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Information on EC 1.14.11.61 - feruloyl-CoA 6-hydroxylase and Organism(s) Ipomoea batatas and UniProt Accession G9M9M1

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IUBMB Comments
Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA. cf. EC 1.14.11.62, trans-4-coumaroyl-CoA 2-hydroxylase.
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This record set is specific for:
Ipomoea batatas
UNIPROT: G9M9M1
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Word Map
The taxonomic range for the selected organisms is: Ipomoea batatas
The enzyme appears in selected viruses and cellular organisms
Synonyms
f6'h1, cyp98a22, feruloyl-coa 6'-hydroxylase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
feruloyl-CoA,2-oxoglutarate:oxygen oxidoreductase (6-hydroxylating)
Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA. cf. EC 1.14.11.62, trans-4-coumaroyl-CoA 2-hydroxylase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
caffeoyl-CoA + 2-oxoglutarate + O2
6'-hydroxycaffeoyl-CoA + succinate + CO2
show the reaction diagram
-
-
-
?
trans-feruloyl-CoA + 2-oxoglutarate + O2
trans-6-hydroxyferuloyl-CoA + succinate + CO2
show the reaction diagram
-
-
-
?
caffeoyl-CoA + 2-oxoglutarate + O2
6'-hydroxycaffeoyl-CoA + succinate + CO2
show the reaction diagram
-
-
-
?
trans-feruloyl-CoA + 2-oxoglutarate + O2
trans-6-hydroxyferuloyl-CoA + succinate + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
absolutely required
Fe2+
absolutely required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0092
trans-feruloyl-CoA
pH 6.5, 30°C
0.0102
trans-feruloyl-CoA
pH 6.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.68
trans-feruloyl-CoA
pH 6.5, 30°C
2.84
trans-feruloyl-CoA
pH 6.5, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform F6H1-2
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F6H12_IPOBA
358
0
39934
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
?
x * 43000, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsumoto, S.; Mizutani, M.; Sakata, K.; Shimizu, B.
Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam
Phytochemistry
74
49-57
2012
Ipomoea batatas (G9M9M1), Ipomoea batatas (G9M9M2)
Manually annotated by BRENDA team