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 (Activating Compound
Activating Compound on EC 3.2.1.147 - thioglucosidase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
abscisic acid
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ABA, significantly increases glucosinolate content, isothiocyanate formation and myrosinase activity by 72.65%, 268.15% and 67.69%, respectively, at 0.05 mg/ml in 5-day-old sprouts
nitrile-specifier protein
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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
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ascorbic acid
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the myrosinase isozymes show different activationinhibition responses towards ascorbic acid with maximal activity around 0.7-1 mM
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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activates, enzyme is conformationally changed, no activation by analogs
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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maximal activation for myrosinase I, 50fold at 0.3 mM. Maximal activation for myrosinase II, 106fold between 0.3 and 0.5 mM
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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active only in presence of L-ascorbic acid, maximal activation at 2 mM
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
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activates, enzyme is still active in absence of ascorbic acid although to much lesser extent, in this circumstances benzyl thiocyanate is an additional product in hydrolysis of benzylglucosinolate
ascorbic acid
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dependent on, all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid, uncompetitive activation by ascorbic acid
ascorbic acid
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considerable activation in the pH range 5.7-7.5, maximal activation at 0.375 mM
ascorbic acid
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1 mM, activation of isoenzyme SA, SB, very low activation of isoenzyme SC
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid, mechanism of ascorbic acid activation, overview
epithiospecifier protein
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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.
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epithiospecifier protein
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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.
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epithiospecifier protein
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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
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epithiospecifier protein
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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.
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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.
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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.
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epithiospecifier protein
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interacts with myrosinase to promote sulfur transfer from the S-glucose moiety to the terminal alkenyl moiety. Degradation of progoitrin produces mainly oxazolidine-2-thione in the absence of epithiospecifier protein and mainly epithionitrile in the presence of epithiospecifier protein
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epithiospecifier protein
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non-specific requirement for epithiospecifier protein
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epithiospecifier protein
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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.
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epithiospecifier protein
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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
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epithiospecifier protein
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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
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epithiospecifier protein
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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
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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
isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity
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additional information
isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity
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additional information
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redox-regulated, the reduced form is more active
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