Information on EC 2.3.1.107 - deacetylvindoline O-acetyltransferase

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The expected taxonomic range for this enzyme is: Catharanthus roseus

EC NUMBER
COMMENTARY
2.3.1.107
-
RECOMMENDED NAME
GeneOntology No.
deacetylvindoline O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetyl-CoA + deacetylvindoline = CoA + vindoline
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Indole alkaloid biosynthesis
-
vindoline and vinblastine biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:deacetylvindoline 4-O-acetyltransferase
Catalyses the final step in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17-O-deacetylvindoline O-acetyltransferase
-
-
-
-
17-O-deacetylvindoline-17-O-acetyltransferase
-
-
-
-
acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase
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-
-
-
acetyl-CoA: 4-O-deacetylvindoline 4-O-acetyltransferase
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-
acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase
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-
-
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acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase
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-
-
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acetylcoenzyme A:deacetylvindoline O-acetyltransferase
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-
-
-
acetyltransferase, deacetylvindoline
-
-
-
-
DAT
-
-
-
-
deacetyl vindoline 4-O-acetyl transferase
Q9ZTK5
-
deacetylvindoline acetyl CoA acetyltransferase
-
-
deacetylvindoline acetyl-CoA acetyl transferase
-
-
deacetylvindoline acetyltransferase
-
-
-
-
deacetylvindoline-4-O-acetyltransferase
-
-
-
-
deacetylvindoline-4-O-acetyltransferase
-
-
deacetylvindoline-4-O-acetyltransferase
Q9ZTK5
-
CAS REGISTRY NUMBER
COMMENTARY
100630-41-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cultivars Nirmal, Prabal, and Dhawal, the mutants gsr-3 and gsr-6, and 1 horticultural variety Pacifica blush
SwissProt
Manually annotated by BRENDA team
cv. Dhawal
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
acetyl-CoA: 4-O-deacetylvindoline 4-O-acetyltransferase catalyzes a late step of terpenoid indole alkaloid biosynthesis, and vindoline biosynthesis, pathway overview
metabolism
-
vindoline constitutes the main terpenoid indole alkaloid accumulated in leaves of Catharanthus roseus, spatial tabersonine-to-vindoline biosynthesis organization involving four enzymes for the six-step conversion, overview. Deacetylvindoline-4-O-acetyltransferase catalyzes teh last step of the pathway
physiological function
-
catalyses last step in vindoline biosynthesis
physiological function
-
key enzyme for the terminal step of vindoline biosynthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
-
-
-
-
?
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
-
-
-
-
r
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of vindoline
-
-
?
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
Q9ZTK5
the enzyme catalyzes the final step in the biosynthesis of vindoline
-
-
?
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of vindoline
-
r
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
-
-
-
-
?
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
Q9ZTK5
-
-
-
?
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
-
last step in alkaloid vindoline biosynthesis, pathway overview
-
-
?
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
Q9ZTK5
last step in alkaloid vindoline biosynthesis, vindoline is reacted to vinblastine and vincristine, pathway overview
-
-
?
propionyl-CoA + 17-O-deacetylvindoline
CoA + 17-O-deacetyl-17-O-propionylvindoline
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of vindoline
-
-
?
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
Q9ZTK5
the enzyme catalyzes the final step in the biosynthesis of vindoline
-
-
?
acetyl-CoA + 17-O-deacetylvindoline
CoA + vindoline
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of vindoline
-
r
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
-
-
-
-
?
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
-
last step in alkaloid vindoline biosynthesis, pathway overview
-
-
?
acetyl-CoA + deacetylvindoline
CoA + vindoline
show the reaction diagram
Q9ZTK5
last step in alkaloid vindoline biosynthesis, vindoline is reacted to vinblastine and vincristine, pathway overview
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
10 mM, activity is enhanced by 18%
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CoA
-
0.037 mM, 50% inhibition
CoA
-
competitive
minovincinine-19-O-acetyltransferase
-
incubation of DAT with varying amounts of crude recombinant minovincinine-19-O-acetyltransferase (MAT) inhibits DAT activity in a dose dependent manner
-
phytoregulator
-
-
-
secologanin
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0.5 mM, 25% inhibition
tabersonine
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0.045 mM, 50% inhibition
tryptamine
-
0.5 mM, 28% inhibition
vindoline
-
0.5 mM, 40% inhibition
vindoline
-
no product inhibition up to 2 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
essential to maintain enzyme activity
jasmonate
-
enhances the vindoline accumulation in in vitro shoot cultures
additional information
-
16 h photoperiod treatment of shoot cultures followed by synchronized formation of new plantlets, peaks of activity at day 12, 20 and 28 after photoperiod treatment
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.005
-
acetyl-CoA
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in HEPES in in Tris-HCl buffer
0.0054
-
acetyl-CoA
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-
0.0065
-
acetyl-CoA
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-
0.0095
-
acetyl-CoA
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-
0.025
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acetyl-CoA
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in potassium phosphate buffer
0.0013
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deacetylvindoline
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0.03
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deacetylvindoline
-
-
0.0007
-
vindoline
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00012
-
-
continuous light, day 0, 4 and 8; photoperiod, day 4
0.0003
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-
continuous light, day 28, 32 and 36; photoperiod, day 8
0.0006
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-
continuous light, day 24; photoperiod, day 0
0.0009
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photoperiod, day 16 and 24
0.0015
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-
photoperiod, day 12
0.0018
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photoperiod, day 32
0.002
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continuous light, day 16; photoperiod, day 20 and 28
0.0024
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continuous light, day 12 and 20; photoperiod, day 36
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
11
-
activity increases from pH 5.5 to 7 and decreases rapidly between pH 9 and 11
6.5
9.5
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about 50% of maximal activity, pH 9.5: about 55% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
of light-treated etiolated seedlings
Manually annotated by BRENDA team
-
iodioblasts and laticifer of the bud
Manually annotated by BRENDA team
-
the enzyme is only expressed in specialized iodioblasts and laticifer cells within light exposed tissues like leaves and stems
Manually annotated by BRENDA team
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iodioblasts and laticifer of stem
Manually annotated by BRENDA team
-
the enzyme is only expressed in specialized iodioblasts and laticifer cells within light exposed tissues like leaves and stems
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
activity is highest in the youngest leaves from the uppermost apical region. The second, third and fourth leaves from the top retain 70, 50, and 25%, respectively, of the former
Manually annotated by BRENDA team
-
the enzyme is only expressed in specialized idioblasts and laticifer cells within light exposed tissues like leaves and stems
Manually annotated by BRENDA team
-
idioblasts and laticifer of the leaf
Manually annotated by BRENDA team
-
only after induction by elicitors
Manually annotated by BRENDA team
-
the enzyme is only expressed in specialized iodioblasts and laticifer cells within light exposed tissues like leaves and stems
Manually annotated by BRENDA team
additional information
-
not detectable in cell suspension culture
Manually annotated by BRENDA team
additional information
Q9ZTK5
Dat gene expression profile analysis in cultivars Nirmal, Prabal, and Dhawal, the mutants gsr-3 and gsr-6, and 1 horticultural variety Pacifica blush, overview, not in root
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
GFP-tagged DAT is localized to the cytoplasm and the nucleus
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 20000 + x * 26000, SDS-PAGE
?
-
x * 54000, SDS-PAGE
additional information
-
the enzyme is no hetero- or homodimer
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4°C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme is expressed as recombinant His-tagged protein in Escherichia coli
-
expressed in Escherichia coli and Catharanthus roseus
-
expression in Escherichia coli
-
gene Dat, DNA sequence determination and analysis
Q9ZTK5
transformation to Agrobacterium tumefaciens
-
transient expression of N-terminally or C-terminally GFP-tagged DAT in Catharanthus roseus cells. Irrespective to the fusion orientation, DAT is localized to the cytoplasm and the nucleus, as highlighted by the perfect overlapping of the fluorescence signal of the fusion protein with the nucleocytoplasmic CFP marker
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
increased expression after treamtment of cell suspension with methyl-ester jasmonic acid
-
Pythium aphanidermatum homogenate and methyl jasmonate upregulate DAT production in cell suspension cultures, elicitation to callus and shoot induce enzyme expression, overview
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
DAT is overexpressed in Catharanthus roseus hairy root cultures: metabolite analysis using HPLC show that transgenic hairy root extracts have an altered alkaloid profile with respect to horhammericine accumulation. It is concluded that expression of DAT in hairy roots alters their monoterpenoid indole alkaloids profile. Evidence is provided that horhammericine accumulates via a DAT interaction with the root specific minovincinine-19-O-acetyltransferase (MAT) that inhibits the MAT mediated conversion of horhammericine into 19-O-acetyl-horhammericine
additional information
-
analysis of interaction of vindoline biosynthetic enzymes including DAT using yeast two-hybrid assays, overview. DAT does not interact with the other enzymes
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
production of therapeutically valuable terpenoid indole alkaloids