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Information on EC 2.4.1.128 - scopoletin glucosyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession O82381

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.128 scopoletin glucosyltransferase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: O82381 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
sgtase, scopoletin glucosyltransferase, scopoletin ugt, nbugt73a24, nbugt73a25, udp-glucose:scopoletin glucosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucosyltransferase, uridine diphosphoglucose-scopoletin
-
-
-
-
SGTase
-
-
-
-
UDP-glucose:scopoletin glucosyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:scopoletin O-beta-D-glucosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
81210-69-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + scopoletin
UDP + scopolin
show the reaction diagram
-
-
-
?
UDP-glucose + scopoletin
UDP + scopolin
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + scopoletin
UDP + scopolin
show the reaction diagram
-
-
-
?
UDP-glucose + scopoletin
UDP + scopolin
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03897 - 0.06045
scopoletin
0.2826 - 1.065
UDP-glucose
0.0152 - 0.04955
scopoletin
0.2772 - 0.2826
UDP-glucose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.11 - 10.92
scopoletin
0.06 - 1.11
scopoletin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28.48 - 210.7
scopoletin
3.92 - 13.05
UDP-glucose
1.21 - 28.48
scopoletin
0.21 - 3.92
UDP-glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.356
71C1, 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30°C
0.03
71C3, 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
glycosyltransferases of family 1 are capable of transferring sugar moieties from activated sugar donors to a wide range of small lipophilic acceptors leading to an increase in water solubility, improved chemical stability and altered biological activity of the sugar conjugates, in plants, family 1 glycosyltransferases play an important role in metabolic homeostasis, regulation of phytohormone activities and detoxification of xenobiotics such as herbicides and pesticides
physiological function
glycosyltransferases of family 1 are capable of transferring sugar moieties from activated sugar donors to a wide range of small lipophilic acceptors leading to an increase in water solubility, improved chemical stability and altered biological activity of the sugar conjugates, in plants, family l glycosyltransferases play an important role in metabolic homeostasis, regulation of phytohormone activities and detoxification of xenobiotics such as herbicides and pesticides
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
U71C1_ARATH
481
0
53875
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
by SDS-PAGE, approximate molecular weight of wild-type enzyme and mutants
80000
by SDS-PAGE, approximate molecular weight of wild-type enzyme and mutants
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D262E/N265Q
by site-directed mutagenesis
D257E/S260L
by site-directed mutagenesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant proteins are purified by affinity chromatography using GST-Sepharose 4B
recombinant proteins are purified by affinity chromatography using GST-Sepharose 4B
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant and mutant glycosyltransferase 71C1 is expressed as fusion protein tagged with a 26 kDa GST protein at the N-terminus in Escherichia coli BL21, production of a chimeric mutant derived from 2 Arabidopsis glucosyltransferases, 71C1 and 71C3, the chimera contains the N-terminal domain of 71C1 and the C-terminal domain of 71C3
recombinant and mutant glycosyltransferase 71C3 is expressed as fusion protein tagged with a 26 kDa GST protein at the N-terminus in Escherichia coli BL21, production of a chimeric mutant derived from 2 Arabidopsis glucosyltransferases, 71C1 and 71C3, the chimera contains the N-terminal domain of 71C1 and the C-terminal domain of 71C3
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weis, M.; Lim, E.K.; Bruce, N.C.; Bowles, D.J.
Engineering and kinetic characterisation of two glucosyltransferases from Arabidopsis thaliana
Biochimie
90
830-834
2008
Arabidopsis thaliana (O82381), Arabidopsis thaliana (Q9LML7)
Manually annotated by BRENDA team