Information on EC 1.14.99.47 - (+)-larreatricin hydroxylase

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The expected taxonomic range for this enzyme is: Larrea tridentata

EC NUMBER
COMMENTARY hide
1.14.99.47
-
RECOMMENDED NAME
GeneOntology No.
(+)-larreatricin hydroxylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-larreatricin + AH2 + O2 = (+)-3'-hydroxylarreatricin + A + H2O
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(+)-larreatricin:oxygen 3'-hydroxylase
Isolated from the plant Larrea tridentata (creosote bush). The enzyme has a strong preference for the 3' position of (+)-larreatricin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-larreatricin + O2 + AH2
(+)-3-hydroxylarreatricin + A + H2O
show the reaction diagram
-
enzyme cataylzes the enantio-specific conversion of (+)-larreatricin into (+)-3-hydroxylarreatricin, with the regiochemistry of catalysis being unambiguously established. The corresponding (-)-enantiomer does not serve as a substrate
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.2
pH 7.0, 30°C
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE, x * 66352, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
enzyme is subject to posttranslational processing by removal of an 8.7-kDa N-terminal transit peptide, residues 1-79, and an 17-kDa COOH-terminal peptide, residues 432–584
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE