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Information on EC 3.2.1.147 - thioglucosidase and Organism(s) Sinapis alba and UniProt Accession P29736
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3.2.1.147 thioglucosidaseIUBMB Comments
Has a wide specificity for thioglycosides.
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Word Map
- 3.2.1.147
- glucosinolates
- isothiocyanate
- brassica
- broccoli
- brassicaceae
- sulforaphane
-
cruciferous
-
nitril
- glucoraphanin
- mustard
- sprout
- oleracea
-
herbivore
- napus
-
cook
-
chemopreventive
- sinapis
- cabbage
- radish
- juncea
-
crucifer
-
epithiospecifier
-
anticarcinogenic
- italica
- brassicales
-
3.2.3.1
- glucotropaeolin
-
generalist
-
armoraciae
- rusticana
- watercress
-
bomb
- floret
- idioblasts
-
cyclocondensation
- kale
- abyssinica
- glucobrassicin
-
4-hydroxybenzyl
- raphanus
- analysis
- pharmacology
-
tuscan
- gluconasturtiin
- erucin
-
mercapturic
-
brussels
- nutrition
- agriculture
- moringa
- lepidium
-
pungen
- crambe
-
blanch
- biotechnology
The taxonomic range for the selected organisms is: Sinapis alba
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
myrosinase, myrosin, thioglucosidase, myrosinase a, thioglucoside glucohydrolase, cptgg1, myr ii, myr1.bn1, myrii, atypical myrosinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-thioglucosidase
beta-thioglucoside glucohydrolase
glucosidase, thio-
-
-
-
-
glucosinolase
-
-
-
-
myrosin
-
-
-
-
myrosinase
sinigrase
-
-
-
-
sinigrinase
-
-
-
-
Thioglucosidase
-
-
-
-
beta-thioglucosidase
-
-
-
-
beta-thioglucoside glucohydrolase
-
-
-
-
myrosinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of S-glycosyl bond
-
-
-
-
hydrolysis of O-beta-glucosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thioglucoside glucohydrolase
Has a wide specificity for thioglycosides.
CAS REGISTRY NUMBER
COMMENTARY
9025-38-1
-
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
4-hydroxybenzylglucosinolate + H2O
D-glucose + 4-hydroxyphenylacetonitrile sulfate + ?
-
-
-
-
?
4-methylsulfinylbutylglucosinolate + H2O
?
-
-
in presence of epithionitrile from Arabidopsis thaliana, formation of epithionitrile and nitrile. In presence of nitrile specifier protein from Pieris rapa, formation of nitrile
-
?
4-methylthiobutylglucosinolate + H2O
?
-
-
in presence of epithionitrile from Arabidopsis thaliana, formation of epithionitrile and nitrile. In presence of nitrile specifier protein from Pieris rapa, formation of nitrile
-
?
allylglucosinolate + H2O
?
-
-
in presence of epithionitrile from Arabidopsis thaliana, formation of epithionitrile and nitrile. In presence of nitrile specifier protein from Pieris rapa, formation of nitrile
-
?
benzylglucosinolate + H2O
?
-
-
in presence of epithionitrile from Arabidopsis thaliana, formation of epithionitrile and nitrile. In presence of nitrile specifier protein from Pieris rapa, formation of nitrile
-
?
glucosinolate + H2O
isothiocyanate + thiocyanate + nitrile + epithionitrile + ?
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
208544, 208548, 208549, 208551, 208552, 208553, 208554, 208557, 208563, 208565, 208571, 208572, 208579, 208580, 208590, 208591, 208593
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate + ?
-
i.e. 2-propenyl glucosinolate
-
-
?
additional information
?
-
myrosinase is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates
-
-
?
additional information
?
-
-
myrosinase is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
2-hydroxybut-3-enylglucosinolate + H2O
additional information
-
-
(S)-2-hydroxy-3-butenylglucosinolate, i.e. epi-progoitrin
a mixture of products which includes 1-cyano-2-hydroxy-3-butene, (R)-5-vinyloxazolidine-2-thione, D-glucose, HSO4- and elemental sulfur is formed without epithiospecifier protein at pH 5.9. These products as well as erythro-1-cyano-2-hydroxy-3,4-epithiobutanes and threo-1-cyano-2-hydroxy-3,4-epithiobutanes are formed by combination of the enzyme and epithiospecifier protein from various sources
?
allylglucosinolate + H2O
additional information
-
-
-
conversion to 1-cyano-2,3-epithiopropane in presence of epithiospecifier protein, conversion to allyl cyanide in absence of epithiospecifier protein
?
allylglucosinolate + H2O
additional information
-
-
-
in presence of epithiospecifier protein 1-cyano-2,3-epithiopropane and allyl isothiocyanate are formed, in absence of epithiospecifier protein only allyl isothiocyanate is formed
?
additional information
?
-
-
hydrolysis of rapeseed meal yields 1-cyano-2-hydroxy-3-butene, 5-vinyloxazolidine-2-thione, 3-butenylisothiocyanate and 4-pentenylisothiocyanate
-
-
?
additional information
?
-
-
enzyme retains the anomeric configuration at the cleavage point, the catalytic residue is a nucleophilic glutamate
-
-
?
additional information
?
-
-
the enzyme does not catalyze a transglycosylation reaction either with alcohols or with other suitable glycosyl acceptors
-
-
?
additional information
?
-
-
hydrolysis of mustard oil glucosides to isothiocyanate, glucose and sulfate
-
-
?
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
additional information
?
-
myrosinase is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates
-
-
?
additional information
?
-
-
myrosinase is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
both epithiospecifier protein and nitrile-specifier protein are true enzymes rather than allosteric cofactors of myrosinase
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
-
dimeric enzyme is stabilized by a Zn2+-ion bound on a twofold axis. The Zn2+ has a tetrahedral coordination, with angles between 97° and 118°, though four residues: His56 and Asp70, and their symmetry-related equivalents
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(Z)-(1-((2-(dimethylammonio)ethyl)thio)-2-phenylethylidene)amino sulfate
a competitive inhibitor. The sulfate group and the phenyl group of the inhibitor bind to the aglycon-binding site of the enzyme, whereas the N,N-dimethyl group binds to the glucose-binding site, binding structure, overview
S-(2-hydroxyethyl)phenylacetothiohydroximate-O-sulfate
10 mM, 23% inhibition
S-(3-hydroxypropyl)phenylacetothiohydroximate-O -sulfate
1 mM, 70% inhibition. IC50: 0.44 mM
S-(4-hydroxybutyl)phenylacetothiohydroximate-O-sulfate
1 mM, 88% inhibition. IC50: 0.25 mM
S-ethyl phenylacetothiohydroximate-O -sulfate
1 mM, 67% inhibition. IC50: 0.58 mM
2-deoxy-2-fluoroglucotropaeolin
-
inhibition occurs via the accumulation of a long-life glucosyl-enzyme intermediate
additional information
no inhibition at 10 mM 2'-sulfatophenyl-1-thio-beta-D-glucopyranoside
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid, mechanism of ascorbic acid activation, overview
nitrile-specifier protein
-
protein factor that alters the outcome of the enzyme catalyzed reaction. Nitrile-specifier protein is a true enzyme rather than an allosteric cofactor of myrosinase
-
ascorbic acid
-
considerable activation in the pH range 5.7-7.5, maximal activation at 0.375 mM
ascorbic acid
-
1 mM, activation of isoenzyme SA, SB, very low activation of isoenzyme SC
epithiospecifier protein
-
ESP, is a small protein of molecular weight 30 to 40 kDa, which co-occurs with myrosinase. ESP does not have thioglucosidase activity, but interacts with myrosinase to promote the transfer of sulfur from the S-glucose moiety of terminally unsaturated glucosinolates to the alkenyl moiety, resulting in the formation of epithionitriles. The presence of ferrous ions are essential for ESP function.
-
epithiospecifier protein
-
in presence of epithiospecifier protein 1-cyano-2,3-epithiopropane and allyl isothiocyanate are formed, in absence of epithiospecifier protein only allyl isothiocyanate is formed
-
epithiospecifier protein
-
a mixture of products which includes 1-cyano-2-hydroxy-3-butene, (R)-5-vinyloxazolidine-2-thione, D-glucose, HSO4- and elemental sulfur is formed from (S)-2-hydroxy-3-butenylglucosinolate without epithiospecifier protein at pH 5.9. These products as well as erythro- and threo-1-cyano-2-hydroxy-3,4-epithiobutanes are formed by combination of the enzyme and epithiospecifier protein from various sources
-
epithiospecifier protein
-
protein factor that alters the outcome of the enzyme catalyzed reaction. Epithiospecifier protein is a true enzyme rather than an allosteric cofactor of myrosinase. No stable association between epithiospecifier protein and myrosinase occurs, but some proximity of both is required for epithionitrile formation to occur
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.28
sinigrin
-
enzyme immobilized into Ca-polygalacturonate, at pH 6.5 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44
S-(3-hydroxypropyl)phenylacetothiohydroximate-O -sulfate
Sinapis alba
1 mM, 70% inhibition. IC50: 0.44 mM
0.25
S-(4-hydroxybutyl)phenylacetothiohydroximate-O-sulfate
Sinapis alba
1 mM, 88% inhibition. IC50: 0.25 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.058
-
plant crude extract, pH and temperature not specified in the publication
0.263
-
mobile enzyme fraction, pH and temperature not specified in the publication
2.42
-
counter-current chromatography fraction, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 70
-
the activity of free and immobilized enzyme forms increases with temperature up to 50-60°C. Beyond this value range it decreases to about 75% of the maximal activity at 70°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 5.6
-
enzyme complex is formed by isoenzymes with isoelectric points between 4.8 and 5.6
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific
-
-
208544, 208553, 208554, 208565, 208579, 208580, 208590, 208591, 665024, 679740, 680575, 715202, 716272, 716638, 731948, 732613, 753624, 755016, 755017
-
myrosinase gene MYR2 is transcribed in all organs of the seedling, myrosinase gene Myr1 shows no transcription in seedling
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the specific activity of the protoplast is less than that of the intact root tissue
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
physiological function
additional information
physiological function
myrosinase and its substrates, the glucosinolates, are part of the plant's defense system
physiological function
glucosinolate-myrosinase is a substrate-enzyme defense mechanism present in Brassica crops. This binary system provides the plant with an efficient system against herbivores and pathogens. Glucosinolate and myrosinase are spatially present in different cells that upon tissue disruption come together and result in the formation of a variety of hydrolysis products with diverse physicochemical and biological properties. 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, the presence of supplementary proteins known as specifier proteins and/or on the physiochemical condition
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
myrosinase activity is required for the formation of characteristic adducts in the endogenous DNA after homogenizing Brassicales plants
physiological function
-
myrosinase is part of the plant chemical defense system (glucosinolate-myrosinase system). Upon tissue disruption, bioactivation of glucosinolates is initiated, i.e. myrosinases get access to their glucosinolate substrates, and glucosinolate hydrolysis results in the formation of toxic isothiocyanates and other biologically active products
physiological function
-
inhibition of Escherichia coli O157:H7 in ripening dry-fermented sausage by addition of ground mustard seed dependent on the plant charge, overview
physiological function
-
myrosinase catalyses the formation of isothiocyanates such as sulforaphane (from broccoli) and 4-(alpha-L-rhamnopyranosyloxy)benzyl isothiocyanate (from moringa), which are potent inducers of the cytoprotective phase-2 response in humans, by hydrolysis of their abundant glucosinolate (beta-thioglucoside N-hydroxysulfate) precursors
physiological function
-
myrosinase catalyses the formation of isothiocyanates such as sulforaphane (from broccoli) and 4-(alpha-L-rhamnopyranosyloxy)benzyl isothiocyanate (from moringa), which are potent inducers of the cytoprotective phase-2 response in humans, by hydrolysis of their abundant glucosinolate (beta-thioglucoside N-hydroxysulphate) precursors
physiological function
-
plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew
additional information
analysis of substrate recognition and mechanism of reaction
additional information
-
brown mustard (Brasiica juncea) has higher myrosinase activity than black (Brassica nigra) and yellow mustard (Sinapis alba)
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). MYRA_SINAL
501
0
57023
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000 - 200000
-
enzyme forms complexes of different molecular weight with several protein subunits
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
the enzyme contains about 19% alpha-helix and 35% beta-sheets, the rest being conformationally aperiodic
?
-
enzyme consists of complexes of several subunits with molecular weights between 10000 Da and 110000 Da, SDS-PAGE
dimer
-
the enzyme protein folds into a (beta/alpha)8 barrel structure forming a glycosylated dimer stabilized by a Zn2+ ion
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
contains 18% carbohydrate: 4% glucosamine, 12% hexose and 2% pentose
glycoprotein
-
contains 13000 Da carbohydrate per dimer, the carbohydrate is required to maintain molecular stability and solubility in the dehydrated environment of the seed
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in 20 mM HEPES, pH 6.5, 150 mM NaCl, and 0.02 mM ZnSO4, X-ray diffraction structure determination and analysis at 1.6 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
maximal activity is maintained in a large pH interval ranging from 5.5 to 8.5. At lower pH values, free and immobilized myrosinase forms show a strong activity loss, at pH 5.0 it is about 50% of the maximal activity, whereas it is almost absent at pH 4.5
716638
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 80
-
the extent of enzyme inactivation increases with pressure (600-800 MPa) and temperature (30-70°C) for all the mustard seeds. At combinations of lower pressures (200-400 MPa) and high temperatures (60-80°C), there is less inactivation. For example, application of 300 MPa and 70°C for 10 min retains 20%, 80% and 65% activity in yellow, black and brown mustard, respectively, whereas the corresponding activity retentions when applying only heat (70°C, 10 min) are 0%, 59% and 35%. Thus, application of moderate pressures (200-400 MPa) can potentially be used to retain myrosinase activity needed for subsequent glucosinolate hydrolysis
60
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extrinsic factors, during postharvest and food processing such as pH, temperature, and pressure
-
the enzyme is quite pressure stable, as its activity is retained after pressure treatment up to 600 MPa combined with temperatures up to 60°C. At low pressures there is an antagonistic effect between pressure and thermal treatment, since the activity of the enzyme is retained after treatment at 70°C up to 300 MPa
-
the extent of enzyme inactivation increases with pressure (600-800 MPa) and temperature (30-70°C) for all the mustard seeds. At combinations of lower pressures (200-400 MPa) and high temperatures (60-80°C), there is less inactivation. For example, application of 300 MPa and 70°C for 10 min retains 20%, 80% and 65% activity in yellow, black and brown mustard, respectively, whereas the corresponding activity retentions when applying only heat (70°C, 10 min) are 0%, 59% and 35%. Thus, application of moderate pressures (200-400 MPa) can potentially be used to retain myrosinase activity needed for subsequent glucosinolate hydrolysis
-
the high enzyme immobilization yield into Ca-polygalacturonate and its activity preservation under different conditions suggest that the enzyme released by plants at root level can be entrapped in root mucigel in order to preserve its activity. Enzyme activity preservation in the gel is high, being 95% of the initial activity after two months
-
there is 84.14% of myrosinase activity retained at 45°C and 22 MPa for 60 min, while only 1% of myrosinase activity remains at 22 MPa and 65°C for 5 min. As the pressure increases from 8 to 22 MPa at 55°C for 60 min, the relative residual activity is significantly reduced from 37.04 to 18.18%
-
Zn2+ stabilizes the enzyme structure, the myrosinase structure also has a substantial number of salt bridges and hydrogen bonds between charged and neutral atoms that confers additional stability to the enzyme. The activity of myrosinase is influenced by some intrinsic and
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Con-A-Sepharose column chromatography, SP-Sepharose column chromatography, and Superdex 200 gel filtration
-
native enzyme from seeds 4.54fold for mobile enzyme fraction, and 41.8fold from counter-current chromatography
-
rapid isolation of catalytically active plant myrosinase from fresh seed powder at high yield and purity, involving three main steps: (i) selective solvation, (ii) counter-current chromatography (CCC) using an aqueous two-phase system (ATPS) mixture of potassium phosphate and polyethylene glycol (PEG), and (iii) in-line desalting. This is followed by ultrafiltration and concanavalin A affinity chromatography. Method optimization and evaluation
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by mechanical wounding, and by herbivore attack, e.g. through Spodoptera frugiperda or Athalia rosae, the kind of herbivore determines the product formed from glucosinolates, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iori, R.; Leoni, O.; Palmieri, S.
Immobilization of myrosinase (thioglucoside glycohydrolase EC 3.2.3.1)
Biotechnol. Lett.
10
575-578
1988
Sinapis alba
-
Buchwaldt, L.; Larsen, L.M.; Ploeger, A.; Sorensen, H.
Fast polymer liquid chromatography isolation and characterization of plant myrosinase, beta-thioglucoside glucohydrolase, isoenzymes
J. Chromatogr.
363
71-80
1986
Brassica napus, Brassica nigra, Sinapis alba
-
Petroski, R.J.
Stereoselectivity of the interaction of thioglucoside glucohydrolase and epithiospecifier protein from various sources
Plant Sci.
44
85-88
1986
Aspergillus sydowii, Brassica rapa, Crambe hispanica subsp. abyssinica, Sinapis alba
-
Petroski, R.J.; Kwolek, W.F.
Interaction of a fungal thioglucoside glycohydrolase and cruciferous plant epithiospecifier protein to form 1-cyanoepithioalkanes: implication of an allosteric mechanism
Phytochemistry
24
213-216
1985
Aspergillus sydowii, Sinapis alba
-
Iversen, T.H.; Myhre, S.; Evjen, K.; Baggerud, C.
Morphology and myrosinase activity in root protoplast of Brassicaceae
Z. Pflanzenphysiol.
112
391-401
1983
Brassica rapa subsp. chinensis, Brassica oleracea, Lepidium sativum, Raphanus sativus, Sinapis alba
-
Petroski, R.J.; Tookey, H.L.
Interactions of thioglucoside glucohydrolase and epithiospecifier protein of cruciferous plants to form 1-cyanoepithioalkanes
Phytochemistry
21
1903-1905
1982
Armoracia rusticana, Brassica oleracea, Brassica rapa, Crambe hispanica subsp. abyssinica, Sinapis alba
-
Palmieri, S.; Leoni, O.; Iori, R.
A steady-state kinetics study of myrosinase with direct ultraviolet spectrophotometric assay
Anal. Biochem.
123
320-324
1982
Sinapis alba
Iversen, T.H.; Baggerud, C.
Myrosinase activity in differentiated and undifferentiated plants of brassicaceae
Z. Pflanzenphysiol.
97
399-407
1980
Brassica rapa subsp. chinensis, Brassica napus, Iberis amara, Lepidium sativum, Raphanus sativus, Sinapis alba
-
Srivastava, V.K.; Hill, D.C.
Glucosinolate hydrolytic products given by Sinapis alba, and Brassica napus thioglucosidases
Phytochemistry
13
1043-1046
1974
Brassica napus, Sinapis alba
-
Bjoerkman, R.; Loennerdal, B.
Studies on myrosinases. III. Enzymatic properties of myrosinases from Sinapis alba and Brassica napus seeds
Biochim. Biophys. Acta
327
121-131
1973
Brassica napus, Sinapis alba
Henderson, H.M.; McEwen, T.J.
Effect of ascorbic acid on thioglucosidases from different crucifers
Phytochemistry
11
3127-3133
1972
Brassica napus, Brassica rapa, Sinapis alba
-
Bjoerkman, R.; Janson, J.C.
Studies on myrosinases. I. Purification and characterization of a myrosinase from white mustard seed (Sinapis alba, L.)
Biochim. Biophys. Acta
276
508-518
1972
Sinapis alba
Hoeglund, A.S.; Lenman, M.; Rask, L.
Myrosinase is localized to the interior of myrosin grains and is not associated to the surrounding tonoplast membrane
Plant Sci.
85
165-170
1992
Sinapis alba
-
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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
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Burmeister, W.P.; Cottaz, S.; Driguez, H.; Iori, R.; Palmieri, S.; Henrissat, B.
The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insight into the substrate recognition and active-site machinery of an S-glycosidase
Structure
5
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1997
Sinapis alba
Botti, M.G.; Taylor, M.G.; Botting, N.P.
Studies on the mechanism of myrosinase. Investigation of the effect of glycosyl acceptors on enzymatic activity
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Sinapis alba
Cottaz, S.; Henrissat, B.; Driguez, H.
Mechanism-based inhibition and stereochemistry of glucosinolate hydrolysis by myrosinase
Biochemistry
35
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Sinapis alba
van Eylen, D.; Indrawat, I.; Hendrickx, M.; Van Loey, A.
Temperature and pressure stability of mustard seed (Sinapis alba L.) myrosinase
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Sinapis alba
Bourderioux, A.; Lefoix, M.; Gueyrard, D.; Tatibouet, A.; Cottaz, S.; Arzt, S.; Burmeister, W.P.; Rollin, P.
The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors
Org. Biomol. Chem.
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Sinapis alba (P29736)
Eriksson, S.; Ek, B.; Xue, J.; Rask, L.; Meijer, J.
Identification and characterization of soluble and insoluble myrosinase isoenzymes in different organs of Sinapis alba
Physiol. Plant.
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Sinapis alba
Burow, M.; Markert, J.; Gershenzon, J.; Wittstock, U.
Comparative biochemical characterization of nitrile-forming proteins from plants and insects that alter myrosinase-catalysed hydrolysis of glucosinolates
FEBS J.
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Sinapis alba
Bellostas, N.; Petersen, I.L.; Sorensen, J.C.; Sorensen, H.
A fast and gentle method for the isolation of myrosinase complexes from Brassicaceous seeds
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Brassica carinata, Brassica napus, Brassica oleracea, Sinapis alba
Besle, A.; Brazzolotto, X.; Tatibouet, A.; Cerniauskaite, D.; Gallienne, E.; Rollin, P.; Burmeister, W.P.
A micromolar O-sulfated thiohydroximate inhibitor bound to plant myrosinase
Acta Crystallogr. Sect. F
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2010
Sinapis alba (P29736), Sinapis alba
Textor, S.; Gershenzon, J.
Herbivore induction of the glucosinolate-myrosinase defense system: major trends, biochemical bases and ecological significance
Phytochem. Rev.
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Arabidopsis thaliana, Brassica rapa subsp. oleifera, Brassica juncea, Brassica napus, Brassica nigra, Brassica oleracea, Brassica rapa, Carica papaya, Raphanus sativus, Raphanus raphanistrum, Sinapis alba, Tropaeolum majus, Athalia rosae, Lepidium virginicum
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Yang, Y.; Liao, X.; Hu, X.; Zhang, Y.; Chen, F.; Wu, J.
The contribution of high pressure carbon dioxide in the inactivation kinetics and structural alteration of myrosinase
Int. J. Food Sci. Technol.
46
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Sinapis alba
Baasanjav-Gerber, C.; Monien, B.H.; Mewis, I.; Schreiner, M.; Barillari, J.; Iori, R.; Glatt, H.
Identification of glucosinolate congeners able to form DNA adducts and to induce mutations upon activation by myrosinase
Mol. Nutr. Food Res.
55
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Sinapis alba
Winde, I.; Wittstock, U.
Insect herbivore counteradaptations to the plant glucosinolate-myrosinase system
Phytochemistry
72
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2011
Arabidopsis thaliana, Sinapis alba, Sinapis arvensis, Tropaeolum majus, Arabis hirsuta, Arabis soyeri
Braschi, I.; Leoni, O.; Cinti, S.; Palmieri, S.; Gessa, C.
Activity of myrosinase from Sinapis alba seeds immobilized into Ca-polygalacturonate as a simplified model of soil-root interface mucigel
Plant Soil
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2011
Sinapis alba
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Cordeiro, R.P.; Wu, C.; Holley, R.A.
Contribution of endogenous plant myrosinase to the antimicrobial activity of deodorized mustard against Escherichia coli O157:H7 in fermented dry sausage
Int. J. Food Microbiol.
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2014
Sinapis alba
Wade, K.L.; Ito, Y.; Ramarathnam, A.; Holtzclaw, W.D.; Fahey, J.W.
Purification of active myrosinase from plants by aqueous two-phase counter-current chromatography
Phytochem. Anal.
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Brassica oleracea, Raphanus sativus, Sinapis alba, Moringa oleifera
Bhat, R.; Vyas, D.
Myrosinase insights on structural, catalytic, regulatory, and environmental interactions
Crit. Rev. Biotechnol.
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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)
Okunade, O.A.; Ghawi, S.K.; Methven, L.; Niranjan, K.
Thermal and pressure stability of myrosinase enzymes from black mustard (Brassica nigra L. W.D.J. Koch. var. nigra), brown mustard (Brassica juncea L. Czern. var. juncea) and yellow mustard (Sinapsis alba L. subsp. maire) seeds
Food Chem.
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Brassica nigra, Sinapis alba, Brassica juncea var. juncea
Wade, K.; Ito, Y.; Ramarathnam, A.; Holtzclaw, W.; Faheya, J.
Purification of active myrosinase from plants by aqueous two-phase counter-current chromatography
Phytochem. Anal.
26
47-53
2015
Sinapis alba, Moringa oleifera, Brassica oleracea var. italica (A0A343IQS8), Raphanus sativus (V9PVN6)
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Martinez-Ballesta, M.; Carvajal, M.
Myrosinase in Brassicaceae the most important issue for glucosinolate turnover and food quality
Phytochem. Rev.
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1045-1051
2015
Arabidopsis thaliana, Brassica rapa subsp. pekinensis, Brassica napus, Brassica rapa, Raphanus sativus, Sinapis alba, Brassica oleracea var. alboglabra, Thellungiella
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