Information on EC 2.3.1.116 - flavonol-3-O-beta-glucoside O-malonyltransferase

Word Map on EC 2.3.1.116
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.116
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RECOMMENDED NAME
GeneOntology No.
flavonol-3-O-beta-glucoside O-malonyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
malonyl-CoA + flavonol 3-O-beta-D-glucoside = CoA + flavonol 3-O-(6-O-malonyl-beta-D-glucoside)
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
Flavone and flavonol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:flavonol-3-O-beta-D-glucoside 6''-O-malonyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
78413-11-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
parsley
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + genistein 7-O-glucoside
CoA + ?
show the reaction diagram
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7.6% of the activity with quercetin 3-O-glucoside
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-
?
malonyl-CoA + isorhamnetin 3-O-glucoside
CoA + isorhamnetin 3-O-glucoside malonylester
show the reaction diagram
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78% of the activity with kaempferol 3-O-glucoside
probably acylated at position 6 of glucose
?
malonyl-CoA + kaempferol 3-O-glucoside
CoA + kaempferol 3-O-glucoside malonylester
show the reaction diagram
malonyl-CoA + p-nitrophenyl beta-D-glucopyranoside
CoA + p-nitrophenyl 6-O-malonyl-beta-D-glucopyranoside
show the reaction diagram
malonyl-CoA + phenyl beta-D-glucopyranoside
CoA + phenyl 6-O-malonyl-beta-D-glucopyranoside
show the reaction diagram
malonyl-CoA + quercetin 3-O-glucoside
CoA + quercetin 3-O-(6-O-malonyl-beta-D-glucoside)
show the reaction diagram
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regiospecific transfer of malonyl group to the 6-hydroxyl group of quercetin 3-O-glucoside, highly specific for these acyl donor and acceptor
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-
?
malonyl-CoA + quercetin 3-O-glucoside
CoA + quercetin 3-O-(6-O-malonylbeta-D-glucoside)
show the reaction diagram
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regiospecific transfer of malonyl group to the 6-hydroxyl group of quercetin 3-O-glucoside, highly specific for these acyl donor and acceptor
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-
?
malonyl-CoA + quercetin 3-O-glucoside
CoA + quercetin 3-O-glucoside malonylester
show the reaction diagram
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60% of the activity with kaempferol 3-O-glucoside
probably acylated at position 6 of glucose
?
succinyl-CoA + quercetin 3-O-glucoside
CoA + quercetin 3-(6-O-succinylbeta-D-glucoside)
show the reaction diagram
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27% of the activity with malonyl-CoA
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?
succinyl-CoA + quercetin 3-O-glucoside
CoA + quercetin 3-O-(6-O-succinyl-beta-D-glucoside)
show the reaction diagram
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19% of the activity with malonyl-CoA
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?
additional information
?
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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
malonyl-CoA + kaempferol 3-O-glucoside
CoA + kaempferol 3-O-glucoside malonylester
show the reaction diagram
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
isorhamnetin 3-O-glucoside
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0.004
kaempferol 3-O-glucoside
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0.005
malonyl-CoA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 9
malonyl-CoA
2.9 - 9
quercetin 3-O-glucoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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most active in Tris buffer containing bovine serum albumin
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 50000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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acidic pH leads to rapid denaturation
486143
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, partially purified enzyme is stable for several months, extensively purified enzyme loses 50% of activity within 2-3 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli