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Information on EC 1.14.14.81 - flavanoid 3',5'-hydroxylase and Organism(s) Solanum melongena and UniProt Accession P37120

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IUBMB 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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Solanum melongena
UNIPROT: P37120
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The taxonomic range for the selected organisms is: Solanum melongena
The enzyme appears in selected viruses and cellular organisms
Synonyms
f3'5'h, flavonoid 3',5'-hydroxylase, flavonoid 3'5'-hydroxylase, flavonoid 3'5' hydroxylase, cyp75a, cyp75a31, f3',5'h, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme belongs to the vast and versatile cytochrome P450 protein family of enzymes
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.
CAS REGISTRY NUMBER
COMMENTARY hide
94047-23-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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-
-
?
apigenin + [reduced NADPH-hemoprotein reductase] + O2
5,7,3',4',5'-pentahydroxyflavone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
dihydrokaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
dihydromyricetin + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
-
-
-
?
kaempferol + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
5,7,3',4',5'-pentahydroxyflavone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C75A2_SOLME
513
1
57784
Swiss-Prot
Secretory Pathway (Reliability: 5)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seitz, C.; Eder, C.; Deiml, B.; Kellner, S.; Martens, S.; Forkmann, G.
Cloning, functional identification and sequence analysis of flavonoid 3'-hydroxylase and flavonoid 3',5'-hydroxylase cDNAs reveals independent evolution of flavonoid 3,5-hydroxylase in the Asteraceae family
Plant Mol. Biol.
61
365-381
2006
Callistephus chinensis (Q9FPN4), Delphinium grandiflorum (Q52YL8), Glandularia x hybrida (Q6J210), Glycine max (Q6YLS3), Gossypium hirsutum (Q84NG3), Lycianthes rantonnei (Q9FPN3), Nierembergia sp. (Q8LP20), Osteospermum hybrid cultivar (Q304Q4), Pericallis cruenta (Q304Q5), Petunia x hybrida (P48418), Solanum melongena (P37120), Solanum tuberosum (Q5EWY2), Torenia hybrid cultivar (Q9FS35), Vinca major (Q76LL4)
Manually annotated by BRENDA team