Information on EC 2.3.1.91 - sinapoylglucose-choline O-sinapoyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.91
-
RECOMMENDED NAME
GeneOntology No.
sinapoylglucose-choline O-sinapoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-O-sinapoyl-beta-D-glucose + choline = D-glucose + sinapoylcholine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sinapate ester biosynthesis
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-
Phenylpropanoid biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-beta-D-glucose:choline 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)transferase
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CAS REGISTRY NUMBER
COMMENTARY hide
85205-00-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
low activity
-
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Manually annotated by BRENDA team
Biscutella lyrata
-
-
-
Manually annotated by BRENDA team
overview
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-
Manually annotated by BRENDA team
Camelina sp.
overview
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-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
Cheiranthus sp.
overview
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Lepidium sp.
overview
-
-
Manually annotated by BRENDA team
Malcomia africana
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Rorippa sp.
overview
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Sisymbrium sp.
overview
-
-
Manually annotated by BRENDA team
low activity
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-di-O-sinapoyl-beta-D-glucose + choline
2-O-sinapoyl-beta-D-glucose + sinapoylcholine
show the reaction diagram
1-feruloyl-beta-D-glucose + choline
D-glucose + feruloylcholine
show the reaction diagram
1-O-caffeoyl-beta-D-glucose + choline
beta-D-glucose + caffeoylcholine
show the reaction diagram
-
-
-
-
?
1-O-feruloyl-beta-D-glucose + choline
beta-D-glucose + feruloylcholine
show the reaction diagram
-
-
-
-
?
1-O-sinapoyl-beta-D-glucose + 2-methylaminoethanol
beta-D-glucose + sinapoyl-2-methylaminoethanol
show the reaction diagram
-
-
-
-
?
1-O-sinapoyl-beta-D-glucose + choline
beta-D-glucose + sinapoylcholine
show the reaction diagram
-
-
-
-
?
1-O-sinapoyl-beta-D-glucose + choline
D-glucose + sinapoylcholine
show the reaction diagram
1-O-sinapoyl-beta-D-glucose + N,N-dimethylethanolamine
beta-D-glucose + sinapoyl-N,N-dimethylethanolamine
show the reaction diagram
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-
-
-
?
1-O-sinapoyl-beta-D-glucose + neopentyl alcohol
beta-D-glucose + neopentylsinapate
show the reaction diagram
-
-
-
-
?
1-O-sinapoyl-beta-D-glucose + Tris
?
show the reaction diagram
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-
-
-
?
1-p-coumaroyl-beta-D-glucose + choline
D-glucose + p-coumaroylcholine
show the reaction diagram
caffeoyl-beta-D-glucose + choline
D-glucose + caffeoylcholine
show the reaction diagram
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poor substrate
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-
?
p-coumaroyl-beta-D-glucose + choline
beta-D-glucose + coumaroylcholine
show the reaction diagram
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-
-
-
?
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
1-O-sinapoyl-beta-D-glucose + choline
D-glucose + sinapoylcholine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
dithiothreitol
additional information
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no inhibition by IAA, NEM, tosylphenylalanine chloromethylketone, diethylchlorocarbamate, p-nitrophenylchloroformate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.2
1,2-Di-O-sinapoyl-beta-D-glucose
0.1
1-O-caffeoyl-beta-D-glucose
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pH 7.0, 30C
0.41
1-O-feruloyl-beta-D-glucose
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pH 7.0, 30C
0.16 - 0.71
1-O-sinapoyl-beta-D-glucose
245
2-Methylaminoethanol
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pH 7.0, 30C
3.2 - 7.64
choline
19
N,N-dimethylethanolamine
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pH 7.0, 30C
25
neopentyl alcohol
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pH 7.0, 30C
1.9
p-coumaroyl-beta-D-glucose
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pH 7.0, 30C
105
Tris
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pH 7.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.258
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partially purified enzyme
0.486
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partially purified enzyme
9.6
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 7.2
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-
additional information
-
pI: 6.1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 9
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about half-maximal activity at pH 5.3 and pH 9.0
5.5 - 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
BnSCT1 promoter activity is uniformly distributed in cotyledons and the hypocotyl. In the surrounding tissues consisting of the single layer of peripheral endosperm cells (aleurone layer) and seed coat, the BnSCT1 promoter activity is restricted to the aleurone cell layer. These results confirm that BnSCT1 gene expression is driven by an inducible promoter that is specific for the tissues derived from double fertilization
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the recombinant enzyme, expressed in Escherichia coli is exclusively present in inclusion bodies
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
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gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 28000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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the 50000 Da mature protein is proteolytically processed in yeast and in planta, most likely resulting in the production of a heterodimer derived from a 30000 Da and a 17000 Da polypeptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure model of 1-O-sinapoyl-beta-glucose:choline sinapoyltransferase based on homology with serine carboxypeptidases.The model confirms the main functional elements conserved within the SCPL protein family, i.e. hydrolase fold, catalytic triad, oxyanion hole and substrate recognition site
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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15 min stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
choline chloride stabilizes
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repeated freeze-thawing, stable to
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, crude extract, 1 week, loss of 20% activity
-20C, partially purified, 2 weeks upon repeated freezing and thawing
-20C, stable at -20C glycerol for several months without loss of activity
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-70C, at least 2 months
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4C, 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis
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expression in a Saccharomyces cerevisiae expression system that lacks the carboxypeptodase Y gene and is defective in vacuolar targeting, resulting in secretion of heterologously expressed SCT
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expression in Escherichia coli, the protein is exclusively present in inclusion bodies
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expression in Saccharomyces cerevisiae
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homology-based cloning strategy, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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structure model of 1-O-sinapoyl-beta-glucose:choline sinapoyltransferase based on homology with serine carboxypeptidases. The model confirms the main functional elements conserved within the SCPL protein family, i.e. hydrolase fold, catalytic triad, oxyanion hole and substrate recognition site
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the T-DNA insertion mutant lacks SCT activity in the seed
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T-DNA insertion
mutant, lacking SCT activity in the seed
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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targeted metabolic engineering, designed to generate low-sinapate ester lines of Brassica napus, because sinaoate esters hamper to use of Brassica napus as animal feeding crop
nutrition
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in crop plants, sinapate esters are antinutritive compounds. They contribute to the bitter taste and astringency of seed products. Sinapate esters form complexes with proteins during seed oil processing, thus compromising the use of the valuable seed meal for animal feed and preventing it from being used as human food supplement. Thus, there is a fundamental interest in reducing the amount of sinapate esters in the seed. Suppressing the expression of the key enzymes in sinapine synthesis, sinapoylglucose:choline O-napoyltransferase (BnSCT) and UDP-glucose:sinapate glucosyltransferase (BnSGT1), by techniques such as dsRNAi should by a valuable step in establishing Brassica napus, an important oil crop, as a protein crop as well