Information on EC 2.4.1.298 - anthocyanidin 3-O-glucoside 5-O-glucosyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.298
-
RECOMMENDED NAME
GeneOntology No.
anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + an anthocyanidin 3-O-beta-D-glucoside = UDP + an anthocyanidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Anthocyanin biosynthesis
-
-
gentiodelphin biosynthesis
-
-
rose anthocyanin biosynthesis II (via cyanidin 3-O-beta-D-glucoside)
-
-
shisonin biosynthesis
-
-
superpathway of anthocyanin biosynthesis (from cyanidin and cyanidin 3-O-glucoside)
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:anthocyanidin-3-O-beta-D-glucoside 5-O-glucosyltransferase
Isolated from the plants Perilla frutescens var. crispa, Verbena hybrida [1], Dahlia variabilis [2] and Gentiana triflora (clustered gentian) [3]. It will also act on anthocyanidin 3-O-(6-O-malonylglucoside) [2] and is much less active with hydroxycinnamoylglucose derivatives [3]. There is no activity in the absence of the 3-O-glucoside group.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
gene Gt5GT7
UniProt
Manually annotated by BRENDA team
gene Gt5GT7
UniProt
Manually annotated by BRENDA team
gene HGT8
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
bifunctional protein, glucosylates the 3-O- and 5-O-positions of anthocyanidins and flavonols
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
UDP-alpha-D-glucose + cyanidin 3-O-(6''-4-coumaroyl)-beta-D-glucoside
UDP + cyanidin 3-O-(6''-4-coumaroyl)-glucoside 5-O-beta-D-glucoside
show the reaction diagram
low activity
-
-
?
UDP-alpha-D-glucose + cyanidin 3-O-(6''-caffeoyl)-beta-D-glucoside
UDP + cyanidin 3-O-(6''-caffeoyl)-glucoside 5-O-beta-D-glucoside
show the reaction diagram
low activity
-
-
?
UDP-alpha-D-glucose + cyanidin 3-O-(6-O-(4-coumaroyl)-beta-D-glucoside)
UDP + cyanidin 3-O-(6-O-(4-coumaroyl)-beta-D-glucosyl)-5-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + cyanidin 3-O-(6-O-malonyl)-beta-D-glucoside
UDP + cyanidin 3-O-beta-D-glucosyl-5-O-(6-O-malonyl)-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + cyanidin 3-O-beta-D-galactoside
UDP + cyanidin 3-O-galactoside 5-O-beta-D-glucoside
show the reaction diagram
-
-
-
?
UDP-alpha-D-glucose + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + cyanidin 3-O-beta-D-rutinoside
UDP + cyanidin 3-O-beta-D-rutinoside 5-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + cyanidin 3-O-beta-D-rutinoside
UDP + cyanidin 3-O-beta-D-rutinoside 5-O-glucoside
show the reaction diagram
64% of the activity with malvidin 3-O-beta-D-glucoside
-
-
?
UDP-alpha-D-glucose + cyanidin 3-O-beta-D-rutinoside
UDP + cyanidin 3-O-rutinoside 5-O-beta-D-glucoside
show the reaction diagram
-
-
-
?
UDP-alpha-D-glucose + delphinidin 3-O-beta-D-glucoside
UDP + delphinidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + malvidin 3-O-beta-D-galactoside
UDP + malvidin 3-O-beta-D-glucoside 5-O-beta-D-galactoside
show the reaction diagram
128% of the activity with malvidin 3-O-beta-D-glucoside
-
-
?
UDP-alpha-D-glucose + malvidin 3-O-beta-D-glucoside
UDP + malvidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + pelargonidin 3-O-(6-O-malonyl)-beta-D-glucoside
UDP + pelargonidin 3-O-(6-O-malonyl)-beta-D-glucosyl-5-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + pelargonidin 3-O-beta-D-glucoside
UDP + pelargonidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + peonidin 3-O-beta-D-glucoside
UDP + peonidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + petunidin 3-O-beta-D-glucoside
UDP + petunidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + quercetin 3-O-beta-D-glucoside
UDP + quercetin 3,5-di-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
UDP-alpha-D-glucose + cyanidin 3-O-(6-O-(4-coumaroyl)-beta-D-glucoside)
UDP + cyanidin 3-O-(6-O-(4-coumaroyl)-beta-D-glucosyl)-5-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + cyanidin 3-O-(6-O-malonyl)-beta-D-glucoside
UDP + cyanidin 3-O-beta-D-glucosyl-5-O-(6-O-malonyl)-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + delphinidin 3-O-beta-D-glucoside
UDP + delphinidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
UDP-alpha-D-glucose + pelargonidin 3-O-(6-O-malonyl)-beta-D-glucoside
UDP + pelargonidin 3-O-(6-O-malonyl)-beta-D-glucosyl-5-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + pelargonidin 3-O-beta-D-glucoside
UDP + pelargonidin 3,5-di-O-beta-D-glucoside
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
slight activation
Mg2+
-
slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
complete inhibition at 1 mM
Co2+
43% inhibition at 1 mM
iodoacetic acid
-
slight inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
dithioerythritol
-
-
EDTA
25% activation at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0209 - 0.1113
cyanidin 3-O-beta-D-glucoside
0.0295 - 0.0535
delphinidin 3-O-beta-D-glucoside
0.0809 - 0.0919
malvidin 3-O-beta-D-glucoside
0.207
pelargonidin 3-O-beta-D-glucoside
-
pH 8.0, 35C
0.3739
peonidin 3-O-beta-D-glucoside
-
pH 8.0, 35C
0.1146
petunidin 3-O-beta-D-glucoside
-
pH 8.0, 35C
4.51
quercetin 3-O-beta-D-glucoside
-
pH 8.0, 35C
0.213 - 0.94
UDP-alpha-D-glucose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.279
malvidin 3-O-beta-D-glucoside
Vitis amurensis
W8QG94
pH 7.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.45
malvidin 3-O-beta-D-glucoside
Vitis amurensis
W8QG94
pH 7.0, 25C
17666
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.18
-
purified enzyme, pH 8.0, 35C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
-
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.7
-
50% of maximal activity at pH 6.5 and pH 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49109
x * 49109, sequence calculation
50973
x * 50973, sequence calculation
51347
x * 51347, sequence calculation
53000
-
gel filtration
54000
x * 54000, calculated, x * 70000, SDS-PAGE of recombinant tagged protein
55400
-
x * 55400, calculated
70000
x * 54000, calculated, x * 70000, SDS-PAGE of recombinant tagged protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
stable for at least 11 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 88fold by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, and another different step of anion exchange chromatography
-
recombinant Gt5GT7 from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of the enzyme from cultivar Regent, revealing five amino acid substitutions and a truncation at the C-terminus causing the inactivation of the enzyme
-
gene Gt5GT7, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression in Escherichia coli, functional expression in Nicotiana tabacum plants leading to accumulation of cyanidin 3-rutinoside-5-glucoside
gene HGT8, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Saccharomyces cerevisiae
gene PF3R4, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Saccharomyces cerevisiae; gene PF3R6, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Saccharomyces cerevisiae
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A259S
-
naturally occuring mutation
I461M
-
naturally occuring mutation
L110V
-
naturally occuring mutation
L372
-
naturally occuring mutation
V121L
-
for the naturally inactive enzyme from cultivar Regent, restoration of the C-terminus in the European allele alone proves to be insufficient for a reversal to a functional allele. An additional V121L transition located in close spatial vicinity of the catalytically active histidine in the active site of the nonfunctional protein is also essential to recover 5GT activity
V307L
-
naturally occuring mutation
A259S
-
naturally occuring mutation
-
L110V
-
naturally occuring mutation
-
L372
-
naturally occuring mutation
-
V121L
-
for the naturally inactive enzyme from cultivar Regent, restoration of the C-terminus in the European allele alone proves to be insufficient for a reversal to a functional allele. An additional V121L transition located in close spatial vicinity of the catalytically active histidine in the active site of the nonfunctional protein is also essential to recover 5GT activity
-
V307L
-
naturally occuring mutation
-