Information on EC 1.14.11.20 - deacetoxyvindoline 4-hydroxylase

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The expected taxonomic range for this enzyme is: Catharanthus roseus

EC NUMBER
COMMENTARY hide
1.14.11.20
-
RECOMMENDED NAME
GeneOntology No.
deacetoxyvindoline 4-hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
deacetoxyvindoline + 2-oxoglutarate + O2 = deacetylvindoline + succinate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vindoline and vinblastine biosynthesis
-
-
Indole alkaloid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
deacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4beta-hydroxylating)
Requires Fe2+ and ascorbate. Also acts on 3-hydroxy-16-methoxy-2,3-dihydrotabersonine and to a lesser extent on 16-methoxy-2,3-dihydrotabersonine.
CAS REGISTRY NUMBER
COMMENTARY hide
132084-83-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the penultimate step in the biosynthesis of vindoline, which constitutes the main terpenoid indole alkaloid accumulated in leaves of Catharanthus roseus, spatial organization of the vindoline biosynthetic pathway, overview. The desacetoxyvindoline-4-hydroxylase interacts directly with the deacetylvindoline-4-O-acetyltransferase, that catalyzes the last step of the biosynthetic pathway, absence of metabolic channeling in the vindoline biosynthetic pathway. Importance of inter- and intracellular translocations of intermediates during the vindoline biosynthesis and potential regulatory role, overview
physiological function
part of vindoline biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
deacetoxyvindoline + 2-oxoglutarate + O2
deacetylvindoline + succinate + CO2
show the reaction diagram
desacetoxyvindoline + 2-oxoglutarate + O2
desacetylvindoline + succinate + CO2
show the reaction diagram
-
strictly specific for position 4, no hydroxylation of indole alkaloid substrates with a 2,3-double bond
-
?
additional information
?
-
-
the desacetoxyvindoline-4-hydroxylase interacts with the deacetylvindoline-4-O-acetyltransferase, analysis via yeast two-hybrid system
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
deacetoxyvindoline + 2-oxoglutarate + O2
deacetylvindoline + succinate + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the desacetoxyvindoline-4-hydroxylase interacts with the deacetylvindoline-4-O-acetyltransferase, analysis via yeast two-hybrid system
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO
-
7.5 mM, 50% inhibition
desacetylvindoline
-
product inhibition, noncompetitive vs. 2-oxoglutarate
succinate
-
product inhibition, competitive vs. 2-oxoglutarate, noncompetitive vs. desacetoxyvindoline
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
2-oxoglutarate
-
-
0.2
ascorbate
-
-
0.000003
desacetoxyvindoline
-
-
0.0085
Fe2+
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.115
deacetylvindoline
-
-
9
succinate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00012
continuous light, day 0, 4 and 8
0.00015
day 32 and 36, continuous light
0.0003
day 28, continuous light
0.00036
day 36, photoperiod
0.0006
day 24, continuous light; day 32, photoperiod; photoperiod, day 0
0.0009
day 8, photoperiod
0.0012
day 12 and 20, continuous light; day 24 and 28, photoperiod; day 4, photoperiod
0.0015
day 16, continuous light; day 20, photoperiod
0.0016
day 16, photoperiod
0.0018
day 12, photoperiod
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
5% of activity in leaf; low expression
Manually annotated by BRENDA team
no association between plantlet formation and other biosynthetic enzymes such as deacetoxyvindoline 4-hydroxylase and tryptophan decarboxylase, is found
Manually annotated by BRENDA team
etiolated seed, contains considerable levels of transcript but almost undetectable enzymic activity. Exposure of seedlings to light results in a rapid increase of enzyme activity without a significant further increase in d4h transcripts over those detected in dark-grown seedlings
Manually annotated by BRENDA team
8% of activity in leaf; low expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme resides in the nucleocytoplasmic compartment following passive diffusion to the nucleus allowed by the protein size. Colocalization with deacetylvindoline-4-O-acetyltransferase
Manually annotated by BRENDA team
additional information
-
vindoline biosynthesis pathway enzyme subcellular localization study, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
* 45647, calculated
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Sephadex G-100, Green 19-agarose, hydroxylapatite, 2-oxoglutarate-Sepharose, Mono-Q
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA, expression in Escherichia coli, possibly dimorphic allele of a single-copy gene; cloning of cDNA, possibly dimorphic allele of a single-copy gene
gene D4H, semi-quantitative RT-PCR expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
artemisinic acid leads to upregulation of the deacetoxyvindoline 4-hydroxylase and upstream enzymes of the vinblastine biosynthesis, i.e. tryptophan decarboxylase, geraniol 10-hydroxylase, tabersonine 16-hydroxylase
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
maximal production of vindoline coincides with maximal activity of enzyme and of deacetylvindoline acetyl-CoA acetyl transferase and tryptophan decarboxylase