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Information on EC 3.2.1.147 - thioglucosidase and Organism(s) Brevicoryne brassicae and UniProt Accession Q95X01

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IUBMB Comments
Has a wide specificity for thioglycosides.
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This record set is specific for:
Brevicoryne brassicae
UNIPROT: Q95X01
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The taxonomic range for the selected organisms is: Brevicoryne brassicae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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a thioglucoside
+
H2O
=
a sugar
+
a thiol
+
=
+
Synonyms
myrosinase, myrosin, thioglucosidase, myrosinase a, thioglucoside glucohydrolase, cptgg1, myr ii, myr1.bn1, myrii, atypical myrosinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-thioglucosidase
-
beta-thioglucosidase glucohydrolase
-
beta-thioglucosidase
-
-
-
-
beta-thioglucoside glucohydrolase
-
-
-
-
glucosidase, thio-
-
-
-
-
glucosinolase
-
-
-
-
myrosin
-
-
-
-
myrosinase
-
-
-
-
sinigrase
-
-
-
-
sinigrinase
-
-
-
-
Thioglucosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of S-glycosyl bond
-
-
-
-
hydrolysis of O-beta-glucosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
thioglucoside glucohydrolase
Has a wide specificity for thioglycosides.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-38-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
show the reaction diagram
best substrate
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
inhibits the enzyme, ascorbic acid addition resulted in production of hydroxylated degradation products
(2R,5R)-dihydroxymethyl-(3R,4R)-dihydroxypyrrolidine
-
inhibition of hydrolysis of sinigrin and progoitrin at pH 5 and at pH 7
1,4-dideoxy-1,4-imino-D-arabinitol
-
inhibition of hydrolysis of progoitrin at pH 5 in citrate buffer and at pH 7 in phosphate buffer, inhibition of hydrolysis of sinigrin at pH 7 in phosphate buffer, no hydrolysis of progoitrin and sinigrin at pH 5 in acetate buffer
1-deoxynojirimycin
-
inhibition of hydrolysis of progoitrin at pH 5 in citrate buffer and at pH 7 in phosphate buffer, inhibition of hydrolysis of sinigrin at pH 7 in phosphate buffer, no hydrolysis of progoitrin and sinigrin at pH 5 in acetate buffer
alexine
-
inhibition of hydrolysis of progoitrin at pH 5 and at pH 7, inhibition of hydrolysis of sinigrin at pH 7, no inhibition of hydrolysis of sinigrin at pH 5
ascorbate
-
0.3 mM, strong activation
castanospermine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activation by ascorbic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
glucotropaeolin
-
37°C, pH 4.5
0.41
sinigrin
-
37°C, pH 4.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.8
glucotropaeolin
-
37°C, pH 4.5
3 - 6
sinigrin
-
37°C, pH 4.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
hydrolysis of sinigrin
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
isoelectric focusing, pH-range 3-9
4.95
-
isoelectric focusing, pH-range 2.5-6.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of head and thorax
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MYRO1_BREBR
464
0
53736
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
126000
-
sucrose density gradient sedimentation
53000
-
2 * 53000, SDS-PAGE
97000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 57000-60000
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
additional information
-
does not appear to be a glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of recombinant enzyme at 1.1 A
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
some loss of activity upon freezing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for more than 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scofield, A.M.; Rossiter, J.T.; Witham, P.; Kite, G.C.; Nash, R.J.; Fellows, E.
Inhibition of thioglucosidase-catalysed glucosinolate hydrolysis by castanospermine and related alkaloids
Phytochemistry
29
107-109
1990
Brevicoryne brassicae, Sinapis sp.
-
Manually annotated by BRENDA team
Bones, A.M.; Rossiter, J.T.
The myrosinase-glucosinolate system, its organisation and biochemistry
Physiol. Plant.
97
194-208
1996
Enterobacter cloacae, Arabis alpina, Armoracia rusticana, Aspergillus niger, Aspergillus sydowii, Brassica rapa subsp. chinensis, Brassica juncea, Brassica napus, Brassica oleracea, Brassica rapa, Brevicoryne brassicae, Erysimum cheiri, Crambe hispanica subsp. abyssinica, Iberis umbellata, Lepidium sativum, Lipaphis erysimi, Paracolobactrum aerogenoides, Raphanus sativus, Sinapis alba, Tropaeolum majus, Eutrema japonicum
-
Manually annotated by BRENDA team
Pontoppidan, B.; Ekbom, B.; Eriksson, S.; Meijer, J.
Purification and characterization of myrosinase from the cabbage aphid (Brevicoryne brassicae), a brassica herbivore
Eur. J. Biochem.
268
1041-1048
2001
Brevicoryne brassicae
Manually annotated by BRENDA team
Jones, A.M.; Bridges, M.; Bones, A.M.; Cole, R.; Rossiter, J.T.
Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.)
Insect Biochem. Mol. Biol.
31
1-5
2001
Brevicoryne brassicae
Manually annotated by BRENDA team
Jones, A.M.; Winge, P.; Bones, A.M.; Cole, R.; Rossiter, J.T.
Characterization and evolution of a myrosinase from the cabbage aphid Brevicoryne brassicae
Insect Biochem. Mol. Biol.
32
275-284
2002
Brevicoryne brassicae (Q95X01), Brevicoryne brassicae
Manually annotated by BRENDA team
Husebye, H.; Arzt, S.; Burmeister, W.P.; Haertel, F.V.; Brandt, A.; Rossiter, J.T.; Bones, A.M.
Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to beta-glucosidases
Insect Biochem. Mol. Biol.
35
1311-1320
2005
Brevicoryne brassicae
Manually annotated by BRENDA team
Bhat, R.; Vyas, D.
Myrosinase insights on structural, catalytic, regulatory, and environmental interactions
Crit. Rev. Biotechnol.
39
508-523
2019
Arabidopsis thaliana (P37702), Arabidopsis thaliana (Q3ECS3), Arabidopsis thaliana (Q8GRX1), Arabidopsis thaliana (Q9C5C2), Armoracia rusticana (Q5PXK2), Aspergillus niger, Aspergillus sydowii, Brassica juncea (Q9ZP01), Brassica napus (Q42629), Brassica napus (Q9STD7), Brassica oleracea var. italica (A0A343IQS8), Brevicoryne brassicae (Q95X01), Brevicoryne brassicae, Capparis spinosa var. ovata, Carica papaya (C9WCQ0), Carica papaya (C9WCQ1), Crambe hispanica subsp. abyssinica, Enterobacter cloacae, Enterococcus casseliflavus, Enterococcus casseliflavus CP1, Escherichia coli, Escherichia coli VL8, Eutrema halophilum, Eutrema japonicum (Q4AE75), Lepidium latifolium, Lepidium sativum, Ligilactobacillus agilis, Ligilactobacillus agilis R16, Raphanus sativus (V9PVN6), Sinapis alba (P29736)
Manually annotated by BRENDA team