Information on EC 2.4.1.116 - cyanidin 3-O-rutinoside 5-O-glucosyltransferase

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The expected taxonomic range for this enzyme is: Gunneridae

EC NUMBER
COMMENTARY
2.4.1.116
-
RECOMMENDED NAME
GeneOntology No.
cyanidin 3-O-rutinoside 5-O-glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-alpha-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
UDP-alpha-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-beta-D-glucoside
show the reaction diagram
also acts on pelargonidin-3-rutinoside, the enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin-3-glucoside
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
transfer of glycosyl group
-
-
PATHWAY
KEGG Link
MetaCyc Link
Anthocyanin biosynthesis
-
pelargonidin conjugates biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:cyanidin-3-O-alpha-L-rhamnosyl-(1->6)-beta-D-glucoside 5-O-beta-D-glucosyltransferase
Isolated from the plants Silene dioica (red campion) [1], Iris ensata (Japanese iris) [2] and Iris hollandica (Dutch iris) [3]. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase
-
-
-
-
glucosyltransferase, uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-
-
-
-
-
UDP-glucose:anthocyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase
-
-
UDP-glucose:cyanidin-3-rhamnosyl-(1-6)-glucoside-5-O-glucosyltransferase
-
-
CAS REGISTRY NUMBER
COMMENTARY
70248-66-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme has activity of both EC 2.4.1.115 and EC 2.4.1.116
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
anthocyanidin + UDP-D-glucose
anthocyanidin 5-O-glucoside + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + anthocyanidin-3-O-glucoside
UDP + anthocyanidin-3,5-O-diglucoside
show the reaction diagram
-
at pH 6.5, but not at pH 7.4, substrate specificity is pH-dependent
-
-
?
UDP-glucose + anthocyanidin-3-O-rutinoside
UDP + anthocyanidin-3-O-rutinoside 5-O-beta-D-glucoside
show the reaction diagram
-
at pH 7.4, substrate specificity is pH-dependent
-
-
?
UDP-glucose + cyanidin-3-O-glucoside
UDP + cyanidin-3,5-diglucoside
show the reaction diagram
-
-
-
-
-
UDP-glucose + cyanidin-3-O-glucoside
UDP + cyanidin-3,5-diglucoside
show the reaction diagram
-
at a much lower rate than cyanidin-3-O-rutinoside, at pH 6.5, but not at pH 7.4, enzyme can use different substrates for 5-O-glycosylation depending on the pH
-
-
?
UDP-glucose + cyanidin-3-O-rutinoside
UDP + cyanidin 3-O-rutinoside-5-O-beta-D-glucoside
show the reaction diagram
-
biosynthetic pathway of cyanidin-3-rhamnosylglucoside-5-glucoside, enzyme activity is controlled by a single dominant gene M
-
-
?
UDP-glucose + cyanidin-3-O-rutinoside
UDP + cyanidin-3-O-rutinoside-5-O-beta-D-glucoside
show the reaction diagram
-
catalyzes the transfer of the glucosyl moiety of UDP-glucose to the 5-hydroxyl group of cyanidin-3-rhamnosyl-(1?6)-glucoside
-
-
?
UDP-glucose + pelargonidin-3-rutinoside
UDP + pelargonidin-3-rutinoside-5-O-beta-D-glucoside
show the reaction diagram
-
also uses pelargonidin-3-rhamnosylglucoside, glucosylates the 5-hydroxyl group
-
-
?
UDPglucose + cyanidin 3-O-D-glucoside
UDP + ?
show the reaction diagram
-
-
depending upon pH, the enzyme catalyzes the formation of either anthocyanidin 3-rhamnosylglucoside or 3,5-diglucoside. Maximal formation of anthocyanidin 3-rhamnosylglucoside-5-gluside at pH 7.4, maximal formation of anthocyanidin 3,5-diglucoside at pH 6.5. Formation of cyanidin 3-rhamnosylglucoside-5-glucoside proceeds 5-10fold faster than the cyanidin 3,5-diglucoside formation
?
UDPglucose + cyanidin 3-O-D-rhamnosylglucoside
UDP + ?
show the reaction diagram
-
-
depending upon pH, the enzyme catalyzes the formation of either anthocyanidin 3-rhamnosylglucoside or 3,5-diglucoside. Maximal formation of anthocyanidin 3-rhamnosylglucoside-5-gluside at pH 7.4, maximal formation of anthocyanidin 3,5-diglucoside at pH 6.5
?
UDPglucose + cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside
UDP + cyanidin-3-O-[D-rhamnosyl-1,6-D-glucoside]-5-O-D-glucoside
show the reaction diagram
-
no activity with ADPglucose
-
?
UDPglucose + cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside
UDP + cyanidin-3-O-[D-rhamnosyl-1,6-D-glucoside]-5-O-D-glucoside
show the reaction diagram
-
involved in anthocyan biosynthesis. Activity is controlled by a single dominant gene
-
-
-
UDPglucose + pelargonidin-3-O-rhamnosylglucoside
UDP + ?
show the reaction diagram
-
-
-
?
anthocyanidin 5-O-glucoside + UDP-D-glucose
anthocyanidin-3,5-O-diglucoside + UDP
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
not: ADP-glucose, enzyme can use different substrates for 5-O-glycosylation depending on the pH
-
-
-
additional information
?
-
-
no substrate: anthocyanidin 3-O-glucoside
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + cyanidin-3-O-rutinoside
UDP + cyanidin 3-O-rutinoside-5-O-beta-D-glucoside
show the reaction diagram
-
biosynthetic pathway of cyanidin-3-rhamnosylglucoside-5-glucoside, enzyme activity is controlled by a single dominant gene M
-
-
?
UDPglucose + cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside
UDP + cyanidin-3-O-[D-rhamnosyl-1,6-D-glucoside]-5-O-D-glucoside
show the reaction diagram
-
involved in anthocyan biosynthesis. Activity is controlled by a single dominant gene
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CaCl2
-
1 mM, 180% stimulation, highest stimulation
CaCl2
-
1 mM, 1.6fold stimulation of glucosyl transfer to anthocyanidin-3-O-rutinoside at pH 7.4, but not of glucosyl transfer to anthocyanidin-3-O-glucoside at pH 6.5
Co2+
-
1 mM, stimulation
Mg2+
-
1 mM, stimulation
Mn2+
-
1 mM, stimulation
additional information
-
enzyme is stimulated by divalent metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
1 mM, 57% inhibition
EDTA
-
1 mM, pH 7.5, inhibits formation of cyanidin 3-rhamnosylglucoside-5-glucoside but has no effect on the formation of cyanidin 3,5-diglucoside at pH 6.5
HgCl2
-
0.1 mM, 95% inhibition, irreversible inhibition
N-ethylmaleimide
-
3 mM, 25% inhibition
NEM
-
3 mM, 25% inhibition, 2-mercpatoethanol or cysteine does not protect
p-chloromercuribenzoate
-
3 mM, 25% inhibition
PCMB
-
3 mM, 25% inhibition, 2-mercpatoethanol or cysteine does not protect
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
1 mM, highest stimulation of divalent cations
Ca2+
-
1 mM CaCl2 stimulates 5-O-glucosylation of cyanidin 3-rhamnosyl-glucoside 1.6fold, pH 7.4
Co2+
-
1 mM activates
Mg2+
-
1 mM activates
Polyvinylpyrrolidone
-
soluble, required for maximal activity in crude extracts
Mn2+
-
1 mM activates
additional information
-
influence of detergents and reducing agents on enzyme activity in crude extracts
-
additional information
-
glucosylation of cyanidin 3-glucoside at pH 6.5 is not stimulated by divalent metal ions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
3.4
anthocyanidin-3-O-glucoside
-
pH 6.5
3.6
-
anthocyanidin-3-O-rutinoside
-
pH 7.4
23.4
-
cyanidin-3-glucoside
-
-
3.6
-
cyanidin-3-O-rutinoside
-
pH 7.4, 30C
3.6
-
cyanidin-3-rhamnosylglucoside
-
-
0.5
-
UDP-glucose
-
pH 7.4, 30C
0.6
-
UDP-glucose
-
pH 6.5 and pH 7.4
0.5
-
UDPglucose
-
reaction with cyanidin 3-rhamnosylglucoside at pH 7.4
0.5
-
UDPglucose
-
-
0.59
-
UDPglucose
-
reaction with + cyanidin 3-rhamnosylglucoside at pH 6.5
0.67
-
UDPglucose
-
reaction with cyanidin-3-glucoside at pH 6.5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00953
-
-
; pH 7.4, 30C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
glucosyl transfer to cyanidin-3-O-glucoside, substrate specificity is pH-dependent
6.5
-
-
activity with cyanidin-3-glucoside; glucosyl transfer to anthocyanidin-3-O-glucoside, substrate specificity is pH-dependent
7.4
-
-
; glucosyl transfer to cyanidin-3-O-rutinoside and pelargonidin-3-rutinoside, substrate specificity is pH-dependent
7.4
-
-
activity with cyanidin-3-rhamnosylglucoside; glucosyl transfer to anthocyanidin 3-O-rutinoside, substrate specificity is pH-dependent
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.3
-
pH 6.0: about 80% of maximal activity, pH 7.3: about 50% of half-maximal activity, reaction with cyanidin 3-glucoside
6.9
8.8
-
about 50% of maximal activity at pH 6.9 and at pH 8.8; half-maximum velocities at pH 6.9 and 8.8, cyanidin-3-O-rutinoside as substrate
7
8.5
-
about half-maximal activity at pH 7 and 8.5, reaction with cyanidin-3-rhamnosylglucoside
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
; not in green parts of the plant
Manually annotated by BRENDA team
additional information
-
not in green parts of the plant
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55000
-
-
gel filtration
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
30 min, stable below
8
-
-
30 min, about 10% loss of activity
8.5
-
-
30 min, about 40% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repeated freeze-thawing inactivates
-
repeated freezing and thawing leads to a rapid decline in activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, about 60-80% loss of activity within 3 months
-
-20C, concentrated enzyme preparation, 3 months, 60-80% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
79.4fold; partial
-