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Information on EC 2.4.1.115 - anthocyanidin 3-O-glucosyltransferase and Organism(s) Vitis vinifera and UniProt Accession P51094
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2.4.1.115 anthocyanidin 3-O-glucosyltransferaseIUBMB Comments
The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.20.4, anthocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself .
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Word Map
- 2.4.1.115
- anthocyanidins
- flavonols
- dihydroflavonol
-
4-reductase
- flavanone
-
3-hydroxylase
- 3-o-glucoside
- hybrida
- delphinidin
-
5-o-glucosyltransferase
-
3-o-glucosylation
- peonidin
-
myrica
-
antirrhinum
-
ammonialyase
-
leucoanthocyanidins
- bayberry
- synthesis
The taxonomic range for the selected organisms is: Vitis vinifera
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
anthocyanidin 3-o-glucosyltransferase, udp-glucose:flavonoid 3-o-glucosyltransferase, udp-glucose flavonoid 3-o-glucosyltransferase, uf3gt, fagt1, ct3gt-a, udp-glucose anthocyanidin 3-o-glucosyltransferase, ih3gt, ugt78k1, ugt78k6, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosyltransferase, uridine diphosphoglucose-anthocyanidin 3-O-
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-
-
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UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase
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-
-
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UDP-glucose:cyanidin-3-O-glucosyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-D-glucose:anthocyanidin 3-O-beta-D-glucosyltransferase
The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.20.4, anthocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].
CAS REGISTRY NUMBER
COMMENTARY
65607-32-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + cyanidin
UDP + cyanidin 3-O-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + quercetin
UDP + quercetin 3-O-beta-D-glucoside
no glucosylation with UDP-galactose, UDP-xylose, UDP-glucuronic acid, UDP-mannose, ADP-glucose, CDP-glucose, GDP-glucose or TDP-glucose
-
-
?
UDP-glucose + delphinidin
UDP + delphinidin 3-O-beta-D-glucoside
-
-
-
?
UDP-glucose + delphinidin
UDP + delphinidin-3-O-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + pelargonidin
UDP + pelargonidin 3-O-beta-D-glucoside
-
72% of the activity with cyanidin
-
-
?
UDP-glucose + malvidin
UDP + malvidin 3-O-beta-D-glucoside
-
10% of the activity with cyanidin
-
-
?
UDP-glucose + peonidin
UDP + peonidin 3-O-beta-D-glucoside
-
52% of the activity with cyanidin
-
-
?
UDP-alpha-D-glucose + cyanidin
UDP + cyanidin 3-O-beta-D-glucoside
-
first step of a anthocyanin branch
-
-
?
UDP-glucose + delphinidin
UDP + delphinidin 3-O-beta-D-glucoside
-
first step of a anthocyanin branch
-
-
?
UDP-glucose + delphinidin
UDP + delphinidin 3-O-beta-D-glucoside
-
95% of the activity with cyanidin
-
-
?
additional information
?
-
the principal, if not only, role of UDP-glucose:flavonoid 3-O-glucosyltransferase is to glucosylate anthocyanidins in red fruit ripening
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-
?
additional information
?
-
-
the principal, if not only, role of UDP-glucose:flavonoid 3-O-glucosyltransferase is to glucosylate anthocyanidins in red fruit ripening
-
-
?
additional information
?
-
the enzyme is responsible for a late step in anthocyanin biosynthesis
-
-
?
additional information
?
-
-
the enzyme is responsible for a late step in anthocyanin biosynthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + cyanidin
UDP + cyanidin 3-O-beta-D-glucoside
-
first step of a anthocyanin branch
-
-
?
UDP-glucose + delphinidin
UDP + delphinidin 3-O-beta-D-glucoside
-
first step of a anthocyanin branch
-
-
?
additional information
?
-
the principal, if not only, role of UDP-glucose:flavonoid 3-O-glucosyltransferase is to glucosylate anthocyanidins in red fruit ripening
-
-
?
additional information
?
-
-
the principal, if not only, role of UDP-glucose:flavonoid 3-O-glucosyltransferase is to glucosylate anthocyanidins in red fruit ripening
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 9.4
-
pH 6.6: about 40% of maximal activity, pH 9.4: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UFOG_VITVI
456
0
50150
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at least three freeze-thaw cycles can be tolerated without apparent loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ford, C.M.; Boss, P.K.; Hoj, P.B.
Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homolog of the enzyme encoded by the maize bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo
J. Biol. Chem.
273
9224-9233
1998
Vitis vinifera (P51094), Vitis vinifera
Do, C.B.; Cormier, F.; Nicolas, Y.
Isolation and characterization of a UDP-glucose:cyanidin 3-O-glucosyltransferase from grape cell suspension cultures (Vitis vinifera)
Plant Sci.
112
43-51
1995
Vitis vinifera
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