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Information on EC 1.14.99.47 - (+)-larreatricin hydroxylase and Organism(s) Larrea tridentata and UniProt Accession Q6UIL3

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IUBMB Comments
Isolated from the plant Larrea tridentata (creosote bush). The enzyme has a strong preference for the 3' position of (+)-larreatricin.
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This record set is specific for:
Larrea tridentata
UNIPROT: Q6UIL3
The expected taxonomic range for this enzyme is: Larrea tridentata
The taxonomic range for the selected organisms is: Larrea tridentata
Synonyms
larreatricin 3'-hydroxylase, larreatricin 3-hydroxylase, More, PPO, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
larreatricin 3'-hydroxylase
297342
-
larreatricin 3-hydroxylase
297342
-
PPO
297342
-
additional information
297342
cf. EC 1.14.18.1
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.
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
-
?
3'-hydroxy-larreatricin + O2
3,3'-dihydroxylarreatricin
show the reaction diagram
-
3-hydroxylation
-
-
?
3-hydroxy-larreatricin + O2
3,3'-dihydroxylarreatricin
show the reaction diagram
-
3'-hydroxylation
-
-
?
larreatricin + O2
3'-hydroxy-larreatricin
show the reaction diagram
-
3'-hydroxylation
-
-
?
larreatricin + O2
3-hydroxy-larreatricin
show the reaction diagram
-
3-hydroxylation
-
-
?
additional information
?
-
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
3'-hydroxy-larreatricin + O2
3,3'-dihydroxylarreatricin
show the reaction diagram
-
3-hydroxylation
-
-
?
3-hydroxy-larreatricin + O2
3,3'-dihydroxylarreatricin
show the reaction diagram
-
3'-hydroxylation
-
-
?
larreatricin + O2
3'-hydroxy-larreatricin
show the reaction diagram
-
3'-hydroxylation
-
-
?
larreatricin + O2
3-hydroxy-larreatricin
show the reaction diagram
-
3-hydroxylation
-
-
?
additional information
?
-
-
the Larrea tridentate PPO gene product acts as a (+)-larreatricin 3'-hydroxylase in vivo
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
a copper-containing enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.2
-
pH 7.0, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
Larrea tridentata PPO contains N-terminal sequences predicting its localization to the chloroplast thylakoid lumen
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
LAHY_LARTR
584
0
66352
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
x * 43000, SDS-PAGE, x * 66352, calculated
66352
-
x * 43000, SDS-PAGE, x * 66352, calculated
SUBUNIT
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
gene PPO, DNA and amino acid sequence determination and analyis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cho, M.H.; Moinuddin, S.G.; Helms, G.L.; Hishiyama, S.; Eichinger, D.; Davin, L.B.; Lewis, N.G.
(+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from the creosote bush (Larrea tridentata)
Proc. Natl. Acad. Sci. USA
100
10641-10646
2003
Larrea tridentata, Larrea tridentata (Q6UIL3)
Manually annotated by BRENDA team
Sullivan, M.
Beyond brown polyphenol oxidases as enzymes of plant specialized metabolism
Front. Plant Sci.
5
1-7
2015
Larrea tridentata (Q6UIL3)
Manually annotated by BRENDA team
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