3.2.1.147: thioglucosidase
This is an abbreviated version!
For detailed information about thioglucosidase, go to the full flat file.
Word Map on EC 3.2.1.147
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3.2.1.147
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glucosinolates
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isothiocyanate
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brassica
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broccoli
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brassicaceae
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sulforaphane
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cruciferous
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nitril
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glucoraphanin
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mustard
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sprout
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oleracea
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herbivore
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napus
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cook
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chemopreventive
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sinapis
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cabbage
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radish
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juncea
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crucifer
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epithiospecifier
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anticarcinogenic
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italica
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brassicales
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3.2.3.1
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glucotropaeolin
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generalist
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armoraciae
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rusticana
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watercress
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bomb
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floret
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idioblasts
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cyclocondensation
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kale
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abyssinica
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glucobrassicin
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4-hydroxybenzyl
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raphanus
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analysis
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pharmacology
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tuscan
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gluconasturtiin
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erucin
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mercapturic
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brussels
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nutrition
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agriculture
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moringa
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lepidium
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pungen
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crambe
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blanch
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biotechnology
- 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
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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
Reaction
Synonyms
ArMy2, AtBGLU37, AtBGLU38, atypical myrosinase, beta-glucosidase 26, peroxisomal, beta-glucosidase 37, beta-glucosidase 38, beta-thioglucosidase, beta-thioglucosidase glucohydrolase, beta-thioglucoside glucohydrolase, beta-thioglucoside glucohydrolase,, BGLU26, CpTGG1, CpTGG2, EC 3.2.3.1, glucosidase, thio-, glucosinolase, More, MYR, MYR II, MYR1 myrosinase, Myr1.Bn1, Myr2.Bn1, MYRc, MYRI, MYRII, myrosin, myrosinase, myrosinase 1, myrosinase 2, myrosinase A, myrosinase B, PEN2, PYK10 myrosinase, sinigrase, sinigrinase, sinigrinase 1, sinigrinase 2, TGG, TGG1, TGG2, TGG4, TGG5, Thioglucosidase, thioglucosidase 1, thioglucosidase 2, thioglucoside glucohydrolase, thioglucoside glucohydrolase 1, thioglycosidase, WjMYR
ECTree
3.2.1.147 thioglucosidaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.2.1.147 - thioglucosidase
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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
1,4-dideoxy-1,4-imino-D-arabinitol
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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
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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
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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
cysteamine
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strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0, little influence on glucose production from sinigrin
DTT
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strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0, little influence on glucose production from sinigrin
fluridon
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glucosinolate content and isothiocyanate formation are reduced by 46.51% and 38.01%, respectively, in fluridon (Flu)-treated sprouts
glucoraphanin
substrate inhibition, kinetics, overview
KNO3
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activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
NaNO3
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activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
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
thiobenzoate
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strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0
Thiomalate
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strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0
Thiophenol
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strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0, little influence on glucose production from sinigrin
(2R,5R)-dihydroxymethyl-(3R,4R)-dihydroxypyrrolidine
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inhibition of hydrolysis of sinigrin and progoitrin at pH 5 and at pH 7
2-deoxy-2-fluoroglucotropaeolin
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inhibition occurs via the accumulation of a long-life glucosyl-enzyme intermediate
arbutin
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0.1 M, 7% inhibition in absence of ascorbate, 26% inhibition in presence of ascorbate
ascorbic acid
inhibitory at over 0.7 mM; inhibitory at over 0.7 mM
ascorbic acid
inhibits the enzyme, ascorbic acid addition resulted in production of hydroxylated degradation products
castanospermine
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the alkaloidal glycosidase inhibitor acts as competitive inhibitor
Fe2+
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at pH 4.5 and 5.5 the formation of isothiocyanate is strongly inhibited, depressed effect at pH 6.5, no effect at pH 7.5. No inhibition of glucose liberation
Fe2+
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slightly suppresses reaction but causes a significant effect by directing degradation of 2-hydroxybut-3-enylglucosinolate to 1-cyano-2-hydroxy-3-ene rather than to 5-vinyloxazolidine-2-thione
glucose
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1.0 M, 22% inhibition in presence of ascorbate, competitive. No inhibition in absence of ascorbate
L-Cys
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5 mM, and 2.5 mM Fe2+, pH 5.0 or 6.5, strong inhibition of formation of allyl isothiocyanate
maltose
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1.0 M, 33% inhibition in absence of ascorbate, 6% inhibition in presence of ascorbate
methyl jasmonate
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decrease in enzyme activity, concommitant increase in levels of 4-methylsulfinylbutylglucosinolate and 8-methylsulfinylbutylglucosinolate in hypocotyl
methyl jasmonate
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spraying exogenous plant hormone methyl jasmonate upon radish sprout decreases the activity of myrosinase and the amount of 4-methylthio-3-butenylisothiocyanate but increases the total phenolic content which results in increased 2,2-diphenyl-1-picrylhydrazyl free radical scavenging capacity
NaBr
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activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
NaCl
enzyme activity is progressively inhibited by NaCl addition to the reactions and is completely inhibited at 1 M NaCl
Salicin
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0.1 M, 1% inhibition in presence of ascorbate, 6% inhibition in absence of ascorbate
sinigrin
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competitive inhibition of hydrolysis of p-nitrophenyl beta-glucoside
Trinitrobenzenesulfonic acid
Sinapis sp.
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rate of inhibition is accelerated by 1 mM ascorbic acid
additional information
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myrosinase activity declined rapidly after crushing, perhaps due to inactivation by the reaction products and/or the depletion of its substrates
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additional information
sugars and glucosides act as competitive inhibitors
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additional information
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application of low pressure (50 to 100 MPa) slightly enhances the activity while at higher pressure (300 MPa), the activity is largely reduced
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additional information
increasing the pressure level (100-800 MPa) results in a decrease in the myrosinase activity in accordance with previous findings of the pressure effect on myrosinase from Brussels sprouts seedlings, dependent also on the temperature, modeling, overview. Enzyme inactivation at 800 MPa
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additional information
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increasing the pressure level (100-800 MPa) results in a decrease in the myrosinase activity in accordance with previous findings of the pressure effect on myrosinase from Brussels sprouts seedlings, dependent also on the temperature, modeling, overview. Enzyme inactivation at 800 MPa
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additional information
the enzyme shows substrate inhibition via a binding site mechanisms, and is sensitive against heat and pressure
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additional information
broccoli myrosinase subunit has two substrate-binding sites: a catalytic site where the substrate is more related to the enzyme and the residues that hydrolyze the substrate, and a second binding site with lower affinity for the substrate that might be an inhibitory site. The molecular simulations confirm the hypothesis of substrate inhibition through a two-binding site mechanism suggested by the kinetic data
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additional information
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broccoli myrosinase subunit has two substrate-binding sites: a catalytic site where the substrate is more related to the enzyme and the residues that hydrolyze the substrate, and a second binding site with lower affinity for the substrate that might be an inhibitory site. The molecular simulations confirm the hypothesis of substrate inhibition through a two-binding site mechanism suggested by the kinetic data
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additional information
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growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
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additional information
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growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
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additional information
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growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
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additional information
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growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
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additional information
no inhibition at 10 mM 2'-sulfatophenyl-1-thio-beta-D-glucopyranoside
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additional information
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low correlation levels (R2) between the glucosinolates (Gls) and myrosinase (MYR) activity of 0.57, 0.28 and 0.39 for the refrigeration, shade and sun exposure treatments are obtained. The cooking regimes tested, i.e. boiling, microwaving, and baking, totally inactivate MYR without affecting the Gls content
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