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
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
44700
-
1 * 44700, SDS-PAGE
45647
* 45647, calculated
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 is able to upregulate the transcriptions of deacetoxyvindoline 4-hydroxylase
-
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
-
upregulated in plants inoculated with endophytes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis