Information on EC 3.1.1.80 - acetylajmaline esterase

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The expected taxonomic range for this enzyme is: Rauvolfia

EC NUMBER
COMMENTARY hide
3.1.1.80
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RECOMMENDED NAME
GeneOntology No.
acetylajmaline esterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
17-O-acetylajmaline + H2O = ajmaline + acetate
show the reaction diagram
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17-O-acetylnorajmaline + H2O = norajmaline + acetate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ajmaline and sarpagine biosynthesis
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Indole alkaloid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
17-O-acetylajmaline O-acetylhydrolase
This plant enzyme is responsible for the last stages in the biosynthesis of the indole alkaloid ajmaline. The enzyme is highly specific for the substrates 17-O-acetylajmaline and 17-O-acetylnorajmaline as the structurally related acetylated alkaloids vinorine, vomilenine, 1,2-dihydrovomilenine and 1,2-dihydroraucaffricine cannot act as substrates [2]. This is a novel member of the GDSL family of serine esterases/lipases.
CAS REGISTRY NUMBER
COMMENTARY hide
110183-46-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
17-O-acetylajmaline + H2O
ajmaline + acetate
show the reaction diagram
17-O-acetylnorajmaline + H2O
norajmaline + acetate
show the reaction diagram
17-O-acetyltetraphyllicine + H2O
?
show the reaction diagram
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86% of the activity with 17-O-acetylnorajmaline
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dithiodipyridine
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0.5 mM, 30-40% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
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0.5 mM, 30-40% inhibition
iodoacetamide
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0.5 mM, 30-40% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
17-O-acetylajmaline
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0.7
17-O-acetylnorajmaline
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8.5
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pH 6.3: about 50% of maximal activity, pH 8.5: about 50% of maximal activity
6.5 - 9.8
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pH 6.5 and pH 9.8: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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isoelectric focusing
7.65
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calculated from sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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gel filtration
40000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 40000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, at the stage of a 150fold enrichment in 0.1 M phosphate buffer, pH 7.0, 1 mM dithiothreitol, half-life: 21 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the expression in Escherichia coli failed although a wide range of conditions were tested. With a virus-based plant expression system, it was possible to express the enzyme functionally in leaves of Nicotiana benthamiana Domin. An extraordinarily high enzyme activity is detected in the Nicotiana tissue, which exceeds that in Rauvolfia cell suspension cultures about 20fold
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