Information on EC 2.4.1.195 - N-hydroxythioamide S-beta-glucosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.195
-
RECOMMENDED NAME
GeneOntology No.
N-hydroxythioamide S-beta-glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + N-hydroxy-2-phenylethanethioamide = UDP + desulfoglucotropeolin
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucosinolate biosynthesis from dihomomethionine
-
-
glucosinolate biosynthesis from hexahomomethionine
-
-
glucosinolate biosynthesis from homomethionine
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-
glucosinolate biosynthesis from pentahomomethionine
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glucosinolate biosynthesis from phenylalanine
-
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glucosinolate biosynthesis from tetrahomomethionine
-
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glucosinolate biosynthesis from trihomomethionine
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glucosinolate biosynthesis from tryptophan
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Tryptophan metabolism
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Glucosinolate biosynthesis
-
-
Biosynthesis of secondary metabolites
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-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:N-hydroxy-2-phenylethanethioamide S-beta-D-glucosyltransferase
Involved with EC 2.8.2.24, desulfoglucosinolate sulfotransferase, in the biosynthesis of thioglucosides in cruciferous plants.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-14-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
Coss
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-
Manually annotated by BRENDA team
R.Br.
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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 + 2-(3-indolyl)acetothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-2-(3-indoyl)acetothiohydroximate
show the reaction diagram
-
-
-
-
?
UDP-glucose + 3-phenylpropanothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-3-phenylpropanothiohydroximate
show the reaction diagram
-
-
-
-
?
UDP-glucose + 4-methylthiobutyrothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-4-methylthiobutyrothiohydroximate
show the reaction diagram
-
relative reaction rate 77%
-
-
?
UDP-glucose + benzothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-benzothiohydroximate
show the reaction diagram
-
relative reaction rate 10%
-
-
?
UDP-glucose + isobutyrothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-isobutyrothiohydroximate
show the reaction diagram
-
relative reaction rate 41%
-
-
?
UDPglucose + butyrothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-butyrothiohydroximate
show the reaction diagram
-
relative reaction rate 70%
-
-
?
UDPglucose + phenylacetothiohydroximate
UDP + desulfoglucotropeolin
show the reaction diagram
UDPglucose + propiothiohydroximate
UDP + S-(alpha-D-glucopyranosyl)-propiothiohydroximate
show the reaction diagram
-
relative reaction rate 50%
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-
?
additional information
?
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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
UDPglucose + phenylacetothiohydroximate
UDP + desulfoglucotropeolin
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
10 mM, relative activity 130%
CaCl2
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activity is stimulated by thiol reducing agents
Mg2+
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10 mM, relative activity 140%
MgCl2
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activity is stimulated by thiol reducing agents
MnCl2
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activity is stimulated by thiol reducing agents
additional information
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purified enzyme lacks an absolute requirement for metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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causes 50% inhibition
p-chloromercuribenzoate
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-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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0.1 mM, activation
2,2'-dipyridyl
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1.0 mM, activation
2-mercaptoethanol
Cysteine hydrochloride
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1.0 mM, activation
dithiothreitol
EDTA
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0.01 mM, activation
glutathione
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1.0 mM, activation
L-cysteine
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.05
4-methylthiobutyrothiohydroximate
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pH 7.4, 30C
0.05
phenylacetothiohydroximate
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pH 6.0, 30C
0.27 - 1.54
UDPglucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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greater activity in phosphate and Tris-HCl buffers than in Tris-maleate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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isoenzymes with different pI values
4.95
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isoenzymes with different pI values
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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gel filtration
50000
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gel filtration
51000
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calculated from cDNA open reading frame
57600
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
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stable below pH 7.5
643823
7.5
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most stable in Tris buffer
644890
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 30
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stable up to 30C
30 - 40
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stable up to 30C for at least 1 h, activity is lost quickly at 40C or greater
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme stability decreases in buffers at pH optimum 6.0
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, freeze-dried protein, specific activity remains unchanged for more than 3 months
-
-20, crude extract stored frozen without loss of activity for 1 year
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0C, storage at temperatures below with or without glycerol results in substantial loss of activity
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4C, only a 5% loss of activity can be detected after 10 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-purified with EC 2.8.2.24
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partially
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA cloned and expressed in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
nutrition