Information on EC 3.2.1.B31 - beta-rutinosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.2.1.B31
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
beta-rutinosidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
rutin + H2O = quercetin + rutinose
show the reaction diagram
-
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
?
isoquercitrin + H2O
quercetin + beta-D-glucose
show the reaction diagram
isorhamnetin 3-O-rutinoside + H2O
isorhamnetin + rutin
show the reaction diagram
kaempferol 3-O-rutinoside + H2O
kaempferol + rutinose
show the reaction diagram
quercitrin + H2O
quercetin + L-rhamnose
show the reaction diagram
-
-
-
?
rutin + H2O
quercetin + rutinose
show the reaction diagram
additional information
?
-
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
isoquercitrin + H2O
quercetin + beta-D-glucose
show the reaction diagram
Q51723
best substrate
-
-
?
quercitrin + H2O
quercetin + L-rhamnose
show the reaction diagram
Q51723
-
-
-
?
rutin + H2O
quercetin + rutinose
show the reaction diagram
Q51723
-
-
-
?
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
-
completely inactivated by ethanol–H2O of above 1:2 (v/v)
methanol
-
methanol-H2O at 1:2 (v/v) leads to a loss of activity of about only 20%. The enzyme is completely inactivated by methanol-H2O at above 1:1 (v/v)
quercitrin
-
weak
troxerutin
-
weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-methyl-1-butanol
-
Isopropyl alcohol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 1.15
isoquercitrin
0.375
isorhamnetin 3-O-rutinoside
-
30°C, pH not specified in the publication
0.95
kaempferol 3-O-rutinoside
-
30°C, pH not specified in the publication
0.07
quercitrin
pH 5.0, 09°C, recombinant enzyme
0.115 - 0.561
rutin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
53.3
isoquercitrin
Pyrococcus furiosus
Q51723
pH 5.0, 09°C, recombinant enzyme
0.22
quercitrin
Pyrococcus furiosus
Q51723
pH 5.0, 09°C, recombinant enzyme
0.026 - 0.027
rutin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
303.3
isoquercitrin
Pyrococcus furiosus
Q51723
pH 5.0, 09°C, recombinant enzyme
4984
2.33
quercitrin
Pyrococcus furiosus
Q51723
pH 5.0, 09°C, recombinant enzyme
1936
0.075 - 0.078
rutin
1095
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
substrate rutin, pH 5.0, 09°C, recombinant enzyme; substrate: rutin, pH 5.0, 95°C
0.23
substrate quercitrin, pH 5.0, 09°C, recombinant enzyme
135.7
-
pH 5.0, 37°C
220
substrate isoquercitrin, pH 5.0, 09°C, recombinant enzyme
596
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5 - 3
-
pH 1.5: about 50% of maximal activity (KCl-HCl buffer), pH 3.0: about 80% of maximal activity (glycine-HCl buffer)
3.9 - 7
-
pH 3.9: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 70
-
4°C: about 90% of maximal activity, 70°C: about 25% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing
5.7
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57400
-
x * 57400, isoenzyme f3gII, SDS-PAGE
58200
-
x * 58200, isoenzyme f3gI, SDS-PAGE
65000
-
x * 65000, SDS-PAGE
74500
-
1 * 74500, SDS-PAGE under reducing conditions
80000
-
gel filtration
89000
-
isoenzyme f3gI and isoenzyme f4gII, gel filtration
245000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 11
-
stable
721860
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 50
-
stable
40
-
stable below
75
half-life: 1017 h
80
half-life: 461 h
85
half-life: 286 h
90
half-life: 173 h
95
half-life: 101 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant extracellular enzyme from culture supernatant by heat treatment and centrifugation
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; DNA aand amino acid sequence determination and analysis, expression in Escherichia coli strain ER2566, the enzyme is secreted