di/tri-hydroxylated catechins and catechin contents
metabolism
essential in gentiodelphin (delphinidin 3-O-glucosyl-5-O-caffeoyl-glucosyl-3'-O-caffeoyl-glucoside) biosynthesis via flavonoid production causing the flower color of petals
metabolism
flavonoid biosynthesis, the relative expression of flavonoid 3'5' hydroxylase and similar genes compared to leucoanthocyanidin reductase correspond to seasonal expression balances
metabolism
the F3'5'H is a key enzyme of the phenylpropanoid pathway
physiological function
pigment accumulation in the base of column of Dendrobium moniliforme is due to the preferential expression of the enzyme. The lack of colors in perianths is at least due to transcriptional control of the enzyme
physiological function
-
coexpression with Norway spruce and apple genes encoding the rest of the flavonoid pathway, PaCHS, PaF3H, PaF30H, MdDFR and PaLAR3, in Nicotiana benthamiana leaves. Catechin and 2,3-(trans)-(+)-gallocatechin accumulate in the leaves 7 days after Agrobacterium infiltration. There is a significant increase in the gallocatechin content of Norway spruce bark and wood after inoculation with the bark beetle-associated sap-staining fungus Endoconidiophora polonica. 2,3 (trans)-(+)-catechin is a stronger inhibitor of fungal growth, while 2,3 (trans)-(+)-gallocatechin is a stronger inhibitor of melanin biosynthesis
physiological function
expression of CYP75A47 gene in petunia results in a color change from pale pink to purple. The petals expressing CYP75A47 gene contain an increased amount of 3',5'-hydroxylated anthocyanidin (malvidin, petunidin and delphinidin)
physiological function
expression of CYP75A48 gene in petunia results in a color change from pale pink to purple. The petals expressing CYP75A48 gene contain an increased amount of 3',5'-hydroxylated anthocyanidin (malvidin, petunidin and delphinidin)
physiological function
overexpression in petunia shows that it has no function in anthocyanin production
physiological function
-
Phalaenopsis genome contains the F3'5'H gene, which is the key gene for violet/blue colour, but the enzyme has no function in anthocyanin production
physiological function
the enzyme is involved in regulation of catechin contents in tea leaves
physiological function
the enzyme is involved in regulation of catechin contents in tea leaves
physiological function
the expression levels of both flavonoid 3'-hydroxylase and flavonoid 3', 5'-hydroxylase, EC 1.14.14.82 and EC 1.14.14.81, respectively, correlate positively with the anthocyanin accumulation pattern in leaves from Epimedium sagittatum
additional information
-
comparison of genetic variants and and Clark w1: flower petals of B09121 contain lower amounts of four major anthocyanins, i.e. malvidin 3,5-di-O-glucoside, petunidin 3,5-di-O-glucoside, delphinidin 3,5-di-O-glucoside and delphinidin 3-O-glucoside, common in purple flowers and contain small amounts of the 5'-unsubstituted versions of the above anthocyanins, peonidin 3,5-di-O-glucoside, cyanidin 3,5-di-O-glucoside and cyanidin 3-O-glucoside, suggesting that F3'5'H activity is reduced and flavonoid 3'-hydroxylase, EC 1.14.13.21, activity is increased compared to Clark w1 plants
additional information
-
comparison of genetic variants and and Clark w1: flower petals of B09121 contain lower amounts of four major anthocyanins, i.e. malvidin 3,5-di-O-glucoside, petunidin 3,5-di-O-glucoside, delphinidin 3,5-di-O-glucoside and delphinidin 3-O-glucoside, common in purple flowers and contain small amounts of the 5'-unsubstituted versions of the above anthocyanins, peonidin 3,5-di-O-glucoside, cyanidin 3,5-di-O-glucoside and cyanidin 3-O-glucoside, suggesting that F3'5'H activity is reduced and flavonoid 3'-hydroxylase, EC 1.14.13.21, activity is increased compared to Clark w1 plants
-
additional information
-
comparison of genetic variants and and Clark w1: flower petals of B09121 contain lower amounts of four major anthocyanins, i.e. malvidin 3,5-di-O-glucoside, petunidin 3,5-di-O-glucoside, delphinidin 3,5-di-O-glucoside and delphinidin 3-O-glucoside, common in purple flowers and contain small amounts of the 5'-unsubstituted versions of the above anthocyanins, peonidin 3,5-di-O-glucoside, cyanidin 3,5-di-O-glucoside and cyanidin 3-O-glucoside, suggesting that F3'5'H activity is reduced and flavonoid 3'-hydroxylase, EC 1.14.13.21, activity is increased compared to Clark w1 plants
-
Show AA Sequence and Transmembrane Helices (137 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F484Y/S487T
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
F48Y
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
S487A
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
S487Y
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
additional information
additional information
identification of 202 tea accessions with 120 single nucleotide polymorphisms (SNPs) at F3'5'H locus, genotyping, functional SNP allelic variants within F3'5'H governing the ratio of di/tri-hydroxylated catechins and catechin contents, association mapping and phenotypic variations in the association population
additional information
identification of 202 tea accessions with 120 single nucleotide polymorphisms (SNPs) at F3'5'H locus, genotyping, functional SNP allelic variants within F3'5'H governing the ratio of di/tri-hydroxylated catechins and catechin contents, association mapping and phenotypic variations in the association population
additional information
pollination-constant and non-astringent (PCNA) type mutants lose the ability to produce proanthocyanidin at an early stage in fruit development
additional information
-
pollination-constant and non-astringent (PCNA) type mutants lose the ability to produce proanthocyanidin at an early stage in fruit development
additional information
pink-flowered Gentiana scabra plants are bred from spontaneous mutations of Gentiana triflora blue-flowered gentian plants, two different transposable elements, terminal-repeat retrotransposon in miniature, inserted in flavonoid 3,5-hydroxylase gene contribute to pink flower coloration, overview
additional information
-
pink-flowered Gentiana scabra plants are bred from spontaneous mutations of Gentiana triflora blue-flowered gentian plants, two different transposable elements, terminal-repeat retrotransposon in miniature, inserted in flavonoid 3,5-hydroxylase gene contribute to pink flower coloration, overview
additional information
-
pink-flowered Gentiana scabra plants are bred from spontaneous mutations of Gentiana triflora blue-flowered gentian plants, two different transposable elements, terminal-repeat retrotransposon in miniature, inserted in flavonoid 3,5-hydroxylase gene contribute to pink flower coloration, overview
additional information
introduction of a binary vector to silence flavonoid 3',5'-hydroxylase and anthocyanin 5,3'-aromatic acyltransferase via RNAi silencing downregulating gentiodelphin biosynthesis, thus affecting flower color
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
additional information
redirection of anthocyanin synthesis in Osteospermum hybrida towards pelargonidin derivatives, which are not synthesized in wild-type plants, by expression of Gerbera hybrida dihydroflavonol 4-reductase, the mutant plants show altered flower colours due to synthesis of pelargonidin anthocyaninsssing Gerbera DFR with a construct or RNAi-mediated suppression of F3'5'H activity results in double transgenic plants accumulating predominantly pelargonidin derivatives in flowers, overview
additional information
-
recombinant expression of the flavonoid 3',5'-hydroxylase from Petunia sp. in Dendrathemum grandiflora plants leads to competition of the endogenous flavonoid 3'-hydroxylase, EC 1.14.13.21, with the recombinant enzyme for the same substrates in the flavonoid biosynthetic pathway leading to a change in flower petal colors, phenotype, overview
additional information
Viola sp.
-
establishment of a bluish color, achieved by delphinidin and derivatives, in Rosa hybrida by overexpression of the F3'5'H gene from Viola sp. and the dihydroflavonol 4-reductase gene from Iris hollandica, while the endogenous dihydroflavonol 4-reductase gene is downregulated, the ability for exclusive accumulation of delphinidin is inherited by the next generations, phenotype, overview
additional information
transgenic Petunia hybrida lines, overexpressing the enzyme from Vitis vinifera, produce high levels of the 3',4',5'-hydroxylated anthocyanin malvidin and very little 3',4'-hydroxylated anthocyanins, they also show a shift from kaempferol to quercetin when compared to the nontransgenic control, flower colours and phenotypes, white and red grape varieties exhibit different temporal expression of F3',5'H1 and cytochrome b5, overview
additional information
-
transgenic Petunia hybrida lines, overexpressing the enzyme from Vitis vinifera, produce high levels of the 3',4',5'-hydroxylated anthocyanin malvidin and very little 3',4'-hydroxylated anthocyanins, they also show a shift from kaempferol to quercetin when compared to the nontransgenic control, flower colours and phenotypes, white and red grape varieties exhibit different temporal expression of F3',5'H1 and cytochrome b5, overview
additional information
-
transcriptional control of anthocyanin biosynthetic genes in extreme phenotypes for berry pigmentation of naturally occurring grapevines, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity declines when microsomal suspensions are subjected to freezing and thawing
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
75°C, storage in presence of 20% sucrose for periods of greater than 1 month results in significant loss of enzyme activity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, genetic mapping, phylogenetic analysis, expression analysis and metabolic profiling, phenotypes
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, sequence comparison, genetic organization, and phylogenetic analysis
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant enzyme overexpression in Petunia hybrida hybrid M1 x R27, which contains a mutated endogenous F3'5'H (HF1), no obvious phenotype
-
expression in Dendrathemum grandiflora transgenic plants using the Agrobacterium tumefaciens stran ABA 4404 transfection method
-
expression in Rosa hybrida transgenic plants, the mutant plants show the accumulation of a high percentage of delphinidin in selected cultuvars, while the wild-type lacks delphinidin and derivatives and the activity of F3'5'H
Viola sp.
-
expression of wild-type enzyme and chimeric mutants in yeast strain INVSc 1 microsomes
functional expression of the enzyme as fusion enzyme with a P450 reductase leading to biosynthesis of plant-specific di- and trihydroxylated flavonols in Escherichia coli strain BL21(DE3), feeding experiments and determination of the flavonoid spectra in different recombinant bacterial lines in vivo, overview
-
gene CYP75A31, DNA and amino acid sequence determination and analysis, functional expression in Saccharomyces cerevisiae microsomes using vector pYeDP60, real-time PCR expression analysis
gene F3',5'h, DNA and amino acid sequence determination and analysis, genomic structure, expression pattern analysis
gene F3',5'H1, DNA and amino acid sequence determination and analysis, phylogenetic tree, developmental expression analysis, comparison of red and white cultivar enzyme expression levels, functional expression in Petunia hybrida altering the hosts' flower color and flavonoid composition
introduction of a flavonoid 3'5' hydroxylase sequence into Lotus root cultures. Expression of the transgene is associated with increased levels of condensed tannins, no alteration in polymer hydroxylation
-
Met210 variant, DNA and amino acid sequence determination and analysis, semi-quantitative RT-PCR expression analysis
-
one copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons, genotyping, quantitative RT-PCR expression analysis
PCR-amplification, transformation into Agrobacterium tumefaciens EHA101 by electroporation used to transform the blue-flowered Gentiana triflora x Gentiana scabra cultivar Albireo via leaf disc infection
subcloning of AK14, encoding flavonoid-3',5'-hydroxylase, into a plant expression vector and transforming it to pink tobacco (Nicotiana tabacum cv. Petit Havana SR1) and pink petunia (var. Falcon), both of which originally lack the enzyme
-
subcloning of TG1, encoding flavonoid-3',5'-hydroxylase, into a plant expression vector and transforming it to pink tobacco (Nicotiana tabacum cv. Petit Havana SR1) which originally lacks the enzyme
the gene from Campanula medium is introduced into Chrysanthemum by using binary vector pB249. Two transgenes, namely, CamF3'5'H and CtA3'5'GT, are enough to generate blue chrysanthemum: The 3',5'-diglucosylated delphinidin exhibits a blue color by intermolecular association with flavone glucosides under the weakly acidic pH conditions of general flower petals
Val210 variant, DNA and amino acid sequence determination and analysis, semi-quantitative RT-PCR expression analysis
-
when sense constructs are introduced into pink flower varieties that are deficient in the enzyme, transgenic plants show flower color changes from pink to magenta along with changes ihn anthocyanin composition. Some transgenic plants show novel pigmentation patterns, e.g. a star-shaped pattern. When sense constructs are introduced into blue flower petunia varieties, the flower color of the transgenic plants changes from deep blue to pale blue or even pale pink. Pigment composition analysis of transgenic plants suggests that the F3'5'H transgene not only creates or inhibits the biosynthetic pathway to 3',5'-hydroxylated anthocyanins but switches the pathway to 3',5'-hydroxylated or 3'-hydroxylated anthocyanins
-
when VmFH1, encoding the flavonoid 3',5'-hydroxylase is expressed in transgenic petunia hybrida under the control of the cauliflower mosaic virus 35S promoter, some transgenic plants show drastic flower color alteration from red to deep red with deep purple sectors
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
Nierembergia sp.
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, phylogenetic analysis of sequences of both enzymes indicate that F3',5'H is recruited from F3'H before the divergence of angiosperms and gymnosperms, overview
DNA and amino acid sequence determination and analysis, sequence comparison, genetic organization, and phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, sequence comparison, genetic organization, and phylogenetic analysis
one copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons, genotyping, quantitative RT-PCR expression analysis
one copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons, genotyping, quantitative RT-PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
berry skin accumulates cyanidin-based anthocyanins and delphinidin-based anthocyanins during development
-
chimeric RNAi technology silences transcription of enzyme, in clone 15 (pale blue) more than in clone 1 (lilac)
expression of gene CYP75A31 increases in response to nitrogen deprivation, in accordance with other genes in the phenylpropanoid pathway, overview
in PCNA mutant, especially the relative expression compared to the substrate-competing flavonoid 3' hydroxylase sinks stronger with seasonal development than in the wild-type
transcript abundance of the flavonoid 3',5'-hydroxylase gene increases significantly during infection with fungus Endoconidiophora polonica
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
additional information
nutrition
the strong catechin-associated SNPs identified in this study can be used for future marker-assisted selection to improve tea quality
nutrition
the strong catechin-associated SNPs identified in this study can be used for future marker-assisted selection to improve tea quality
additional information
understanding the regulation of flavonoid hydroxylases could be used to modify flavonoid composition of fruits
additional information
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understanding the regulation of flavonoid hydroxylases could be used to modify flavonoid composition of fruits
additional information
introduction of the F3'5'H gene encoding flavonoid 3',5'-hydroxylase can produce delphinidin in various flowers such as roses and carnations, turning the flower color purple or violet. Blue chrysanthemum is produced by introducing the A3'5'GT gene encoding anthocyanin 3',5'-O-glucosyltransferase, in addition to F3'5'H encoding flavonoid 3',5'-hydroxylase, into the host plant. The B-ring glucosylated delphinidin-based anthocyanin that is synthesized by the two transgenes develops blue coloration by co-pigmentation with colorless flavone glycosides naturally present in the ray floret of chrysanthemum
additional information
two transgenes, namely, CamF3'5'H and CtA3'5'GT, are enough to generate blue chrysanthemum: The 3',5'-diglucosylated delphinidin exhibits a blue color by intermolecular association with flavone glucosides under the weakly acidic pH conditions of general flower petals
additional information
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two transgenes, namely, CamF3'5'H and CtA3'5'GT, are enough to generate blue chrysanthemum: The 3',5'-diglucosylated delphinidin exhibits a blue color by intermolecular association with flavone glucosides under the weakly acidic pH conditions of general flower petals
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JOURNAL
VOL.
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YEAR
ORGANISM (UNIPROT)
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Campanula medium (O04773)
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