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Information on EC 2.4.1.136 - gallate 1-beta-glucosyltransferase
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EC Tree
2.4.1.136 gallate 1-beta-glucosyltransferaseIUBMB Comments
A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. Vanillin is the best acceptor investigated.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ugt84a25a, ugt84a26a, udp-glucose:gallate glucosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-O-galloyl-beta-D-glucose-forming UGT
-
glucosyltransferase, uridine diphosphoglucose-vanillate 1-
-
-
-
-
UDP-glucose-vanillate 1-glucosyltransferase
-
-
-
-
UDP-glucose:gallate glucosyltransferase
UDP-glucose:vanillate 1-O-glucosyltransferase
-
-
-
-
UDP-glucose:gallate glucosyltransferase
-
-
-
-
UDP-glucose:gallate glucosyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + gallate = UDP + 1-galloyl-beta-D-glucose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:gallate beta-D-glucosyltransferase
A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. Vanillin is the best acceptor investigated.
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CAS REGISTRY NUMBER
COMMENTARY
89700-30-1
-
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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 + 4-hydroxybenzoate
UDP + 1-O-(4-hydroxybenzoyl)-beta-D-glucopyranose
-
48% of activity compared to vanillate
-
-
?
UDP-alpha-D-glucose + cinnamate
UDP + 1-O-cinnamoyl-beta-D-glucose
-
9% of activity compared to vanillate
-
-
?
UDP-glucose + caffeate
UDP + 1-caffeoyl-beta-D-glucose
-
-
-
?
UDP-glucose + ferulate
UDP + 1-feruloyl-beta-D-glucose
-
-
-
?
UDP-glucose + gallate
UDP + 1-galloyl-beta-D-glucose
-
-
-
?
UDP-glucose + p-coumarate
UDP + 1-O-p-coumaroyl-beta-D-glucose
-
32% of activity compared to vanillate
-
-
?
UDP-glucose + protocatechuate
UDP + 1-protocatechuoyl-beta-D-glucose
-
-
-
?
UDP-glucose + sinapate
UDP + 1-sinapoyl-beta-D-glucose
-
-
-
?
UDP-glucose + vanillate
UDP + 1-vanilloyl-beta-D-glucose
-
-
-
?
UDPglucose + 3,4,5-trimethoxybenzoate
UDP + 1-O-3,4,5-trimethoxybenzoyl-beta-D-glucose
-
7% of activity compared to vanillate
-
-
?
UDPglucose + anisate
UDP + 1-O-anisoyl-beta-D-glucose
-
38% of activity compared to vanillate
-
-
?
UDPglucose + benzoate
UDP + benzoyl-beta-D-glucose
-
16% of activity compared to vanillate
-
-
?
UDPglucose + ferulate
UDP + 1-O-feruloyl-beta-D-glucose
-
35% of activity compared to vanillate
-
-
?
UDPglucose + m-coumarate
UDP + 1-O-m-coumaroyl-beta-D-glucose
-
14% of activity compared to vanillate
-
-
?
UDPglucose + protocatechuate
UDP + protocatechuyl-beta-D-glucose
-
22% of activity compared to vanillate
-
-
?
UDPglucose + sinapate
UDP + 1-O-sinapoyl-beta-D-glucose
-
13% of activity compared to vanillate
-
-
?
UDPglucose + veratrate
UDP + 1-O-veratroyl-beta-D-glucose
-
71% of activity compared to vanillate
-
-
?
UDPglucose + gallate
UDP + 1-O-galloyl-beta-D-glucose
-
-
i.e. beta-glucogallin
r
UDPglucose + gallate
UDP + 1-O-galloyl-beta-D-glucose
-
52% of activity compared to vanillate
i.e. beta-glucogallin
r
UDPglucose + gallate
UDP + 1-O-galloyl-beta-D-glucose
-
physiological role probably is the formation of beta-glucogallin, the putative first intermediate in the biosynthesis of gallotannins
i.e. beta-glucogallin
r
UDPglucose + gallate
UDP + 1-O-galloyl-beta-D-glucose
-
physiological role probably is the formation of beta-glucogallin, the putative first intermediate in the biosynthesis of gallotannins
i.e. beta-glucogallin
r
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A25a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A25a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A25a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A25a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A25a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A26a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A26a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A26a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A26a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids, substrate specificity, overview. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a. UGT84A26a can be classified as 1-O-ester-forming glucosyltransferases with a preference for hydroxybenzoic acids as glucose acceptor
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a
-
-
-
additional information
?
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a
-
-
-
additional information
?
-
-
the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids. UGT84A25b and UGT84A26b are predicted to have similar substrate specificity as UGT84A25a and UGT84A26a
-
-
-
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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-glucose + gallate
UDP + 1-galloyl-beta-D-glucose
-
-
-
?
UDPglucose + gallate
UDP + 1-O-galloyl-beta-D-glucose
-
physiological role probably is the formation of beta-glucogallin, the putative first intermediate in the biosynthesis of gallotannins
i.e. beta-glucogallin
r
UDPglucose + gallate
UDP + 1-O-galloyl-beta-D-glucose
-
physiological role probably is the formation of beta-glucogallin, the putative first intermediate in the biosynthesis of gallotannins
i.e. beta-glucogallin
r
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.168
gallate
pH 6.0, 30°C, recombinant enzyme
0.19
gallate
pH 6.0, 30°C, recombinant enzyme
0.149
protocatechuate
pH 6.0, 30°C, recombinant enzyme
0.17
protocatechuate
pH 6.0, 30°C, recombinant enzyme
0.103
vanillate
pH 6.0, 30°C, recombinant enzyme
0.111
vanillate
pH 6.0, 30°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.7
gallate
pH 6.0, 30°C, recombinant enzyme
13.5
gallate
pH 6.0, 30°C, recombinant enzyme
10.1
protocatechuate
pH 6.0, 30°C, recombinant enzyme
12.7
protocatechuate
pH 6.0, 30°C, recombinant enzyme
10.4
vanillate
pH 6.0, 30°C, recombinant enzyme
12.6
vanillate
pH 6.0, 30°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56.32
gallate
pH 6.0, 30°C, recombinant enzyme
80.34
gallate
pH 6.0, 30°C, recombinant enzyme
67.79
protocatechuate
pH 6.0, 30°C, recombinant enzyme
74.71
protocatechuate
pH 6.0, 30°C, recombinant enzyme
93.69
vanillate
pH 6.0, 30°C, recombinant enzyme
122.33
vanillate
pH 6.0, 30°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phylogenetic analysis classifies four of seven isolated genes as UDP glycosyltransferase (UGT) 84A subfamily proteins (UGT84A25a, -b, UGT84A26a, -b). In vitro enzyme assays show that the UGT84A proteins catalyze esterification of UDP-glucose and gallic acid to form 1-O-galloyl-beta-D-glucose. UGT84A25a and -26a also form 1-O-glucose esters of other structurally related hydroxybenzoic and hydroxycinnamic acids with a preference for hydroxybenzoic acids
metabolism
the UGT84A subfamily enzymes of Eucalyptus camaldulensis are responsible for constitutive production of 1-O-galloyl-beta-D-glucose, which is the first step of hydrolyzable tannin biosynthesis
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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). GGT23_PUNGR
506
0
56129
Swiss-Prot
Chloroplast (Reliability: 4)
GGT24_PUNGR
517
0
57277
Swiss-Prot
Chloroplast (Reliability: 5)
GGT_QUERO
510
0
56555
Swiss-Prot
other Location (Reliability: 5)
A0A396GLK0_MEDTR
968
0
108206
TrEMBL
other Location (Reliability: 4)
A0A072VRL6_MEDTR
259
0
29141
TrEMBL
other Location (Reliability: 5)
A0A2Z5V6P8_EUCCA
511
0
56548
TrEMBL
Mitochondrion (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene UGT84A25a, seven full-length candidate cDNAs are isolated from Eucalyptus camaldulensis by homology-based cloning and expressed in Escherichia coli as recombinant N-terminal His-tagged proteins, DNA and amino acid sequence determination and analysis, phylogenetic analysis. Reverse transcription quantitative real-time PCR enzyme expression analysis
gene UGT84A25b, seven full-length candidate cDNAs are isolated from Eucalyptus camaldulensis by homology-based cloning and expressed in Escherichia coli as recombinant N-terminal His-tagged proteins, DNA and amino acid sequence determination and analysis, phylogenetic analysis. Reverse transcription quantitative real-time PCR enzyme expression analysis
gene UGT84A26a, seven full-length candidate cDNAs are isolated from Eucalyptus camaldulensis by homology-based cloning and expressed in Escherichia coli as recombinant N-terminal His-tagged proteins, DNA and amino acid sequence determination and analysis, phylogenetic analysis. Reverse transcription quantitative real-time PCR enzyme expression analysis
gene UGT84A26b, seven full-length candidate cDNAs are isolated from Eucalyptus camaldulensis by homology-based cloning and expressed in Escherichia coli as recombinant N-terminal His-tagged proteins, DNA and amino acid sequence determination and analysis, phylogenetic analysis. Reverse transcription quantitative real-time PCR enzyme expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression of UGT84A25a/b and UGT84A26a/b is not induced by either short-term or long-term Al3+ treatment of roots
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gross, G.
Partial purification and properties of UDP-glucose: vanillate 1-O-glucosyl transferase from oak leaves
Phytochemistry
22
2179-2182
1983
Quercus rubra
-
brenda
Gross, G.
Synthesis of beta-glucogallin from UDP-glucose and gallic acid by an enzyme preparation from oak leaves
FEBS Lett.
148
67-70
1982
Quercus rubra
-
brenda
Tahara, K.; Nishiguchi, M.; Frolov, A.; Mittasch, J.; Milkowski, C.
Identification of UDP glucosyltransferases from the aluminum-resistant tree Eucalyptus camaldulensis forming beta-glucogallin, the precursor of hydrolyzable tannins
Phytochemistry
152
154-161
2018
Eucalyptus camaldulensis (A0A2Z5V6P3), Eucalyptus camaldulensis (A0A2Z5V6P8), Eucalyptus camaldulensis (A0A2Z5V6P9), Eucalyptus camaldulensis (A0A2Z5VC92), Eucalyptus camaldulensis
brenda
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