Information on EC 2.3.1.92 - sinapoylglucose-malate O-sinapoyltransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.3.1.92
-
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RECOMMENDED NAME
GeneOntology No.
sinapoylglucose-malate O-sinapoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-O-sinapoyl-beta-D-glucose + (S)-malate = D-glucose + sinapoyl-(S)-malate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylpropanoid biosynthesis
-
-
sinapate ester biosynthesis
-
-
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SYSTEMATIC NAME
IUBMB Comments
1-O-sinapoyl-beta-D-glucose:(S)-malate O-sinapoyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY hide
76095-65-3
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
rape, ssp. oleifera
-
-
Manually annotated by BRENDA team
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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 + L-malate
?
show the reaction diagram
-
at 26% the rate of the reaction with 1-O-sinapoylglucose
-
-
?
1-O-(4-coumaroyl)-beta-D-glucose + L-malate
D-glucose + 4-coumaroyl-L-malate
show the reaction diagram
-
poor substrate
-
-
?
1-O-caffeoyl-beta-D-glucose + L-malate
D-glucose + caffeoyl-L-malate
show the reaction diagram
-
at 45% the rate of the reaction with 1-O-sinapoylglucose
-
-
?
1-O-feruloyl-beta-D-glucose + L-malate
D-glucose + feruloyl-L-malate
show the reaction diagram
-
at 85% the rate of the reaction with 1-O-sinapoylglucose
-
-
?
1-O-sinapoyl-beta-D-glucose
1,2-di-O-sinapoyl-beta-D-glucose + D-glucose
show the reaction diagram
-
in the absence or weak binding of L-malate at pH 8.0
-
-
?
1-O-sinapoyl-beta-D-glucose + H2O
sinapic acid + D-glucose
show the reaction diagram
-
minor hydrolytic activity under standard conditions, strongly increasing in the absence of L-malate and at pH 8.0
-
-
?
1-O-sinapoyl-beta-D-glucose + L-malate
D-glucose + sinapoyl-L-malate
show the reaction diagram
1-O-sinapoyl-beta-D-glucose + L-malate
sinapoyl-L-malate + D-glucose
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 + L-malate
D-glucose + sinapoyl-L-malate
show the reaction diagram
1-O-sinapoyl-beta-D-glucose + L-malate
sinapoyl-L-malate + D-glucose
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for divalent cations
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-3-hydroxybutyrate
-
competitive inhibition of 13%
(S)-2-hydroxybutyrate
-
competitive inhibition of 12%
D-malate
Glutarate
-
competitive inhibition of 15%
L-malate
succinate
-
competitive inhibition of 21%
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activation by dithioerythritol and 2-mercaptoethanol
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.115 - 0.46
1-O-sinapoyl-beta-D-glucose
0.89 - 54
L-malate
additional information
additional information
-
kinetic data
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
215
D-malate
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000084
-
mutant R322E
0.0001092
-
mutant N73A
0.000126
-
mutant D172E/S175A
0.000168
-
mutant D358A
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
various buffer systems
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
about half-maximal activity at pH 5.5 and 6.5
5.7 - 6.8
-
about half-maximal activity at pH 5.7 and 6.8, various buffer systems
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
traces
Manually annotated by BRENDA team
-
flowering stem
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47190
-
expressed in Escherichia coli, MALDI-TOF
51000
-
1 * 51000, SDS-PAGE
52000 - 55000
-
expressed in wild-type and in Nicotiana tabacum, SDS-PAGE
52000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 51000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
protein expressed in Escherichia coli has an 8 kDa lower molecular weight than wild-type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
14 h stable
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mg/ml bovine serum albumin stabilizes
-
L-malate stabilizes during purification
-
Stable to repeated freeze-thawing
-
thawing after freezing at -20°C leads to 50% loss of activity, bovine serum albumin stabilizes
-
Unstable to dilution
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 3 weeks
-
0°C, 3 weeks
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isozymes on isoelectric focusing of purified enzyme, 4 isoforms on isoelectric focusing of crude extract, in varying proportions depending on light conditions during growth
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21DE3
expressed in Escherichia coli BL21DE3; expressed in Nicotiana tabacum cv. Xanthi
-
expression in Escherichia coli, the protein is exclusively present in inclusion bodies
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D172E/S175A
-
mutant, relative activity 15%
D358A
-
mutant, relative activity 20%
H411A
-
mutant, no activity
N73A
-
mutant, relative activity 13%
R322E
-
mutant, relative activity 1%
S173A
-
mutant, no activity
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.92)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)