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Information on EC 3.2.1.147 - thioglucosidase
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EC Tree
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 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtBGLU37
AtBGLU38
atypical myrosinase
beta-glucosidase 26, peroxisomal
beta-glucosidase 37
beta-glucosidase 38
beta-thioglucosidase
beta-thioglucosidase glucohydrolase
beta-thioglucoside glucohydrolase
BGLU26
EC 3.2.3.1
glucosidase, thio-
-
-
-
-
glucosinolase
-
-
-
-
MYR
myrosin
-
-
-
-
myrosinase
PEN2
sinigrase
-
-
-
-
sinigrinase
sinigrinase 1
sinigrinase 2
TGG1
TGG2
Thioglucosidase
-
-
-
-
thioglucoside glucohydrolase
thioglycosidase
beta-thioglucosidase
-
-
-
-
beta-thioglucoside glucohydrolase
-
-
-
-
EC 3.2.3.1
-
-
formerly
-
myrosinase
-
-
-
-
myrosinase
-
-
sinigrinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a thioglucoside + H2O = a sugar + a thiol
the mechanism involves a first step acid-base catalyzed reaction with the formation of the glycosyl enzyme intermediate and the benzyl isothiocyanate obtained by the enzyme-independent Lossen rearrangement of the transient thiohydroximate-O-sulfonate, a sulfate anion and a proton are also released
-
a thioglucoside + H2O = a sugar + a thiol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-beta-glucosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of S-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
thioglucoside glucohydrolase
Has a wide specificity for thioglycosides.
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CAS REGISTRY NUMBER
COMMENTARY
9025-38-1
-
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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
(2S)-2-hydroxy-3-butenyl glucosinolate + H2O
D-glucose +
-
i.e. epi-progoitrin
presence of endogenous epithiospecifier protein directs the reaction toward formation of an epithionitrile
-
?
(R)-4-methylsulfinylbutyl glucosinolate + H2O
?
-
i.e. glucoraphanin or GRP
-
-
?
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
2-(4-hydroxyphenyl)ethylglucosinolate + H2O
D-glucose + 4-(2-carboxy-1-hydroxyethyl)phenyl sulfate
-
-
-
-
?
2-(4-methoxyphenyl)ethylglucosinolate + H2O
D-glucose + 4-(2-cyano-1-hydroxyethyl)phenyl sulfate + 4-(2-cyanoethyl)phenyl sulfate
-
-
-
-
?
2-hydroxy-3-butenylglucosinolate + H2O
5-vinyl-2-oxazolidine thione + D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-phenylethylglucosinolate + H2O
2-phenylethyl-isothiocyanate + D-glucose
-
-
-
-
?
2-propenylglucosinolate + H2O
2-propenyl-isothiocyanate + D-glucose
-
epithiospecifier protein and nitrile-specifier protein can switch myrosinase-catalyzed degradation of 2-propenylglucosinolate from isothiocyanate to nitrile, only epithiospecifier protein generates the corresponding epithionitrile
-
-
?
3-benzyloxypropylglucosinolate + H2O
3-benzyloxypropyl-isothiocyanate + D-glucose
-
-
-
-
?
3-butenylglucosinolate + H2O
3-butenyl-isothiocyanate + D-glucose
-
-
-
-
?
3-methylthiopropylglucosinolate + H2O
3-methylthiopropyl-isothiocyanate + D-glucose
-
-
-
-
?
4-(methylsulfinyl)butyl glucosinolate + H2O
D-glucose + ?
-
i.e. glucoraphanin
presence of endogenous epithiospecifier protein directs the reaction toward formation of sulforaphane nitrile in place of the anticancerogenic sulforaphane
-
?
4-benzyloxybutylglucosinolate + H2O
4-benzyloxybutyl-isothiocyanate + D-glucose
-
-
-
-
?
4-hydroxybenzyl glucosinolate + H2O
4-hydroxybenzyl isothiocyanate + D-glucose
-
-
-
-
?
4-hydroxybenzylglucosinolate + H2O
D-glucose + 4-hydroxyphenylacetamide sulfate + ?
-
-
-
-
?
4-hydroxybenzylglucosinolate + H2O
D-glucose + 4-hydroxyphenylacetonitrile sulfate + ?
-
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
4-methylsulfinylbutyl glucosinolate + H2O
4-methylsulfinylbutyl isothiocyanate + D-glucose
-
isolated from seeds of Sinapis alba
-
-
?
4-methylsulfinylbutylglucosinolate + H2O
4-methylsulfinylbutyl-isothiocyanate + D-glucose
-
-
-
-
?
4-methylthiobutylglucosinolate + H2O
4-methylthiobutyl-isothiocyanate + D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
4-nitrophenyl 2-acetamido-2-deoxy-1-thio-beta-D-glucopyranoside + H2O
4-nitrobenzenethiol + N-acetyl-D-glucosamine
4-pentenylglucosinolate + H2O
4-pentenyl-isothiocyanate + D-glucose
-
-
-
-
?
5-methylthiopentylglucosinolate + H2O
5-methylthiopentyl-isothiocyanate + D-glucose
-
-
-
-
?
6-methylthiohexylglucosinolate + H2O
6-methylthiohexyl-isothiocyanate + D-glucose
-
-
-
-
?
7-methylthioheptylglucosinolate + H2O
7-methylthioheptyl-isothiocyanate + D-glucose
-
-
-
-
?
8-methylthiooctylglucosinolate + H2O
8-methylthiooctyl-isothiocyanate + D-glucose
-
-
-
-
?
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
benzylisothiocyanate + D-glucose + ?
-
nitrile-specifier proteins, especially nitrile-specifier protein 2, NSP2, in conjunction with myrosinase enable the enzyme to generate nitriles, overview
-
-
?
glucoraphenin + H2O
?
-
3.8% of the activity with epi-progoitrin
-
-
?
glucosinolate + H2O
isothiocyanate + thiocyanate + nitrile + epithionitrile + ?
-
-
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indo-3-ylmethyl isothiocyanate + D-glucose
-
high activity
-
-
?
indolyl-3-methylglucosinolate + H2O
indolyl-3-methyl-isothiocyanate + D-glucose
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
progoitrin + H2O
(1E,3S)-3-hydroxy-n-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
(2R)-2-hydroxy-2-phenylethylglucosinolate + H2O
D-glucose + ?
-
i.e. glucosibarin
-
-
?
(2R)-2-hydroxy-2-phenylethylglucosinolate + H2O
D-glucose + ?
-
i.e. glucosibarin
-
-
?
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
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
-
?
4-nitrophenyl 2-acetamido-2-deoxy-1-thio-beta-D-glucopyranoside + H2O
4-nitrobenzenethiol + N-acetyl-D-glucosamine
-
-
-
-
?
4-nitrophenyl 2-acetamido-2-deoxy-1-thio-beta-D-glucopyranoside + H2O
4-nitrobenzenethiol + N-acetyl-D-glucosamine
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
a poor substrate for ArMy2
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
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
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
glucoraphanin + H2O
sulforaphane + D-glucose
-
-
-
?
glucosinalbin + H2O
?
-
9.5% of the activity with epi-progoitrin
-
-
?
glucotropaeolin + H2O
?
-
7.8% of the activity with epi-progoitrin
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
progoitrin + H2O
?
-
9.8% of the activity with epi-progoitrin
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
best substrate
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
i.e. 2-propenyl glucosinolate, substrate saturation at 6 mM
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
D-glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
-
-
-
?
sinigrin + H2O
D-glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
15.3% of the activity with epi-progoitrin
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
208545, 208548, 208550, 208557, 208563, 208565, 208566, 208571, 208578, 208580, 208583, 208584, 208585, 208586, 208589
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
2-propenylglucosinolate
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
Paracolobactrum aerogenoides
-
-
-
-
?
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
-
-
-
-
?
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 + 3-isothiocyanatoprop-1-ene + SO42-
Sinapis sp.
-
-
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate + ?
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
-
-
-
-
?
2-hydroxybut-3-enylglucosinolate + H2O
additional information
-
-
-
in absence of ascorbate 5-vinyloxazolidine-2-thione is the only product, whereas in the presence of added ascorbate 1-cyano-2-hydroxybut-3-ene is also formed
?
2-hydroxybut-3-enylglucosinolate + H2O
additional information
-
-
-
5-vinyloxazolidine-2-thione is the sole product above pH 5.4, reaching a maximum at pH 8.0, whilst 1-cyano-2-hydroxybut-3-ene is the main product at low pH reaching a maximum at pH 3.4
?
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
?
2-phenethylglucosinolate + H2O
additional information
-
-
-
in presence of ascorbic acid, isothiocyanate and nitrile are obtained but no thiocyanate
?
2-phenethylglucosinolate + H2O
additional information
-
Sinapis sp.
-
-
nitrile formation is favoured at lower pH levels, the ratio of nitrile to isothiocyanate is directly related to the hydrogen ion concentration of the medium
?
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
?
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
-
-
-
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
-
-
-
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 ascorbic acid, isothiocyanate and nitrile are obtained but no thiocyanate
?
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
?
allylglucosinolate + H2O
additional information
-
Sinapis sp.
-
-
nitrile formation is favoured at lower pH levels, the ratio of nitrile to isothiocyanate is directly related to the hydrogen ion concentration of the medium
?
additional information
?
-
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
-
-
?
additional information
?
-
-
differences in basal activity of myrosinase isozymes, no activity with desulfosinigrin
-
-
?
additional information
?
-
-
myrosinase acts on glucosinolates to form an unstable aglycone intermediate that can rearrange spontaneously to form an isothiocyanate. Interaction of a protein called epithiospecifier protein with myrosinase diverts the reaction toward the production of epithionitriles or nitriles depending on the glucosinolate structure, while nitrile-specifier proteins, especially nitrile-specifier protein 2, NSP2, enable to generate nitriles in conjunction with myrosinase, tissue distributions of the specifier proteins, overview
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
indole glucosinolates are in planta substrates for PYK10
-
-
?
additional information
?
-
-
enzyme PYK10 has in vitro myrosinase activity toward indole glucosinolates. PYK10 exhibits both O-glucosidase and S-glucosidase activity. No activity against sinigrin. PYK10 hydrolyzes both coumarin glucosides and glucosinolates, and accounts for the bulk of total myrosinase activity against indol-3-ylmethyl glucosinolate in Arabidopsis thaliana roots
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
the enzyme is active with indole and aliphatic glucosinolates
-
-
?
additional information
?
-
the enzyme is active with indole and aliphatic glucosinolates
-
-
?
additional information
?
-
the enzyme is active with indole and aliphatic glucosinolates
-
-
?
additional information
?
-
the enzyme is active with indole and aliphatic glucosinolates
-
-
?
additional information
?
-
myrosinase-catalyzed deglycosylation of a glucosinolate releases beta-D-glucose and an unstable intermediate, which undergoes rearrangements to finally yield an isothiocyanate
-
-
?
additional information
?
-
-
myrosinase-catalyzed deglycosylation of a glucosinolate releases beta-D-glucose and an unstable intermediate, which undergoes rearrangements to finally yield an isothiocyanate
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
hydrolysis of rapeseed meal yields 1-cyano-2-hydroxy-3-butene, 5-vinyloxazolidine-2-thione, 3-butenylisothiocyanate and 4-pentenylisothiocyanate
-
-
?
additional information
?
-
MYR is a beta-thioglucosidase that hydrolyses glucosinolates to a variety of products such as isothiocyanates, thiocyanates, nitriles, epithionitriles, and oxazolidine-thiones depending on the nature of the glucosinolates. Glucosinolates are themselves biologically inactive, but glucosinolates hydrolytic products, such as thiocyanates, isothiocyanates, nitriles, and oxazolidine-2-thione, produced by MYR during processing of oilseed rape meal are biologically active. Glucosinolate profiles of wild-type and mutant plants, overview
-
-
?
additional information
?
-
-
MYR is a beta-thioglucosidase that hydrolyses glucosinolates to a variety of products such as isothiocyanates, thiocyanates, nitriles, epithionitriles, and oxazolidine-thiones depending on the nature of the glucosinolates. Glucosinolates are themselves biologically inactive, but glucosinolates hydrolytic products, such as thiocyanates, isothiocyanates, nitriles, and oxazolidine-2-thione, produced by MYR during processing of oilseed rape meal are biologically active. Glucosinolate profiles of wild-type and mutant plants, overview
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Ioszyme MYRI is maximally active against aliphatic glucosinolate followed by aromatic glucosinolates, and indole glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Ioszyme MYRI is maximally active against aliphatic glucosinolate followed by aromatic glucosinolates, and indole glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Ioszyme MYRII is maximally active against aliphatic glucosinolate followed by aromatic glucosinolates, and indole glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Ioszyme MYRII is maximally active against aliphatic glucosinolate followed by aromatic glucosinolates, and indole glucosinolates
-
-
?
additional information
?
-
-
in intact plant tissues, the enzyme is physically separated from its GSL substrates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
substrate docking analysis. modeling of glucoraphanin and sinigrin into the regulatory and the active site, three-dimensional structure model of broccoli myrosinase, modeling and validation, overview
-
-
?
additional information
?
-
-
substrate docking analysis. modeling of glucoraphanin and sinigrin into the regulatory and the active site, three-dimensional structure model of broccoli myrosinase, modeling and validation, overview
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
recombinant TGG1 has weak ascorbic acid-independent O-beta-glucosidase activity with substrate specificity
-
-
?
additional information
?
-
-
recombinant TGG1 has weak ascorbic acid-independent O-beta-glucosidase activity with substrate specificity
-
-
?
additional information
?
-
the enzyme is inactive towards glucovanillin and n-octyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme is inactive towards glucovanillin and n-octyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase in general catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity
-
-
?
additional information
?
-
myrosinase in general catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. The enzyme from Crambe abyssinica is highly specific for epi-progoitrin
-
-
?
additional information
?
-
-
induced by addition of 0.01% sinigrin and 6% mustard extract
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
induced by addition of 0.01% sinigrin and 6% mustard extract
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
the enzyme produces nitriles from desulfoglucosinolates
-
-
?
additional information
?
-
Escherichia coli VL8
-
the enzyme produces nitriles from desulfoglucosinolates
-
-
?
additional information
?
-
-
compositions and contents of glucosinolates in salt cress, Thellungiella halophila, at different developmental stages, HPLC-MS analysis, profiles, overview
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview. Paraphoma radicina strain E5 shows a low overall activity on glucosinolates compared to other endophytic fungi
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview. Paraphoma radicina strain E5 shows a low overall activity on glucosinolates compared to other endophytic fungi
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview. Paraphoma radicina strain E5 shows a low overall activity on glucosinolates compared to other endophytic fungi
-
-
?
additional information
?
-
highest myrosinase activity is detected with allylglucosinolate. Activity with 3-butenylglucosinolate, 4-pentenylglucosinolate, and 4-methylsulfinylbutyl glucosinolate is 50-70% of that with allylglucosinolate, overview
-
-
?
additional information
?
-
-
highest myrosinase activity is detected with allylglucosinolate. Activity with 3-butenylglucosinolate, 4-pentenylglucosinolate, and 4-methylsulfinylbutyl glucosinolate is 50-70% of that with allylglucosinolate, overview
-
-
?
additional information
?
-
-
leaves of four-week old Brassica rapa plants that have been damaged by Psylliodes chrysocephala adults for one week are analyzed for their glucosinolates profiles, overview
-
-
?
additional information
?
-
-
the enzyme is normally physically segregated from the glucosinolates, but when the cells are damaged, e.g. during food preparation, mastication or injury by predators such as insects, the enzyme is released and catalyzes their hydrolysis of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
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
-
-
?
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
-
-
?
progoitrin + H2O
additional information
-
-
-
mainly oxazolidine-2-thione in the absence of epithiospecifier protein and mainly epithionitrile in the presence of epithiospecifier protein
?
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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
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucobrassicin + H2O
indol-3-ylmethylisothiocyanate + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucocochlearin + H2O
(1E)-2-methyl-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
glucoiberin + H2O
(1E)-4-(methylsulfinyl)-N-(sulfooxy)butanimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
gluconapin + H2O
(1E)-N-(sulfooxy)pent-4-enimidothioic acid + D-glucose
-
-
-
-
?
glucoraphanin + H2O
sulforaphane + D-glucose
-
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
sinigrin + H2O
(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose
-
-
-
-
?
additional information
?
-
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
indole glucosinolates are in planta substrates for PYK10
-
-
?
additional information
?
-
MYR is a beta-thioglucosidase that hydrolyses glucosinolates to a variety of products such as isothiocyanates, thiocyanates, nitriles, epithionitriles, and oxazolidine-thiones depending on the nature of the glucosinolates. Glucosinolates are themselves biologically inactive, but glucosinolates hydrolytic products, such as thiocyanates, isothiocyanates, nitriles, and oxazolidine-2-thione, produced by MYR during processing of oilseed rape meal are biologically active. Glucosinolate profiles of wild-type and mutant plants, overview
-
-
?
additional information
?
-
-
MYR is a beta-thioglucosidase that hydrolyses glucosinolates to a variety of products such as isothiocyanates, thiocyanates, nitriles, epithionitriles, and oxazolidine-thiones depending on the nature of the glucosinolates. Glucosinolates are themselves biologically inactive, but glucosinolates hydrolytic products, such as thiocyanates, isothiocyanates, nitriles, and oxazolidine-2-thione, produced by MYR during processing of oilseed rape meal are biologically active. Glucosinolate profiles of wild-type and mutant plants, overview
-
-
?
additional information
?
-
-
in intact plant tissues, the enzyme is physically separated from its GSL substrates
-
-
?
additional information
?
-
-
induced by addition of 0.01% sinigrin and 6% mustard extract
-
-
?
additional information
?
-
-
induced by addition of 0.01% sinigrin and 6% mustard extract
-
-
?
additional information
?
-
-
compositions and contents of glucosinolates in salt cress, Thellungiella halophila, at different developmental stages, HPLC-MS analysis, profiles, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview. Paraphoma radicina strain E5 shows a low overall activity on glucosinolates compared to other endophytic fungi
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview. Paraphoma radicina strain E5 shows a low overall activity on glucosinolates compared to other endophytic fungi
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview. Paraphoma radicina strain E5 shows a low overall activity on glucosinolates compared to other endophytic fungi
-
-
?
additional information
?
-
-
leaves of four-week old Brassica rapa plants that have been damaged by Psylliodes chrysocephala adults for one week are analyzed for their glucosinolates profiles, overview
-
-
?
additional information
?
-
-
the enzyme is normally physically segregated from the glucosinolates, but when the cells are damaged, e.g. during food preparation, mastication or injury by predators such as insects, the enzyme is released and catalyzes their hydrolysis of glucosinolates
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
additional information
?
-
-
decomposition of glucosinolates in horseradish extract inoculated by endophytic fungi from horseradish, overview
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
both epithiospecifier protein and nitrile-specifier protein are true enzymes rather than allosteric cofactors of myrosinase
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe2+
-
shifts the enzyme to nitril fomration with increasing concentration
K+
KNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
Mg2+
Mn2+
Na+
NaBr
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
NaNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
Zn2+
additional information
Ca2+
-
slight activation in presence of 1 mM ascorbate, no effect in absence of ascorbate
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
additional information
-
the isozymes are active in a wide range of salt concentrations but sensitive to high salt concentrations
additional information
-
Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production
additional information
-
Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production
additional information
-
Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production
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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
-
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
cysteamine
-
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
-
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
-
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
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
NaNO3
-
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
-
strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0
Thiomalate
-
strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0
Thiophenol
-
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
-
inhibition of hydrolysis of sinigrin and progoitrin at pH 5 and at pH 7
2-deoxy-2-fluoroglucotropaeolin
-
inhibition occurs via the accumulation of a long-life glucosyl-enzyme intermediate
arbutin
-
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
-
the alkaloidal glycosidase inhibitor acts as competitive inhibitor
Fe2+
-
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+
-
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
-
1.0 M, 22% inhibition in presence of ascorbate, competitive. No inhibition in absence of ascorbate
L-Cys
-
5 mM, and 2.5 mM Fe2+, pH 5.0 or 6.5, strong inhibition of formation of allyl isothiocyanate
maltose
-
1.0 M, 33% inhibition in absence of ascorbate, 6% inhibition in presence of ascorbate
methyl jasmonate
-
decrease in enzyme activity, concommitant increase in levels of 4-methylsulfinylbutylglucosinolate and 8-methylsulfinylbutylglucosinolate in hypocotyl
methyl jasmonate
-
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
-
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
-
0.1 M, 1% inhibition in presence of ascorbate, 6% inhibition in absence of ascorbate
sinigrin
-
competitive inhibition of hydrolysis of p-nitrophenyl beta-glucoside
Trinitrobenzenesulfonic acid
Sinapis sp.
-
rate of inhibition is accelerated by 1 mM ascorbic acid
additional information
-
myrosinase activity declined rapidly after crushing, perhaps due to inactivation by the reaction products and/or the depletion of its substrates
-
additional information
sugars and glucosides act as competitive inhibitors
-
additional information
-
application of low pressure (50 to 100 MPa) slightly enhances the activity while at higher pressure (300 MPa), the activity is largely reduced
-
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
-
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
-
additional information
the enzyme shows substrate inhibition via a binding site mechanisms, and is sensitive against heat and pressure
-
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
-
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
-
additional information
-
growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
-
additional information
-
growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
-
additional information
-
growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
-
additional information
-
growth inhibition of the fungus by allyl isothiocyanate and 2-phenylethyl isothiocyanate
-
additional information
no inhibition at 10 mM 2'-sulfatophenyl-1-thio-beta-D-glucopyranoside
-
additional information
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
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
-
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
-
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
-
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
-
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
-
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
-
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
-
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
-
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
-
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
-
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
-
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
-
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
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid, mechanism of ascorbic acid activation, overview
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
-
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
-
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
-
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
-
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
-
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
-
epithiospecifier protein
-
non-specific requirement for epithiospecifier protein
-
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
-
additional information
-
application of low pressure (50 to 100 MPa) slightly enhances the activity while at higher pressure (300 MPa), the activity is largely reduced
-
additional information
isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity
-
additional information
isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity
-
additional information
-
redox-regulated, the reduced form is more active
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Astrocytoma
Rapha Myr®, a Blend of Sulforaphane and Myrosinase, Exerts Antitumor and Anoikis-Sensitizing Effects on Human Astrocytoma Cells Modulating Sirtuins and DNA Methylation.
Carcinogenesis
Apoptosis as a Mechanism of the Cancer Chemopreventive Activity of Glucosinolates: a Review
Carcinogenesis
Preclinical and clinical evaluation of sulforaphane for chemoprevention in the breast.
Carcinoma, Hepatocellular
Glucosinolate-Enriched Fractions from Maca (Lepidium meyenii) Exert Myrosinase-Dependent Cytotoxic Effects against HepG2/C3A and HT29 Tumor Cell Lines.
Cerebral Palsy
Toxicity of Glucosinolate Degradation Products from Brassica napus Seed Meal Toward Aphanomyces euteiches f. sp. pisi.
Colitis
Lightly Cooked Broccoli Is as Effective as Raw Broccoli in Mitigating Dextran Sulfate Sodium-Induced Colitis in Mice.
Colonic Neoplasms
Glucosinolate-Enriched Fractions from Maca (Lepidium meyenii) Exert Myrosinase-Dependent Cytotoxic Effects against HepG2/C3A and HT29 Tumor Cell Lines.
Colonic Neoplasms
Myrosinase Hydrolysates of Brassica oleraceae L. Var. italica Reduce the Risk of Colon Cancer.
Colorectal Neoplasms
Engineered commensal microbes for diet-mediated colorectal-cancer chemoprevention.
Colorectal Neoplasms
Inhibition of dimethylhydrazine-induced aberrant crypt foci and induction of apoptosis in rat colon following oral administration of the glucosinolate sinigrin.
Cysts
Effects of intact glucosinolates and products produced from glucosinolates in myrosinase-catalyzed hydrolysis on the potato cyst nematode (Globodera rostochiensis Cv. Woll).
Encephalomyelitis
Protective role of (RS )-glucoraphanin bioactivated with myrosinase in an experimental model of multiple sclerosis.
Encephalomyelitis
The protective effects of bioactive (RS)-glucoraphanin on the permeability of the mice blood-brain barrier following experimental autoimmune encephalomyelitis.
Encephalomyelitis, Autoimmune, Experimental
Protective role of (RS )-glucoraphanin bioactivated with myrosinase in an experimental model of multiple sclerosis.
Encephalomyelitis, Autoimmune, Experimental
The protective effects of bioactive (RS)-glucoraphanin on the permeability of the mice blood-brain barrier following experimental autoimmune encephalomyelitis.
Infections
Glucosinolate profile and Myrosinase gene expression are modulated upon Plasmodiophora brassicae infection in cabbage.
Infections
The myrosinase-glucosinolate system in the interaction between Leptosphaeria maculans and Brassica napus.
Infections
Toxicity of Glucosinolate Degradation Products from Brassica napus Seed Meal Toward Aphanomyces euteiches f. sp. pisi.
Multiple Sclerosis
Protective role of (RS )-glucoraphanin bioactivated with myrosinase in an experimental model of multiple sclerosis.
Multiple Sclerosis
The protective effects of bioactive (RS)-glucoraphanin on the permeability of the mice blood-brain barrier following experimental autoimmune encephalomyelitis.
Neoplasms
Apoptosis as a Mechanism of the Cancer Chemopreventive Activity of Glucosinolates: a Review
Neoplasms
Characterization of a novel ?-thioglucosidase CpTGG1 in Carica papaya and its substrate-dependent and ascorbic acid-independent O-?-glucosidase activity.
Neoplasms
Identification, synthesis, and enzymology of non-natural glucosinolate chemopreventive candidates.
Neoplasms
Induction of Apoptosis and Cytotoxicity by Raphasatin in Human Breast Adenocarcinoma MCF-7 Cells.
Neoplasms
Kaiware Daikon (Raphanus sativus L.) extract: a naturally multipotent chemopreventive agent.
Neoplasms
Myrosinase Hydrolysates of Brassica oleraceae L. Var. italica Reduce the Risk of Colon Cancer.
Neoplasms
Relationship of climate and genotype to seasonal variation in the glucosinolate-myrosinase system. II. Myrosinase activity in ten cultivars of Brassica oleracea grown in fall and spring seasons.
Neuroblastoma
Moringin from Moringa Oleifera Seeds Inhibits Growth, Arrests Cell-Cycle, and Induces Apoptosis of SH-SY5Y Human Neuroblastoma Cells through the Modulation of NF-?B and Apoptotic Related Factors.
Neuroinflammatory Diseases
Moringin activates Wnt canonical pathway by inhibiting GSK3? in a mouse model of experimental autoimmune encephalomyelitis.
Parkinson Disease
Anti-inflammatory and anti-apoptotic effects of (RS)-glucoraphanin bioactivated with myrosinase in murine sub-acute and acute MPTP-induced Parkinson's disease.
Parkinson Disease
The Isothiocyanate Isolated from Moringa oleifera Shows Potent Anti-Inflammatory Activity in the Treatment of Murine Subacute Parkinson's Disease.
Spinal Cord Injuries
RS-Glucoraphanin bioactivated with myrosinase treatment counteracts proinflammatory cascade and apoptosis associated to spinal cord injury in an experimental mouse model.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.81
4-nitrophenyl beta-D-glucopyranoside
recombinant enzyme, pH 5.5, 37°C
0.05
sinigrin
recombinant enzyme TGG2, pH 5.5, 37°C, in presence of ascorbate
0.108
sinigrin
recombinant enzyme TGG1, pH 5.5, 37°C, in presence of ascorbate
6.28
sinigrin
-
enzyme immobilized into Ca-polygalacturonate, at pH 6.5 and 37°C
additional information
additional information
kinetics modeling: Michaelis-Menten model (M-M), two-binding sites model (TBSM), and Michaelis-Menten with substrate inhibition (MMSI) model. The TBSM represents more accurately the system behaviour, with the highest R2 values, equal to 97.3% for glucoraphanin and 98.4% for sinigrin
-
additional information
additional information
-
kinetics modeling: Michaelis-Menten model (M-M), two-binding sites model (TBSM), and Michaelis-Menten with substrate inhibition (MMSI) model. The TBSM represents more accurately the system behaviour, with the highest R2 values, equal to 97.3% for glucoraphanin and 98.4% for sinigrin
-
additional information
additional information
-
the Km value of the fungus myrosinase is 20fold higher compared to the non-activated plant myrosinase
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.04
sinigrin
recombinant enzyme TGG2, pH 5.5, 37°C, in presence of ascorbate
10.7
sinigrin
recombinant enzyme TGG1, pH 5.5, 37°C, in presence of ascorbate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
4-nitrophenyl beta-D-glucopyranoside
recombinant enzyme, pH 5.5, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.368
sinigrin
-
sinigrin substrate inhibition, Michaelis-Menten modelling, pH 7.0, 40°C
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.018
-
plant crude extract, pH and temperature not specified in the publication
0.04
-
mobile enzyme fraction, pH and temperature not specified in the publication
0.058
-
plant crude extract, pH and temperature not specified in the publication
0.059
-
plant crude extract, pH and temperature not specified in the publication
0.069
-
plant crude extract, pH and temperature not specified in the publication
0.238
-
mobile enzyme fraction, pH and temperature not specified in the publication
0.263
-
mobile enzyme fraction, pH and temperature not specified in the publication
0.322
-
mobile enzyme fraction, pH and temperature not specified in the publication
0.69 - 2.04
-
enzyme from florets of the different cultivars, pH not specified in the publication, glucose assay, 40°C
0.73 - 0.86
-
enzyme from roots of the different cultivars, pH not specified in the publication, glucose assay, 40°C
0.85
-
counter-current chromatography fraction, pH and temperature not specified in the publication
1.09 - 1.68
-
enzyme from roots of the different cultivars, pH not specified in the publication, glucose assay, 40°C
1.12
-
counter-current chromatography fraction, pH and temperature not specified in the publication
1.27 - 1.85
-
enzyme from leaves of the different cultivars, pH not specified in the publication, glucose assay, 40°C
1.58
-
counter-current chromatography fraction, pH and temperature not specified in the publication
1.96 - 2.39
-
enzyme from leaves of the different cultivars, pH not specified in the publication, glucose assay, 40°C
13.08 - 15.62
-
enzyme from florets of the different cultivars, pH not specified in the publication, AITC assay, 25°C
14.46 - 20.6
-
enzyme from leaves of the different cultivars, pH not specified in the publication, AITC assay, 25°C
2.42
-
counter-current chromatography fraction, pH and temperature not specified in the publication
4.44 - 10.68
-
enzyme from roots of the different cultivars, pH not specified in the publication, AITC assay, 25°C
6.37 - 15.3
-
enzyme from roots of the different cultivars, pH not specified in the publication, AITC assay, 25°C
6.87 - 14.7
-
enzyme from leaves of the different cultivars, pH not specified in the publication, AITC assay, 25°C
additional information
additional information
-
the specific myrosinase activity in wild type seeds ranges from 0.1186-0.4263 micromol glucose/min/mg protein
additional information
-
the water contents vary from fresh broccoli with 90% water content to almost complete dry broccoli with 10% water content. The water content values are related to the aw values (partial vapor pressure of water in a substance divided by the standard state partial vapor pressure of water) in a non-linear relationship that is the moisture isotherm curve. Highest activity at 70°C with 31% water content, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
5.5
5.5 - 10.5
6 - 6.5
6 - 7
6.5
6.5 - 7
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 12
-
isozymes TGG4 and TGG5 are active at pH 2.5, and TGG4 shows a broad optimum at pH 5.5-10.5, while TGG5 peaks at pH 5.5 and than loses activity at pH 6.5 and 8.5, both show 50% of maximal activity at pH 11.5
3 - 8
-
pH 3.0: about 45% of maximal activity, pH 8.0: about 55% of maximal activity
3 - 9
-
pH 3.0: about 60% of maximal activity, pH 9.0: 80-90% of maximal activity
4 - 7
-
about 35% of maximal activity of enzyme form Cc and Cb, about 45% of maximal activity of enzyme form Ca at pH 4.0 and at pH 7.0
4 - 9
-
pH 4.0: about 45% of maximal activity, pH 9.0: about 40% of maximal activity
4.2 - 10
-
pH 4.2: about 40% of maximal activity, pH 10.0: about 55% of maximal activity
4.5 - 12
-
isozyme TGG1, inactive below pH 4.5, rather unaffected by differences in pH above 5.5
4.5 - 7
-
pH 4.5: about 40% of maximal activity, pH 7.0: about 70% of maximal activity
4.5 - 7.5
-
pH 4.5: about 75% of maximal activity, pH 7.5: about 85% of maximal activity, at 37°C, hydrolysis of epi-progoitrin
4.5 - 9
-
pH 4.5: about 55% of maximal activity, pH 9.0: about 80% of maximal activity, recombinant enzyme
5 - 10
5 - 11
CpTGG2 is active in broad pH range, almost inactive below pH 3.0 and above pH 13.0
5 - 8.5
-
pH 5.0: about 40% of maximal activity, pH 8.5: about 45% of maximal activity, hydrolysis of epiprogoitrin
5.2 - 8
-
pH 5.2: about 45% of maximal activity, pH 8.0: about 60% of maximal activity
5.2 - 8.5
-
pH 5.2: about 75% of maximal activity, pH 9.5: about 55% of maximal activity, at 37°C, hydrolysis of sinigrin
5.5 - 7.5
-
pH 5.5: about 40% of maximal activity, pH 7.5: about 60% of maximal activity
6 - 7.2
-
activity in presence of ascorbic acid is greater in sodium phosphate buffer than in citric acid /Na2HPO4 buffer
5 - 10
-
pH 5.0: about 70% of maximal activity, pH 10: about 40% of maximal activity, hydrolysis of progoitrin
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
-
at atmospheric pressure. Application of low pressure (50 to 100 MPa) slightly enhances the activity while at higher pressure (300 MPa), the activity is largely reduced
37
40
50
55
60
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 90
CpTGG2 is active in broad temperature range, peaks at 40°C, gradually decreases between 40°C and 90°C, and shows 13% residual activity at 80°C and 1% at 90°C
20 - 60
-
isozyme TGG1, 65% of maximal activity at 20°C, progressive increase that peaks at 40°C, high activity at 50°C, inactivation above 60°C
20 - 65
20 - 80
-
20% of maximal activity at 20°C, progressive increase that peaks at 70°C, 30% of maximal activity at 80°C
20 - 90
-
20% of maximal activity at 20°C, progressive increase that peaks at 60°C, 5% of maximal activity at 90°C
25 - 50
-
about 45% of maximal activity at 25°C and at 50°C, in presence of 1 mM ascorbic acid
30 - 70
-
30°C, about 60% of maximal activity of the enzyme from white cabbage, about 45% of maximal activity of the enzyme from red cabbage, 70°C: about 75% of maximal activity of the enzyme from red cabbage, about 50% of maximal activity of the enzyme from white cabbage
4 - 90
-
activity range, profile overview. Over 50% of maximal activity at 30-60°C
40 - 70
-
the water contents vary from fresh broccoli with 90% water content to almost complete dry broccoli with 10% water content. The water content values are related to the aw values (partial vapor pressure of water in a substance divided by the standard state partial vapor pressure of water) in a non-linear relationship that is the moisture isotherm curve. Highest activity at 70°C with 31% water content, overview
40 - 80
-
40°C: about 55% of maximal activity of enzyme form Ca, about 50% of maximal activity of enzyme form Cb, about 60% of maximal activity of enzyme form Cc, 80°C: about 55% of maximal activity of enzyme form Ca, about 60% of maximal activity of enzyme form Cb, about 60% of maximal activity of enzyme form Cc
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
20 - 65
-
20°C: about 85% of maximal activity, 65°C: about 45% of maximal activity, recombinant enzyme
20 - 65
-
20°C: about 70% of maximal activity, 65°C: about 65% of maximal activity at 37°C, hydrolysis of sinigrin
20 - 65
-
20°C: about 75% of maximal activity, 65°C: about 60% of maximal activity, at 37°C, hydrolysis of epi-progoitrin
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 5.6
4.9
4.8 - 5.6
-
enzyme complex is formed by isoenzymes with isoelectric points between 4.8 and 5.6
4.8 - 5.6
-
enzyme complex is formed by isoenzymes with isoelectric points between 4.8 and 5.6
4.8 - 5.6
-
enzyme complex is formed by isoenzymes with isoelectric points between 4.8 and 5.6
4.8 - 5.6
-
enzyme complex is formed by isoenzymes with isoelectric points between 4.8 and 5.6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NR463, UV mutation induces myrosinase overproduction. strain NR463U4 produces 2.35 U/ml at 36 h of cultivation
-
-
brenda
cultivars Hinova, Megaton, Alfredo, Candela, and Bronco
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
isolated from Armoracia rusticana roots, from cultivated populations in the region of Ujleta or Debrecen
-
-
brenda
Sinapis sp.
isozyme TGG1; ecotype Columbia, Col-0, isozyme TGG1, gene tgg1
UniProt
brenda
isozyme TGG2; ecotype Columbia, Col-0, isozyme TGG2, gene tgg2
UniProt
brenda
-
208542, 208545, 208548, 208566, 208583, 208584, 208585, 208586, 666616, 666810, 680575, 710234, 714916, 715767
-
-
brenda
kale, Acephala Group, cv. Red Winter, Red Russian, Dwarf Blue Curled Vates
-
-
brenda
leaves are collected in California (Moringa Farms, Sherman Oaks, CA, USA)
-
-
brenda
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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
low expression of isoform TGG1, no expression of isoform TGG2. Monitoring of the levels of glucosinolates
brenda
-
cellular separation of myrosinase enzyme and glucosinolate substrate. In the flower stalk, myrosinase-containing phloem cell are located between phloem sieve elements and glucosinolate-rich S cells
brenda
additional information
-
of root. The level of the myrosinase activity in the peeling, which consists of the epidermis, cortex and vasvular cambium, is much higher than that in the peeled root
brenda
-
of root. The level of the myrosinase activity in the peeling, which consists of the epidermis, cortex and vascular cambium, is much higher than that in the peeled root
brenda
-
of root. The level of the myrosinase activity in the peeling, which consists of the epidermis, cortex and vasvular cambium, is much higher than that in the peeled root
brenda
-
enzyme activity is restricted to guard cells and phloem idioblasts
brenda
TGG1 is a strikingly abundant protein in guard cells
brenda
TGG1 is highly abundant in guard cells of leaves
brenda
-
TGG1 is highly abundant in guard cells of leaves
-
brenda
-
hypocotyl of seedling, high expression of isoform TGG1, no expression of isoform TGG2
brenda
TGG1 is cell type-specific expressed in specialized myrosin cells
brenda
-
TGG1 is cell type-specific expressed in specialized myrosin cells
-
brenda
-
activity is 4-5 times higher in the outer leaves than in the stalk, the inner leaves and the centre of the Brussels sprouts
brenda
-
myrosin cells are different from companion cells and the glucosinolate-containing S-cells
brenda
-
myrosin cells are different from companion cells and the glucosinolate-containing S-cells
brenda
-
exclusively localized to the interior of the myrosin grains
brenda
-
enzyme activity is restricted to guard cells and phloem idioblasts
brenda
-
-
208544, 208553, 208554, 208565, 208579, 208580, 208590, 208591, 665024, 679740, 680575, 715202, 716272, 716638, 731948, 732613, 753624, 755016, 755017
brenda
-
hypocotyl of seedling, high expression of isoform TGG1, no expression of isoform TGG2
brenda
-
myrosinase gene MYR2 is transcribed in all organs of the seedling, myrosinase gene Myr1 shows no transcription in seedling
brenda
-
the enzyme activity can vary among different botanical groups and different growing seasons
brenda
additional information
-
no myrosin cells are detected in the ground tissue
brenda
additional information
TGG1 accumulates abnormally in mns mutants
brenda
additional information
TGG1 accumulates abnormally in mns mutants
brenda
additional information
TGG2 accumulates abnormally in mns mutants
brenda
additional information
TGG2 accumulates abnormally in mns mutants
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression
brenda
additional information
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
brenda
additional information
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
brenda
additional information
-
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
-
brenda
additional information
-
TGG1 accumulates abnormally in mns mutants
-
brenda
additional information
-
TGG2 accumulates abnormally in mns mutants
-
brenda
additional information
glucosinolate contents in young and storage root and in leaves, overview
brenda
additional information
-
glucosinolate contents in young and storage root and in leaves, overview
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression
brenda
additional information
-
in intact plant tissues, the enzyme is physically separated from its GSL substrates
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific
brenda
additional information
-
the TGG2 orthologue is present in different organs, but not in roots
brenda
additional information
-
glucosinolate profiles in different tissues, overview
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
-
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
-
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
-
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
brenda
additional information
-
the fungus accepts sinigrin as sole carbon source
-
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific
brenda
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. In the halophyte Thellungiella salt stress enhances myrosinase activity during the vegetative phase in the rosette leaves, with no relation between the changes in glucosinolate content and myrosinase activity in the roots
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
endoplasmic reticulum (ER) bodies in Arabidopsis thaliana contain large amounts of beta-glucosidases, and PYK10 is the most abundant beta-glucosidase in root ER bodies
-
brenda
-
associated with the cytoplasmic side of internal membranes
brenda
-
the specific activity of the protoplast is less than that of the intact root tissue
-
brenda
-
the specific activity of the protoplast is less than that of the intact root tissue
-
brenda
-
the specific activity of the protoplast is less than that of the intact root tissue
-
brenda
-
the specific activity of the protoplast is less than that of the intact root tissue
-
brenda
-
the specific activity of the protoplast is less than that of the intact root tissue
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family 1 and has up to 76% sequence similarity to other beta-glucosidases, phylogenetic analyses. Species-specific diversification of this gene family in insects and an independent evolution of the beetle myrosinase from other insect beta-glucosidases
evolution
-
in silico three-dimensional modeling, combined with phylogenomic analysis, suggests that PYK10 represents a clade of 16 myrosinases that arose independently from the other well-documented class of six thioglucoside glucohydrolases. Phylogenomic and three-dimensional structural modeling analysis identified the presence of two independent classes of myrosinases, represented by PYK10/PEN2 and thioglucoside glucohydrolases (TGGs). Analysis of evolutionary origin of myrosinases, overview. Gene modules composed of IG modification, hydrolysis and catabolism genes may facilitate a functional differentiation among myrosinases
evolution
most of the MYR I clustered myrosinase genes use GC-AG intron splice donor site for intron 1 whereas TGG4, TGG5, and TGG6 of Arabidopsis thaliana (AtTGG4-6) and Arabidopsis lyrata (AlTGG4-6) genes in the MYR II cluster contain a GC-AG splice donor for intron 10. AtTGG5 also has a GC splice donor site for intron 3
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
evolution
-
the purified enzyme from Lepidum latifolium is encoded by the MYR I gene subfamily
malfunction
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
malfunction
-
double haploid myrosin cell-free plants (MINELESS plants) have significantly reduced myrosinase levels and glucosinolate hydrolysis products
malfunction
the classic myrosinase beta-thioglucoside glucohydrolase (TGG)-deficient double mutant tgg1 tgg2, rather than atypical myrosinase-deficient mutant pen2-2, is more sensitive to the mycotoxin fumonisin B1 (FB1) than wild-type Col-0, and the elevated expression of isozyme TGG1, but not of PEN2, correlates with the decrease in indole glucosinolate (IGS), TGG-dependent IGS hydrolysis is involved in FB1-induced programmed cell death (PCD)
malfunction
the tgg1, single and tgg1 tgg2 double mutants show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
malfunction
-
the classic myrosinase beta-thioglucoside glucohydrolase (TGG)-deficient double mutant tgg1 tgg2, rather than atypical myrosinase-deficient mutant pen2-2, is more sensitive to the mycotoxin fumonisin B1 (FB1) than wild-type Col-0, and the elevated expression of isozyme TGG1, but not of PEN2, correlates with the decrease in indole glucosinolate (IGS), TGG-dependent IGS hydrolysis is involved in FB1-induced programmed cell death (PCD)
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malfunction
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the tgg1, single and tgg1 tgg2 double mutants show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
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metabolism
metabolism of tryptophan-derived indole glucosinolate (IGS), camalexin and indol-3-acetic acid (IAA) as well as methioninederived aliphatic glucosinolate (AGS) in Arabidopsis thaliana involving the myrosinase enzymes TGG1 and PEN2, overview
metabolism
metabolism of tryptophan-derived indole glucosinolate (IGS), camalexin and indole-3-acetic acid (IAA) as well as methioninederived aliphatic glucosinolate (AGS) in Arabidopsis thaliana involving the myrosinase enzymes TGG1 and PEN2, overview. FB1-induced biosynthesis of glucosinolates. FB1 treatment triggers not only biosynthesis but also hydrolysis of IGS
metabolism
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regulatory effects of abscisic acid (ABA) on glucosinolate contents and isothiocyanate formation of cabbage sprouts, overview. Cotyledon of ABA-treated sprouts represent the highest content of glucosinolates, which is 2.65 and 2.34fold of that in hypocotyl and root, respectively. The content of glucosinolates in cotyledon represents 67.52-78.71% of the total glucosinolates in cabbage sprouts, while hypocotyl and root represent 8.34-13.79% and 12.69-20.81%, respectively. Moreover, ABA increases the relative percentage of glucosinolates in hypocotyl, and fluridon increases the relative percentage of glucosinolates in root
metabolism
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metabolism of tryptophan-derived indole glucosinolate (IGS), camalexin and indole-3-acetic acid (IAA) as well as methioninederived aliphatic glucosinolate (AGS) in Arabidopsis thaliana involving the myrosinase enzymes TGG1 and PEN2, overview. FB1-induced biosynthesis of glucosinolates. FB1 treatment triggers not only biosynthesis but also hydrolysis of IGS
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metabolism
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metabolism of tryptophan-derived indole glucosinolate (IGS), camalexin and indol-3-acetic acid (IAA) as well as methioninederived aliphatic glucosinolate (AGS) in Arabidopsis thaliana involving the myrosinase enzymes TGG1 and PEN2, overview
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physiological function
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enzyme reaction products of glucosinolate hydrolysis, especially sulforaphane, i.e. 1-isothiocyanato-4-methylsulfinyl butane, are involved in the anticarcinogenic effects of broccoli
physiological function
myrosinase and its substrates, the glucosinolates, are part of the plant's defense system
physiological function
myrosinase TGG1 redundantly functions in abscisic acid and methyl jasmonate signaling in guard cells
physiological function
myrosinase TGG2 redundantly functions in abscisic acid and methyl jasmonate signaling in guard cells
physiological function
myrosinase-catalysed release of toxic and bioactive compounds such as isothiocyanates, upon activation or tissue damage, play a role in the plant defense system
physiological function
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the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
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the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
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the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
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Brassica napus contains a defence system known as the glucosinolate-myrosinase system or the mustard oil bomb. The mustard oil bomb which includes myrosinase and glucosinolates is triggered by abiotic and biotic stress, resulting in the formation of toxic products such as nitriles and isothiocyanates
physiological function
-
myrosinase activity is required for the formation of characteristic adducts in the endogenous DNA after homogenizing Brassicales plants
physiological function
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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
-
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
-
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
-
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
-
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
-
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
adult beetles selectively accumulate glucosinolates from their food Brassicaceae plants to up to 1.75% of their body weight and express their own myrosinase, GC-MS analyses, overview. Glucosinolates of different classes accumulate at divergent rates
physiological function
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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
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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-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-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-hydroxysulfate) precursors
physiological function
Brassicaceae, including Arabidopsis thaliana and Brassica crop species comprise the glucosinolate-myrosinase system, in which myrosinase thioglucosidase (TGG) catalyses glucosinolate breakdown into various biologically active molecules upon tissue disruption or insect attac. The glucosinolate-myrosinase system represents a chemical-based plant defence system. A close association between chemical defence systems and physical defence barriers, represented by the cuticle, exists
physiological function
classical TGG-dependent hydrolysis of indole glucosinolate (IGS) restricts FB1-induced programmed cell death (PCD). Mycotoxin fumonisin B1 (FB1) causes the accumulation of reactive oxygen species (ROS) which then leads to PCD in Arabidopsis thaliana. FB1-induced biosynthesis of glucosinolates. FB1 treatment triggers not only biosynthesis but also hydrolysis of IGS
physiological function
glucoraphanin from broccoli and its sprouts and seeds is a water soluble and relatively inert precursor of sulforaphane, the reactive isothiocyanate that is formed by the activity of myrosinase and potently inhibits neoplastic cellular processes. It prevents a number of disease states in humans
physiological function
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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
-
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
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
-
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
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
-
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
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
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
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
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
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
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
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
-
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
-
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
-
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
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
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. Myrosinase binding proteins and/or myrosinase-associated proteins are critical parts of the myrosinase complex, and are required for full enzyme activity
physiological function
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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
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
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
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
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
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. A clear genotype and plant developmental stage-dependence is associated to the correspondence between glucosinolates content and myrosinase activity in Thellungiella
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. Other proteins can interact with the myrosinase forming myrosinase-binding proteins (MBPs) and myrosinase associated proteins (MyAP). They have been identified as complexes contributing to the plant defense system in different Brassica species such as Brassica napus or Arabidopsis thaliana. Potential N-linked sugar binding sites of the myrosinase are implicated in the binding of MBP
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, overview. Other proteins can interact with the myrosinase forming myrosinase-binding proteins (MBPs) and myrosinase associated proteins (MyAP). They have been identified as complexes contributing to the plant defense system in different Brassica species such as Brassica napus or Arabidopsis thaliana. Three-dimensional analysis of the structure of this complex shows that the protein does not show affinity for sugar structures to link N-glycan, but a weak affinity for starch or glycolipid involved the lectin activity of the MBP family in the interaction between the myrosinase complex and other molecules. Important role of the myrosinase activity in guard cells of Arabidopsis plants. Water stress increases abscisic acid levels that enhance glucosinolates delivery from the vacuole, myrosinase activity or its substrate affinity. Hydrolyzed products of glucosinolates may induce inward K+-channel activity resulting in stomata closure
physiological function
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PYK10, the most abundant beta-glucosidase in Arabidopsis thaliana root endoplasmic reticulum (ER) bodies, hydrolyzes indole glucosinolates (IGs) in addition to the previously reported in vitro substrate scopolin. PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in Arabidopsis thaliana. Variation of the myrosinase-glucosinolate system exists within individual plants. The co-expressed gene cluster of PYK10 is enriched in genes required for the production of glucosinolates. Glucosinolates are in planta substrates for PYK10 that are tightly linked to the physiological functions of ER bodies. ER bodies are potentially engaged in plant-microbe interactions via indole glucosinolate metabolism and in abiotic stress responses via coumarin metabolism
physiological function
-
the cabbage stem flea beetle (Psylliodes chrysocephala) is a key pest of oilseed rape in Europe, and is specialized to feed on Brassicaceae plants armed with the glucosinolate-myrosinase defense system, e.g. Brassica rapa, Sinapis alba, or Arabidopsis thaliana. Upon tissue damage, the beta-thioglucosidase enzyme myrosinase hydrolyzes glucosinolates (GLS) to form toxic isothiocyanates (ITCs) which deter non-adapted herbivores. Feeding damage usually causes rapid enzymatic breakdown of GLS to toxic ITCs in the insect gut. Metabolites derived from 4-methylsulfinylbutyl isothiocyanate in feces of Psylloides chrysocephala, feces extracts of beetles that have fed on detached leaves of different Arabidopsis thaliana genotypes, overview. Psylloides chrysocephala partially detoxifies ITCs by conjugation with glutathione via the conserved mercapturic acid pathway, and can largely prevent GLS hydrolysis in ingested plant tissue by sequestration and desulfation. Psylloides chrysocephala selectively sequester GLS from their host plants and store these throughout their life cycle. In addition, Psylloides chrysocephala metabolizes GLS to desulfo-GLS, which implies the evolution of GLS sulfatase activity in this specialist
physiological function
-
the enzyme is a redox-regulated isoform of myrosinase. Myrosinase is involved in the hydrolysis of glucosinolates to isothiocyanates, nitriles, and thiocyanates that are responsible for various ecological and health benefits. The thiol-regulated kinetic behavior of the myrosinase isozyme from Lepidium latifolium signifies the enzyme's strategy to fine-tune its activity in different redox environments, thus regulating its biological effects. A responsive glucosinolate-myrosinase system in this plant seems possible owing to its high glucosinolate content
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
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
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
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
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
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
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
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
-
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
-
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
-
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
-
physiological function
-
classical TGG-dependent hydrolysis of indole glucosinolate (IGS) restricts FB1-induced programmed cell death (PCD). Mycotoxin fumonisin B1 (FB1) causes the accumulation of reactive oxygen species (ROS) which then leads to PCD in Arabidopsis thaliana. FB1-induced biosynthesis of glucosinolates. FB1 treatment triggers not only biosynthesis but also hydrolysis of IGS
-
physiological function
-
Brassicaceae, including Arabidopsis thaliana and Brassica crop species comprise the glucosinolate-myrosinase system, in which myrosinase thioglucosidase (TGG) catalyses glucosinolate breakdown into various biologically active molecules upon tissue disruption or insect attac. The glucosinolate-myrosinase system represents a chemical-based plant defence system. A close association between chemical defence systems and physical defence barriers, represented by the cuticle, exists
-
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
-
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
-
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
-
physiological function
-
the enzyme is involved in the decomposition of glucosinolates produced by Armoracia rusticana roots to defend against enodphytic fungi. The detected minor glucosinolates include aliphatic (gluconapin, glucocochlearin), thiomethylalkyl (glucoiberin), and indolic (glucobrassicin) types as well
-
additional information
-
Brassicaceae myrosinases are glycoproteins that have multiple forms with different molecular masses, number of subunits, subunit size and carbohydrate content
additional information
-
decreased sulforaphene concentration and reduced myrosinase activity of radish root during cold storage. Postharvest conditions, even with storage of the radish roots at cold temperature, may play a key role in either the maintenance of SFE or myrosinase activity
additional information
the enzyme is sensitive to endoglycosidase digestion
additional information
the enzyme is sensitive to endoglycosidase digestion
additional information
analysis of substrate recognition and mechanism of reaction
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
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
additional information
-
brown mustard (Brasiica juncea) has higher myrosinase activity than black (Brassica nigra) and yellow mustard (Sinapis alba)
additional information
-
brown mustard (Brasiica juncea) has higher myrosinase activity than black (Brassica nigra) and yellow mustard (Sinapis alba)
additional information
-
brown mustard (Brasiica juncea) has higher myrosinase activity than black (Brassica nigra) and yellow mustard (Sinapis alba)
additional information
-
glucosinolates (Gls) total contents in tubers are within the 0.0049-0.0542 mmol/g dry matter range, of which 96-99% corresponded to glucoaubrietin, i.e. 4-methoxybenzyl glucosinolate. Other less abundant Gls are glucotropaeolin and tentatively two isomers of hydroxybenzyl Gls. Identification and quantification of Gls in the different cultivars, mass spectrometric analysis
additional information
-
redox-regulated, the reduced form is more active
additional information
the cyp79B2 cyp79B3 mutant, which has a greatly reduced level of indole glucosinolates, is more sensitive to mycotoxin fumonisin B1 (FB1)
additional information
the cyp79B2 cyp79B3 mutant, which has a greatly reduced level of indole glucosinolates, is more sensitive to mycotoxin fumonisin B1 (FB1)
additional information
-
three-dimensional analysis of the structure of the enzyme-myrosinase-binding protein (MBP) complex in Arabidopsis thaliana shows that the protein does not show affinity for sugar structures to link N-glycan, but a weak affinity for starch or glycolipid involved the lectin activity of the MBP family in the interaction between the myrosinase complex and other molecules
additional information
-
the cyp79B2 cyp79B3 mutant, which has a greatly reduced level of indole glucosinolates, is more sensitive to mycotoxin fumonisin B1 (FB1)
-
additional information
-
the enzyme is sensitive to endoglycosidase digestion
-
Show AA Sequence and Transmembrane Helices (979 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
124000
126000
130000
140000
140000 - 200000
150000
156000
157000
160000
188000
270000 - 350000
-
enzyme forms complexes of different molecular weight with several protein subunits
30000
Sinapis sp.
-
x * 30000, enzyme consists of at least 4 subunits, myrosinase F-IIB, SDS-PAGE
40000
Sinapis sp.
-
x * 40000, enzyme consists of at least 4 subunits, myrosinase F-IA, F-IB and F-IIA, SDS-PAGE
470000
500000 - 600000
-
enzyme forms complexes of different molecular weight with several protein subunits
580000
59500
x * 70000, recombinant TGG2, SDS-PAGE, x * 59500, about, TGG2 sequence calculation
59700
x * 59700, calculated for mature protein, x * 65000, SDS-PAGE
61000
61100
x * 75000, glycosylated enzyme TGG1, SDS-PAGE, x * 61100, deglycosylated enzyme TGG1, SDS-PAGE
62000
62700
x * 63000, glycosylated enzyme TGG2, SDS-PAGE, x * 62700, deglycosylated enzyme TGG2, SDS-PAGE
63000
x * 63000, glycosylated enzyme TGG2, SDS-PAGE, x * 62700, deglycosylated enzyme TGG2, SDS-PAGE
65000
70000
75000
140000 - 200000
-
enzyme forms complexes of different molecular weight with several protein subunits
140000 - 200000
-
enzyme forms complexes of different molecular weight with several protein subunits
65000
x * 59700, calculated for mature protein, x * 65000, SDS-PAGE
65000
-
x * 65000, SDS-PAGE. Immunoblot analysis reveals the major bands of myrosinase polypeptide classes (denoted as 65, 70, and 75 kDa) in wild type samples of seeds
70000
x * 70000, recombinant TGG2, SDS-PAGE, x * 59500, about, TGG2 sequence calculation
70000
-
x * 70000, SDS-PAGE. Immunoblot analysis reveals the major bands of myrosinase polypeptide classes (denoted as 65, 70, and 75 kDa) in wild type samples of seeds
75000
-
x * 75000, SDS-PAGE. Immunoblot analysis reveals the major bands of myrosinase polypeptide classes (denoted as 65, 70, and 75 kDa) in wild type samples of seeds
75000
x * 75000, glycosylated enzyme TGG1, SDS-PAGE, x * 61100, deglycosylated enzyme TGG1, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
trimer
additional information
?
x * 63000, glycosylated enzyme TGG2, SDS-PAGE, x * 62700, deglycosylated enzyme TGG2, SDS-PAGE
?
x * 75000, glycosylated enzyme TGG1, SDS-PAGE, x * 61100, deglycosylated enzyme TGG1, SDS-PAGE
?
-
enzyme consists of complexes of several subunits with molecular weights between 10000 Da and 110000 Da, SDS-PAGE
?
-
enzyme consists of complexes of several subunits with molecular weights between 10000 Da and 110000 Da, SDS-PAGE
?
-
x * 65000, SDS-PAGE. Immunoblot analysis reveals the major bands of myrosinase polypeptide classes (denoted as 65, 70, and 75 kDa) in wild type samples of seeds
?
-
x * 70000, SDS-PAGE. Immunoblot analysis reveals the major bands of myrosinase polypeptide classes (denoted as 65, 70, and 75 kDa) in wild type samples of seeds
?
-
x * 75000, SDS-PAGE. Immunoblot analysis reveals the major bands of myrosinase polypeptide classes (denoted as 65, 70, and 75 kDa) in wild type samples of seeds
?
-
enzyme consists of complexes of several subunits with molecular weights between 10000 Da and 110000 Da, SDS-PAGE
?
x * 70000, recombinant TGG2, SDS-PAGE, x * 59500, about, TGG2 sequence calculation
?
-
enzyme consists of complexes of several subunits with molecular weights between 10000 Da and 110000 Da, SDS-PAGE
?
Sinapis sp.
-
x * 30000, enzyme consists of at least 4 subunits, myrosinase F-IIB, SDS-PAGE
?
Sinapis sp.
-
x * 40000, enzyme consists of at least 4 subunits, myrosinase F-IA, F-IB and F-IIA, SDS-PAGE
dimer
-
the enzyme protein folds into a (beta/alpha)8 barrel structure forming a glycosylated dimer stabilized by a Zn2+ ion
additional information
-
existence of different oligomeric states in different redox environments
additional information
the enzyme contains about 19% alpha-helix and 35% beta-sheets, the rest being conformationally aperiodic
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
all four potential N-glycosylation sites are subjected to glycosylation and are occupied by oligomannosidic structures with Man5GlcNAc2 as the main oligosaccharide, found on the majority of TGG1 glycopeptides. In addition, Man6GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2 are also present on several glycosylation sites, while on Asn108 the predominant peak corresponds to Man9Glc-NAc2. TGG2 N-glycans are not altered in the mvp1 mutant
glycoprotein
all nine potential N-glycosylation sites are subjected to glycosylation and are occupied by oligomannosidic structures with Man5GlcNAc2 as the main oligosaccharide, found on the majority of TGG1 glycopeptides. In addition, Man6GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2 are also present on several glycosylation sites, while on Asn108 the predominant peak corresponds to Man9Glc-NAc2. TGG1 from mns mutants displays incompletely processed oligomannosidic N-glycans, while TGG1 N-glycans are not altered in the mvp1 mutant
glycoprotein
deglycosylation under nondenaturing conditions has limited effect on TGG1 activity
glycoprotein
deglycosylation under nondenaturing conditions has no effect on TGG2 activity
glycoprotein
deglycosylation affects TGG1 activity
glycoprotein
deglycosylation does not affect TGG2 activity
glycoprotein
-
all nine potential N-glycosylation sites are subjected to glycosylation and are occupied by oligomannosidic structures with Man5GlcNAc2 as the main oligosaccharide, found on the majority of TGG1 glycopeptides. In addition, Man6GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2 are also present on several glycosylation sites, while on Asn108 the predominant peak corresponds to Man9Glc-NAc2. TGG1 from mns mutants displays incompletely processed oligomannosidic N-glycans, while TGG1 N-glycans are not altered in the mvp1 mutant
-
glycoprotein
-
all four potential N-glycosylation sites are subjected to glycosylation and are occupied by oligomannosidic structures with Man5GlcNAc2 as the main oligosaccharide, found on the majority of TGG1 glycopeptides. In addition, Man6GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2 are also present on several glycosylation sites, while on Asn108 the predominant peak corresponds to Man9Glc-NAc2. TGG2 N-glycans are not altered in the mvp1 mutant
-
glycoprotein
the enzyme ArMy2 possesses 5 putative N-glycosylation sites, degree of glycosylation is about 19%
glycoprotein
-
N-linked glycosylation sites, myrosinase I contains 18% carbohydrate
glycoprotein
-
myrosinase C1 contains 9.3% carbohydrate, myrosinase C2 contains 15.2% carbohydrate, myrosinase C3 contains 17.4% carbohydrate
glycoprotein
-
size differences between the different myrosinases are mainly due to differences in glycosylation
glycoprotein
-
contains fucose, mannose and N-acetylglucosamine. Enzyme form Ca contains 18.9% carbohydrate, enzyme form Cb contains 11.7% carbohydrate, enzyme form Cc contains 9.6% carbohydrate
glycoprotein
-
N-linked sugar binding sites of the myrosinase are implicated in the binding of myrosinase-binding proteins (MBPs)
glycoprotein
-
carbohydrate chains distributed over the surface of the enzyme
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
glycoprotein
Sinapis sp.
-
hexose content of enzyme F-IA is 15.8%, hexose content of enzyme F-IB is 17.8%, hexose content of enzyme F-IIA is 22.5%, hexose content of enzyme F-IIB is 8.6%
proteolytic modification
sequence contains a signal peptide of 1900 Da
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D175A
-
generated mutant, D175A mutant shows significant activity toward pNP-S-GlcNAc
additional information
additional information
-
construction of isoform TGG1 and TGG2 single and double mutants. Glucosinolate breakdown in leaves of single mutant plants is comparable to wild-type, whereas the double mutant exhibits no catalytic activity in vitro and dmage-induce breakdown of endogenous glucosinolates is apparently absent for aliphatic and greatly slowed down for indole glucosinolates. Mature leaves of mutants have increased glucosinolate levels, but developmental decreases in glucosinolate content during senescence and germination are unaffected. Insect herbivores vary in their respones to mutants. Weight gain of Trichoplusia ni and Manduca sexta is significantly increased upon feeding with mutant leaves, while reproduction of Myzus persicae and Brevicoryne brassica is unaffected
additional information
construction of isozyme mutants, tgg1-3, tgg2-1, and tgg1-3/tgg2-1. Abscisic acid, methyl jasmonate, and H2O2 induce stomatal closure in wild type, tgg1-3 and tgg2-1, but fail to induce stomatal closure in tgg1-3 tgg2-1. All mutants and wild-type show Ca2+-induced stomatal closure and abscisic acid-induced reactive oxygen species production
additional information
construction of isozyme mutants, tgg1-3, tgg2-1, and tgg1-3/tgg2-1. Abscisic acid, methyl jasmonate, and H2O2 induce stomatal closure in wild type, tgg1-3 and tgg2-1, but fail to induce stomatal closure in tgg1-3 tgg2-1. All mutants and wild-type show Ca2+-induced stomatal closure and abscisic acid-induced reactive oxygen species production
additional information
generation of tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg2 single mutant, the pavement cells appear bigger compared to wild-type, flattened and show an irregular jigsaw puzzle shape. Stomata in the tgg2 single mutant are also relatively bigger than the wild-type, and the stomatal aperture is mostly fully open. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
generation of tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg2 single mutant, the pavement cells appear bigger compared to wild-type, flattened and show an irregular jigsaw puzzle shape. Stomata in the tgg2 single mutant are also relatively bigger than the wild-type, and the stomatal aperture is mostly fully open. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
generation of tgg1, single and tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg1 single mutant, the pavement cells are bigger in size, but still showing a regular jigsaw puzzle shape as in the wild-type. The stomata in the tgg1 single mutant also appear bigger. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
generation of tgg1, single and tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg1 single mutant, the pavement cells are bigger in size, but still showing a regular jigsaw puzzle shape as in the wild-type. The stomata in the tgg1 single mutant also appear bigger. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
the costructed tgg1 tgg2 double mutant, which has greatly reduced TGG activity, shows more severe lesion formation and cell death symptoms than Col-0. Mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
the costructed tgg1 tgg2 double mutant, which has greatly reduced TGG activity, shows more severe lesion formation and cell death symptoms than Col-0. Mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
-
mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
-
additional information
-
the costructed tgg1 tgg2 double mutant, which has greatly reduced TGG activity, shows more severe lesion formation and cell death symptoms than Col-0. Mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
-
additional information
-
generation of tgg1, single and tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg1 single mutant, the pavement cells are bigger in size, but still showing a regular jigsaw puzzle shape as in the wild-type. The stomata in the tgg1 single mutant also appear bigger. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
-
additional information
-
generation of tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg2 single mutant, the pavement cells appear bigger compared to wild-type, flattened and show an irregular jigsaw puzzle shape. Stomata in the tgg2 single mutant are also relatively bigger than the wild-type, and the stomatal aperture is mostly fully open. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
-
additional information
genetic modification of Brassica napus plants to remove myrosinase-storing idioblasts to eliminate release of cell toxic reaction products and metabolites. Construction of transgenic plants ectopically expressing barnase, a ribonuclease, using a seed myrosin cell-specific Myr1.Bn1 promoter, which is lethal for the embryo. Co-expressing barnase under the control of the Myr1.Bn1 promoter with the barnase inhibitor, barstar, under the control of the cauliflower mosaic virus 35S promoter enables a selective and controlled death of myrosin cells without affecting plant viability. Transgenic plants with myrosin defence cells show negligible production of glucosinolate hydrolysis products and altered epithiospecifier protein profile and glucosinolate levels, overview. Glucosinolate profiles of wild-type and mutant plants, overview
additional information
-
genetic modification of Brassica napus plants to remove myrosinase-storing idioblasts to eliminate release of cell toxic reaction products and metabolites. Construction of transgenic plants ectopically expressing barnase, a ribonuclease, using a seed myrosin cell-specific Myr1.Bn1 promoter, which is lethal for the embryo. Co-expressing barnase under the control of the Myr1.Bn1 promoter with the barnase inhibitor, barstar, under the control of the cauliflower mosaic virus 35S promoter enables a selective and controlled death of myrosin cells without affecting plant viability. Transgenic plants with myrosin defence cells show negligible production of glucosinolate hydrolysis products and altered epithiospecifier protein profile and glucosinolate levels, overview. Glucosinolate profiles of wild-type and mutant plants, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 10.3
the purified recombinant enzyme TGG1 retains more than 50% of their maximal activity in buffers with pH values ranging from 4.8 to 10.3
732658
4.8 - 11
the purified recombinant enzyme TGG1 retains more than 50% of their maximal activity in buffers with pH values ranging from 4.8 to 11.0
732658
5.5 - 8.5
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 80
4 - 55
40
40 - 70
-
enzyme inactivation rate estimated by using the first-order inactivation model. A reversible step in MYR inactivation is excluded
50
60
70
70 - 80
95
additional information
30
-
myrosinase of the mutant strain NR463U4 retains activity 3.5times longer than wild-type enzyme
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
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
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
4 - 55
purified recombinant enzyme TGG1, retains over 70% activity at temperatures between 4°C and 55°C for 30 min
4 - 55
purified recombinant enzyme TGG2, retains over 70% activity at temperatures between 4°C and 55°C for 30 min
40
-
30 min, 30 min, 5% loss of activity of the enzyme from red cabbage, 15% loss of activity of the enzyme from white cabbage
60
-
30 min, enzyme from red cabbage is stable, enzyme from white cabbage loses about 60% of its activity
70 - 80
-
10 min, 35% activity remaining at normal pressure, 65% activity at 300 MPa, inactivation at 80°C
70 - 80
-
10 min, 59% activity remaining at normal pressure, 80% activity at 300 MPa, inactivation at 80°C
95
purified recombinant enzyme, 10 min, pH 5.8, inactivation
additional information
-
study on kinetics of thermal enzyme inactivation in broccoli juice at elevated pressure for optimization of health effects. Pressure has an antagonistic effect on thermal inactivation at 50°C and above. Isothiocyanates formed by enzyme are relatively thermolabile and pressure stable
additional information
low pressure retards thermal inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extrinsic factors, during postharvest and food processing such as pH, temperature, and pressure
-
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
-
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 enzyme is stable only in presence of 2-mercapethanol and ascorbic acid
-
the extent of enzyme inactivation increases with pressure (600-800 MPa) and temperature (30-70C) for all the mustard seeds. At combinations of lower pressures (200-400 MPa) and high temperatures (60-80C), there is less inactivation. For example, application of 300 MPa and 70C 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 (70C, 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%
-
unstable after extraction from mycelium, considerably inactivated during dialysis and precipitation process with ammonium sulfate, stabilized by 10 mM 2-mercaptoethanol and 1 mM ascorbic acid
-
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
-
the extent of enzyme inactivation increases with pressure (600-800 MPa) and temperature (30-70C) for all the mustard seeds. At combinations of lower pressures (200-400 MPa) and high temperatures (60-80C), there is less inactivation. For example, application of 300 MPa and 70C 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 (70C, 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 extent of enzyme inactivation increases with pressure (600-800 MPa) and temperature (30-70C) for all the mustard seeds. At combinations of lower pressures (200-400 MPa) and high temperatures (60-80C), there is less inactivation. For example, application of 300 MPa and 70C 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 (70C, 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 extent of enzyme inactivation increases with pressure (600-800 MPa) and temperature (30-70C) for all the mustard seeds. At combinations of lower pressures (200-400 MPa) and high temperatures (60-80C), there is less inactivation. For example, application of 300 MPa and 70C 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 (70C, 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
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation by methylene blue
Sinapis sp.
-
208568
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
81% decreased sulforaphene concentration and 40% reduced myrosinase activity of radish root during cold storage at 0°C for 4 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Con-A-Sepharose column chromatography, SP-Sepharose column chromatography, and Superdex 200 gel filtration
-
fast and gentle procedure for the isolation of enzyme complex from seed
native enzyme 1318fold from broccoli by ammonium sulfate fractionation followed by concanavalin A affinity chromatography, with an intermediate dialysis step
-
native enzyme 69.3fold from leaves to homogeneity by ammonium sulfate fractionation, ultrafiltration, concanavalin A affinity chromatography, and gel filtation
-
native enzyme by three chromatographic step involving gel filtration
native enzyme from freeze-dried 3-day-old broccoli sprouts 5.51fold for mobile enzyme fraction, and 14.6fold from counter-current chromatography
-
native enzyme from freeze-dried 7-day-old daikon sprouts 3.45fold for mobile enzyme fraction, and 22.9fold from counter-current chromatography
-
native enzyme from freeze-dried leaves 2.20fold for mobile enzyme fraction, and 61.5fold from counter-current chromatography
-
native enzyme from inflorescences by ammonium sulfate fractionation, dialysis, concanavalin A affinity chromatography, and gel filtration
native enzyme from powder of freeze-dried seedlings of Brussels sprouts, by solubilization, and concanavalin A affinity chromatography with elution by methyl-alpha-D-mannopyranoside
native enzyme from root by ammonium sulfate fractionation and gel filtration
-
native enzyme from roots
native enzyme from seeds
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 3-day-old sprouts 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
rapid isolation of catalytically active plant myrosinase from 7-day-old sprouts 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
rapid isolation of catalytically active plant myrosinase from fresh leaves 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
-
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
-
recombinant His-tagged root isozymes TGG4 and TGG5 and His-tagged leaf isozyme TGG1 from Pichia pastoris by nickel affinity chromatography to homogeneity
-
recombinant His6-tagged ArMy2 from Pichia pastoris by nickel affinity chromatography
TGG1 51.9fold from from T-DNA insertion lines of Arabidopsis using lectin affinity and anion exchange chromatography
TGG2 84.2fold from from T-DNA insertion lines of Arabidopsis using lectin affinity and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination and analysis, combining proteomics and transcriptomics analysis, phylogenetic analysis
expression of myrosinase MYR1 in Saccharomyces cerevisiae. The recombinant enzyme is enzymatically active which shows that the enzyme, which in plant is complex bound with myrosinase-binding proteins and myrosinase-associated proteins, is functional in its free form. Expression of the enzyme is transient and the growth of the yeast cells is significantly reduced during the period of expression of myrosinase
-
gene pTGG2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Pichia pastoris
gene tgg1, exxpression of recombinant TGG1, sequence comparisons
gene tgg2, recombinant expression of TGG2, sequence comparisons
myrosinase is encoded by two different families of genes: MA and MB. The MA type myrosinases are encoded by approximately 4 genes, the MB type myrosinases are encoded by more than 10 genes
-
myrosinases are encoded by a multigene family consisting of two subgroups. Cloning and sequencing of the two nuclear genes, Myr1.Mn1 and Myr2.Mn1, representing each of these two subgroups
-
overexpression of His-tagged root isozymes TGG4 and TGG5 and His-tagged leaf isozyme TGG1 in Pichia pastoris
-
overexpression of nitrile-specifier protein 2, NSP2, in transgenic Arabidopsis thaliana plants leading to increased nitrile production
-
phylogenetic analysis and tree, recombinant expression of wild-type and mutant enzymes
-
phylogenetic tree, recombinant overexpression of His6-tagged ArMy2 in Pichia pastoris
recombinant gene Myr1.Bn1, expressionin transgenic Brassica napus plants
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at harvest, myrosinase activity considerably increases in the yellow and red hypocotyls compared to the black ecotype
-
cabbage cultivars grown in the northern area of Spain with low temperatures and radiation lead to higher mean values of myrosinase activity
-
in crushed heat-treated leaves of Nakajimana (70°C for 30 s), myrosinase activity increases 4fold
-
in the halophyte Thellungiella salt stress enhances myrosinase activity during the vegetative phase in the rosette leaves, with no relation between the changes in glucosinolate content and myrosinase activity in the roots
-
inhibition of the glucosinolate-myrosinase system is observed when oxalic acid with a pH of 3.0 or below is used
-
myrosinase activity in leaves of significantly decreases when Nakajimana leaves are heated over 70°C
-
significant losses of myrosinase activity are observed during the post-harvest drying stage
-
TGG1 transcript levels are higher in leaves of mns1 mns2 mns3 plants
the cultivars with the highest vitamin C content have the lowest myrosinase activity
-
the enzyme is induced by herbivore attack, e.g. by Pieris rapae, the kind of herbivore determines the product formed from glucosinolates, overview
the enzyme is induced by herbovore attack, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by mechanical wounding, and by herbivore attack, e.g. by Pieris brassicae or Pieris rapae, but not by Delia radicum, the kind of herbivore determines the product formed from glucosinolates, overview
-
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
-
the enzyme is induced by mechanical wounding, phytohormone jasmonic acid, and by herbivore attack, e.g. by Phaedon cochleariae, but not by Plutella xylostella, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by mechanical wounding, phytohormones jasmonic acid and salicylate, and by herbivore attack, e.g. by Delia floralis, Phyllotreta cruciferae, Plutella xylostella, and Psylliodes chrysocephala, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by phytohormone jasmonic acid and methyljasmonic acid, and by herbivore attack, e.g. by Brevicoryne brassicae, Myzus persicae, Spodoptera exigua, and Plutella xylostella, but not by Pieris rapae, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by phytohormone jasmonic acid and methyljasmonic acid, by mechanical wounding, and by herbivore attack, e.g. by Athalia rosae, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by phytohormone jasmonic acid, overview
-
the enzyme is induced by phytohormones jasmonic acid and salicylate, and by herbivore attack, e.g. by Plutella xylostella, Myzus persicae, and Pieris rapae, but not by nematodes and earthworms or Delia radicum and Delia floralis, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by phytohormones jasmonic acid and salicylate, overview
-
the enzyme is induced by phytohormones, such as jasmonic acid and salicylate, overview
-
the enzyme is not induced by herbivore attack with Pieris rapae, overview
-
the glucosinolate-myrosinase system is activated in the presence of oxalic acid at pH 4.0-7.0
-
water stress increases abscisic acid levels that enhanced glucosinolates delivery from the vacuole, myrosinase activity or its substrate affinity
-
TGG1 transcript levels are higher in leaves of mns1 mns2 mns3 plants
TGG1 transcript levels are higher in leaves of mns1 mns2 mns3 plants
-
-
the enzyme is induced by herbivore attack, e.g. by Pieris rapae, the kind of herbivore determines the product formed from glucosinolates, overview
-
the enzyme is induced by herbivore attack, e.g. by Pieris rapae, the kind of herbivore determines the product formed from glucosinolates, overview
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biotechnology
-
Aspergillus sp. NR463U4 maintains constant myrosinase production for 8 months. High production and prolonged stability of myrosinase demonstrates that this mutant could be a candidate for industrial application
nutrition
pharmacology
sulforaphane, the reactive isothiocyanate that potently inhibits neoplastic cellular processes and prevents a number of disease states in humans, is difficult to deliver in an enriched and stable form for purposes of direct human consumption. Evaluation of the bioavailability of sulforaphane, either by direct administration of glucoraphanin (a glucosinolate, or beta-thioglucoside-N-hydroxysulfate), or by co-administering glucoraphanin and the enzyme myrosinase to catalyze its conversion to sulforaphane at economic, reproducible and sustainable yields, overview. Following administration of glucoraphanin in a commercially prepared dietary supplement to a small number of human volunteers, the volunteers have equivalent output of sulforaphane metabolites in their urine to that which they produce when given an equimolar dose of glucoraphanin in a simple boiled and lyophilized extract of broccoli sprouts. Furthermore, when either broccoli sprouts or seeds are administered directly to subjects without prior extraction and consequent inactivation of endogenous myrosinase, regardless of the delivery matrix or dose, the sulforaphane in those preparations is 3 to 4fold more bioavailable than sulforaphane from glucoraphanin delivered without active plant myrosinase
agriculture
-
larvae of the sawfly Athalia rosae are highly tolerant to variations in the glucosinolate-myrosinase system of its host Brassica juncea. In plants showing high levels of glucosinolate or of enzyme activity, a significant decrease is observed upon treatment with the larvae, whereas levels of insoluble myrosinases coverge in plant lines with high and low level of activity after feeding of larvae
agriculture
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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
analysis
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micellar electrokinetic capillary chromatography method for monitoring the myrosinase catalyzed hydrolysis of 2-hydroxy substituted glucosinolates and formation of the corresponding oxazolidine-2-thiones and nitriles. Method has a detection limit of 0.04 mM and a limit of quantification of 0.2 mM and 0.3 mM for the glucosibarin-derived oxazolidine-2-thione and nitrile, respectivityl
analysis
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micellar electrokinetic capillary chromatography method for monitoring the myrosinase catalyzed hydrolysis of 2-hydroxy substituted glucosinolates and formation of the corresponding oxazolidine-2-thiones and nitriles. Method has a detection limit of 0.04 mM and a limit of quantification of 0.2 mM and 0.3 mM for the glucosibarin-derived oxazolidine-2-thione and nitrile, respectivityl
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nutrition
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in intact vegetable tissues, the enzyme is present in compartments separated from its substrate, the glucosinolates. The enzymatic hydrolysis can merely occur after cellular disruption. In this respect, processes such as cutting, cooking, freezing, or pressurizing of the vegetables will have large effect on the glucosinolate hydrolysis by myrosinase
nutrition
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study on kinetics of thermal enzyme inactivation in broccoli juice at elevated pressure for optimization of health effects. Pressure has an antagonistic effect on thermal inactivation at 50°C and above. Isothiocyanates formed by enzyme are relatively thermolabile and pressure stable
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Release 2023.1 (January 2023)
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