Information on EC 3.2.1.147 - thioglucosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.147
-
RECOMMENDED NAME
GeneOntology No.
thioglucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a thioglucoside + H2O = a sugar + a thiol
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-beta-glucosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of S-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glucosinolate breakdown
-
glucosinolate breakdown (via thiocyanate-forming protein)
-
Tryptophan metabolism
-
SYSTEMATIC NAME
IUBMB Comments
thioglucoside glucohydrolase
Has a wide specificity for thioglycosides.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-thioglucosidase
-
-
-
-
beta-thioglucosidase
-
-
beta-thioglucosidase
C9WCQ0
-
beta-thioglucosidase
-
-
beta-thioglucoside glucohydrolase
-
-
-
-
beta-thioglucoside glucohydrolase
-
-
beta-thioglucoside glucohydrolase
C9WCQ1
-
beta-thioglucoside glucohydrolase
-
-
beta-thioglucoside glucohydrolase,
-
-
EC 3.2.3.1
-
-
formerly
-
EC 3.2.3.1
-
formerly
glucosidase, thio-
-
-
-
-
MYR
Q9STD7
-
MYR1 myrosinase
-
-
myrosin
-
-
-
-
myrosinase
-
-
-
-
myrosinase
Q9STD7
-
myrosinase
-
-
myrosinase
-
-
myrosinase
C9WCQ0
-
myrosinase
C9WCQ1
-
myrosinase
-
-
myrosinase
-
-
myrosinase 1
P37702
-
myrosinase 2
Q9C5C2
-
myrosinase A
-
-
myrosinase B
-
-
sinigrase
-
-
-
-
sinigrinase
-
-
-
-
TGG1
C9WCQ0
-
TGG2
C9WCQ1
-
Thioglucosidase
-
-
-
-
thioglucoside glucohydrolase
-
-
thioglucoside glucohydrolase
-
-
thioglucoside glucohydrolase 1
-
-
thioglycosidase
-
-
thioglycosidase
-
-
glucosinolase
-
-
-
-
additional information
C9WCQ1
TGGs belong to the glycosyl hydrolase family 1
CAS REGISTRY NUMBER
COMMENTARY
9025-38-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoforms TGG1 and TGG2
-
-
Manually annotated by BRENDA team
isozyme TGG1; ecotype Columbia, Col-0, isozyme TGG1, gene tgg1
UniProt
Manually annotated by BRENDA team
isozyme TGG2; ecotype Columbia, Col-0, isozyme TGG2, gene tgg2
UniProt
Manually annotated by BRENDA team
six myrosinase genes, TGG1-TGG6
-
-
Manually annotated by BRENDA team
i.e. horseradish
-
-
Manually annotated by BRENDA team
AKU 3302
-
-
Manually annotated by BRENDA team
Aspergillus niger AKU 3302
AKU 3302
-
-
Manually annotated by BRENDA team
NR463, UV mutation induces myrosinase overproduction. strain NR463U4 produces 2.35 U/ml at 36 h of cultivation
-
-
Manually annotated by BRENDA team
slight activity
-
-
Manually annotated by BRENDA team
strain BRK-147-A
-
-
Manually annotated by BRENDA team
Brassica carinata BRK-147-A
strain BRK-147-A
-
-
Manually annotated by BRENDA team
Brassica caulorapa
i.e. kohlrabi
-
-
Manually annotated by BRENDA team
i.e. leaf mustard
-
-
Manually annotated by BRENDA team
i.e. yellow mustard
-
-
Manually annotated by BRENDA team
4 isoenzymes: RA, RB, RC and RD
-
-
Manually annotated by BRENDA team
cv. Bronowski; cv. Turret
-
-
Manually annotated by BRENDA team
cv. Bronowski; cv. Zephyr
-
-
Manually annotated by BRENDA team
cv. panter
-
-
Manually annotated by BRENDA team
i.e. oilseed rape
-
-
Manually annotated by BRENDA team
i.e. rape
-
-
Manually annotated by BRENDA team
L. cv. Bienvenu
-
-
Manually annotated by BRENDA team
myrosinase M65, M70 and M75
-
-
Manually annotated by BRENDA team
recombinant gene Myr1.Bn1; cv. Westar, gene Myr1
UniProt
Manually annotated by BRENDA team
L. cv. Italica
-
-
Manually annotated by BRENDA team
L. var. alboglabra, i.e. Chineses kale; L. var. botrytis, i.e. cauliflower; L. var. capitata L.; L. var. italica Plenca, i.e. broccoli
-
-
Manually annotated by BRENDA team
var. bullata subvar. gemmifera, i.e. Brussel sprouts
-
-
Manually annotated by BRENDA team
var. capitata L. f. alba DC i.e. white cabbage; var. gemmifera i.e. Brussel sprouts
-
-
Manually annotated by BRENDA team
cultivars Hinova, Megaton, Alfredo, Candela, and Bronco
-
-
Manually annotated by BRENDA team
cultivar Nakajimana
-
-
Manually annotated by BRENDA team
cv. Echo
-
-
Manually annotated by BRENDA team
ssp. rapifera
-
-
Manually annotated by BRENDA team
ssp. rapifera, i.e. turnip
-
-
Manually annotated by BRENDA team
subsp. rapa
-
-
Manually annotated by BRENDA team
var. chinensis
-
-
Manually annotated by BRENDA team
i.e. chineses mustard
-
-
Manually annotated by BRENDA team
i.e. Chineses cabbage
-
-
Manually annotated by BRENDA team
i.e. cabbage aphid
-
-
Manually annotated by BRENDA team
cultivar Solo II
UniProt
Manually annotated by BRENDA team
cv. Solo II, gene pTGG2
UniProt
Manually annotated by BRENDA team
strain 506
-
-
Manually annotated by BRENDA team
Enterobacter cloacae 506
strain 506
-
-
Manually annotated by BRENDA team
ecotype Shandong, China
-
-
Manually annotated by BRENDA team
Eutrema wasabi
-
-
-
Manually annotated by BRENDA team
i.e. wild candytuft; var. coronaria, i.e. candytuft
-
-
Manually annotated by BRENDA team
i.e. cress
-
-
Manually annotated by BRENDA team
Paracolobactrum aerogenoides
-
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
3 isoenzymes: SA, SB and SC
-
-
Manually annotated by BRENDA team
i.e. white mustard
-
-
Manually annotated by BRENDA team
white mustard
-
-
Manually annotated by BRENDA team
Sinapis sp.
-
-
-
Manually annotated by BRENDA team
Sinapis sp.
myrosinase F-IA, D-IB, F-IIA and F-IIB
-
-
Manually annotated by BRENDA team
strain OTG1
-
-
Manually annotated by BRENDA team
Sphingobacterium sp. OTG1
strain OTG1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
physiological function
-
myrosinase and its substrates, the glucosinolates, are part of the plant's defense system
physiological function
-
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
Q9STD7
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
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
P37702, Q9C5C2
myrosinase TGG1 redundantly functions in abscisic acid and methyl jasmonate signaling in guard cells; myrosinase TGG2 redundantly functions in abscisic acid and methyl jasmonate signaling in guard cells
physiological function
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2-hydroxy-2-phenylethylglucosinolate + H2O
D-glucose + ?
show the reaction diagram
Brassica carinata, Brassica carinata BRK-147-A
-
i.e. glucosibarin
-
-
?
(2S)-2-hydroxy-3-butenyl glucosinolate + H2O
D-glucose +
show the reaction diagram
-
i.e. epi-progoitrin
presence of endogenous epithiospecifier protein directs the reaction toward formation of an epithionitrile
-
?
(R)-4-methylsulfinylbutyl glucosinolate + H2O
?
show the reaction diagram
-
i.e. glucoraphanin or GRP
-
-
?
2-(4-hydroxyphenyl)ethylglucosinolate + H2O
D-glucose + 4-(2-carboxy-1-hydroxyethyl)phenyl sulfate
show the reaction diagram
-
-
-
-
?
2-(4-methoxyphenyl)ethylglucosinolate + H2O
D-glucose + 4-(2-cyano-1-hydroxyethyl)phenyl sulfate + 4-(2-cyanoethyl)phenyl sulfate
show the reaction diagram
-
-
-
-
?
2-hydroxybut-3-enylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
2-phenylethylglucosinolate + H2O
2-phenylethyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
2-propenylglucosinolate + H2O
2-propenyl-isothiocyanate + D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
3-butenylglucosinolate + H2O
3-butenyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
3-deoxyglucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
3-methylthiopropylglucosinolate + H2O
3-methylthiopropyl-isothiocyanate + D-D-glucose
show the reaction diagram
-
-
-
-
?
4-(methylsulfinyl)butyl glucosinolate + H2O
D-glucose + ?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
4-deoxyglucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
4-hydroxybenzylglucosinolate + H2O
D-glucose + 4-hydroxyphenylacetamide sulfate
show the reaction diagram
-
-
-
-
?
4-hydroxybenzylglucosinolate + H2O
D-glucose + 4-hydroxyphenylacetonitrile sulfate
show the reaction diagram
-
-
-
-
?
4-methylsulfinylbutylglucosinolate + H2O
?
show the reaction diagram
-
-
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-methylsulfinylbutylglucosinolate + H2O
4-methylsulfinylbutyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
4-methylthiobutylglucosinolate + H2O
?
show the reaction diagram
-
-
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
4-methylthiobutyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl 2-acetamido-2-deoxy-1-thio-beta-D-glucopyranoside + H2O
4-nitrobenzenethiol + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl 2-acetamido-2-deoxy-1-thio-beta-D-glucopyranoside + H2O
4-nitrobenzenethiol + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
show the reaction diagram
C9WCQ0, -
-
-
-
?
4-pentenylglucosinolate + H2O
4-pentenyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
5-methylthiopentylglucosinolate + H2O
5-methylthiopentyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
6-deoxyglucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
6-methylthiohexylglucosinolate + H2O
6-methylthiohexyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
7-methylthioheptylglucosinolate + H2O
7-methylthioheptyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
benzylglucosinolate + H2O
?
show the reaction diagram
-
-
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
show the reaction diagram
-
nitrile-specifier proteins, especially nitrile-specifier protein 2, NSP2, in conjunction with myrosinase enable the enzyme to generate nitriles, overview
-
-
?
benzylglucosinolate + H2O
D-glucose + hippuric acid
show the reaction diagram
-
-
-
-
?
epi-progoitrin + H2O
?
show the reaction diagram
-
-
-
-
?
epi-progoitrin + H2O
?
show the reaction diagram
-
i.e. 2(S)-2-hydroxy-3-butenyl glucosinolate
-
-
?
glucoapparin + H2O
?
show the reaction diagram
-
-
-
-
?
glucobrassicin + H2O
?
show the reaction diagram
-
-
-
-
?
glucocheirolin + H2O
?
show the reaction diagram
-
-
-
-
?
gluconasturtiin + H2O
D-glucose + ?
show the reaction diagram
Brassica carinata, Brassica carinata BRK-147-A
-
-
-
-
?
glucoraphenin + H2O
?
show the reaction diagram
-
3.8% of the activity with epi-progoitrin
-
-
?
glucosinalbin + H2O
?
show the reaction diagram
-
-
-
-
?
glucosinalbin + H2O
?
show the reaction diagram
-
-
-
-
-
glucosinalbin + H2O
?
show the reaction diagram
-
-
-
-
?
glucosinalbin + H2O
?
show the reaction diagram
-
9.5% of the activity with epi-progoitrin
-
-
?
glucosinolate + H2O
isothiocyanate + thiocyanate + nitrile + epithionitrile + ?
show the reaction diagram
-
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
-
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
C9WCQ0, -
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
-
7.8% of the activity with epi-progoitrin
-
-
?
glucotropaeolin + H2O
D-glucose + ?
show the reaction diagram
Brassica carinata, Brassica carinata BRK-147-A
-
-
-
-
?
indol-3-ylmethyl glucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
nasturtin + H2O
?
show the reaction diagram
-
best substrate, i.e. 2-phenylethyl glucosinolate
-
-
?
neo-glucobrassicin + H2O
?
show the reaction diagram
-
-
-
-
?
p-hydroxybenzylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
p-hydroxybenzylglucosinolate + H2O
D-glucose + ?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
progoitrin + H2O
?
show the reaction diagram
-
-
-
-
?
progoitrin + H2O
?
show the reaction diagram
-
9.8% of the activity with epi-progoitrin
-
-
?
sinalbin + H2O
?
show the reaction diagram
-
i.e. 4-hydroxybenzyl glucosinolate
-
-
?
singrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
Paracolobactrum aerogenoides
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
Eutrema wasabi
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
Sinapis sp.
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
Brassica caulorapa
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
-
2-propenylglucosinolate
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
Enterobacter cloacae 506
-
-
-
-
?
sinigrin + H2O
glucose + isothiocyanate
show the reaction diagram
Aspergillus niger AKU 3302
-
-
-
-
?
sinigrin + H2O
D-glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
15.3% of the activity with epi-progoitrin
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
Eutrema wasabi
-
-
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose
show the reaction diagram
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose
show the reaction diagram
-, Q9STD7
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose
show the reaction diagram
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose
show the reaction diagram
P37702, Q9C5C2
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose
show the reaction diagram
C9WCQ1
i.e. 2-propenyl glucosinolate, substrate saturation at 6 mM
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
-
-
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
C9WCQ0, -
-
-
-
?
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
-
i.e. allylglucosinolate
-
-
?
2-hydroxy-3-butenylglucosinolate + H2O
5-vinyl-2-oxazolidine thione + D-glucose
show the reaction diagram
-
-
-
-
?
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-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
show the reaction diagram
C9WCQ0, -
-
-
-
?
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
?
2-phenethylglucosinolate + H2O
additional information
-
-
-
in presence of ascorbic acid, isothiocyanate and nitrile are obtained but no thiocyanate
?
8-methylthiooctylglucosinolate + H2O
8-methylthiooctyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
allylglucosinolate + H2O
additional information
-
-
-
-
-
?
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
?
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
-
-
-
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
?
show the reaction diagram
-
-
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
additional information
-
-
-
-
-
?
benzylglucosinolate + H2O
additional information
-
-
-
-
?
indolyl-3-methylglucosinolate + H2O
indolyl-3-methyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
in intact plant tissues, the enzyme is physically separated from its GSL substrates
-
-
-
additional information
?
-
-, Q9STD7
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 is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates
-
-
-
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
?
-
C9WCQ0, -
recombinant TGG1 has weak ascorbic acid-independent O-beta-glucosidase activity with substrate specificity
-
-
-
additional information
?
-
C9WCQ0, -
the enzyme is inactive towards glucovanillin and n-octyl-beta-D-glucopyranoside
-
-
-
additional information
?
-
Enterobacter cloacae 506
-
induced by addition of 0.01% sinigrin and 6% mustard extract
-
-
-
phenylethylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
progoitrin + H2O
additional information
-
-
-
-
-
?
progoitrin + H2O
additional information
-
-
-
-
-
?
progoitrin + H2O
additional information
-
-
-
-
-
?
progoitrin + H2O
additional information
-
-
-
-
-
?
progoitrin + H2O
additional information
-
-
-
mainly oxazolidine-2-thione in the absence of epithiospecifier protein and mainly epithionitrile in the presence of epithiospecifier protein
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-hydroxybut-3-enylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
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
?
-
-
in intact plant tissues, the enzyme is physically separated from its GSL substrates
-
-
-
additional information
?
-
-, Q9STD7
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 is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates
-
-
-
additional information
?
-
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
-
-
-
additional information
?
-
Enterobacter cloacae 506
-
induced by addition of 0.01% sinigrin and 6% mustard extract
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
both epithiospecifier protein and nitrile-specifier protein are true enzymes rather than allosteric cofactors of myrosinase
-
additional information
C9WCQ0
the enzyme is ascorbic acid-independent
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(NH4)2SO4
-
activation is stronger in presence of 1 mM ascorbate
Ba2+
-
activation is stronger in presence of 1 mM ascorbate
Ca2+
Eutrema wasabi
-
1 mM CaCl2, activates
Ca2+
-
slight activation in presence of 1 mM ascorbate, no effect in absence of ascorbate
Co2+
Eutrema wasabi
-
1 mM CoCl2, activates
Co2+
-
1 mM, stimulates
Co2+
-
1 mM, stimulates
Cu+
-
1 mM, stimulates
Cu2+
-
1 mM, stimulates
Fe2+
-
shifts the enzyme to nitril fomration with increasing concentration
K+
Eutrema wasabi
-
1 mM KCl2, activates
K+
-
K2SO4, activation is stronger in presence of 1 mM ascorbate
KNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
Li+
-
1 mM LiCl2, activates
Mg2+
Eutrema wasabi
-
1 mM MgCl2, slight activation
Mg2+
-
activation is stronger in presence of 1 mM ascorbate
Mg2+
-
1 mM, slight activation
Mg2+
-
a combination of MgCl2 and ascorbic acid enhances activity
Mn2+
Eutrema wasabi
-
1 mM MnCl2, activates
Na+
Eutrema wasabi
-
1 mM NaCl2, slight activation
Na+
-
Na2SO4, activation is stronger in presence of 1 mM ascorbate
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
Ni2+
Eutrema wasabi
-
1 mM NiCl2, activates
Sn2+
Eutrema wasabi
-
1 mM SnCl2, activates
Sr2+
Eutrema wasabi
-
1 mM SrCl2, activates
Zn2+
Eutrema wasabi
-
1 mM ZnCl2, activates
Zn2+
-
1 mM ZnCl2, slight activation
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
Mn2+
-
1 mM, stimulates
additional information
-
the isozymes are active in a wide range of salt concentrations but sensitive to high salt concentrations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2-sulfato)ethyl 1-thio-beta-D-glucopyranoside
-
10mM, 30% inhibition
(2R,5R)-dihydroxymethyl-(3R,4R)-dihydroxypyrrolidine
-
inhibition of hydrolysis of sinigrin and progoitrin at pH 5 and at pH 7
(2R,5R)-dihydroxymethyl-(3R,4R)-dihydroxypyrrolidine
Sinapis sp.
-
-
(3-sulfato)propyl 1-thio-beta -D-glucopyranoside
-
IC50: 5 mM
(3-sulfonato)propyl 1-thio-beta-D-glucopyranoside
-
10 mM, 15% inhibition
(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
1,10-phenanthroline
Eutrema wasabi
-
-
1,10-phenanthroline
-
1 mM, 26% inhibition
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
1-O-methyl-alpha-D-glucopyranose
-
-
1-O-methyl-alpha-D-glucopyranose
-
0.1 M, 25% inhibition
2-deoxy-2-fluoroglucotropaeolin
-
-
2-deoxy-2-fluoroglucotropaeolin
-
inhibition occurs via the accumulation of a long-life glucosyl-enzyme intermediate
2-deoxyglucotropaeolin
-
-
2-methoxy-5-nitrotropone
Eutrema wasabi
-
-
2-methoxy-5-nitrotropone
-
1 mM, strong
5,5'-dithiobis(2-nitrobenzoic acid)
Eutrema wasabi
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
Sinapis sp.
-
-
Ag+
-
1 mM AgNO3, 79% inhibition
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
amygdalin
-
0.02 M, 14% inhibition
amygdalin
-
0.1 mM, 98% inhibition
Arbutin
-
0.1 M, 21% inhibition
Arbutin
-
0.1 M, 27% inhibition
Arbutin
-
0.1 M, 7% inhibition in absence of ascorbate, 26% inhibition in presence of ascorbate
ascorbate
-
0.3 mM, strong activation
ascorbic acid
-
0.1 mM L-ascorbic acid, 88% inhibition
ascorbic acid
-
-
Ca2+
-
1 mM, CaCl2, 14% inhibition
Ca2+
-
1 mM CaSO4, 55% inhibition
castanospermine
-
0.3 mM, 50% inhibition, competitive
castanospermine
-
-
castanospermine
-
-
Co2+
-
1 mM, CoCl2, 27% inhibition
Co2+
-
1 mM CoNO3, 66% inhibition
Cu+
-
1 mM, CuCl, 56% inhibition
Cu2+
Eutrema wasabi
-
1 mM CuCl2, complete inhibition
Cu2+
-
1 mM, CuCl2, 78% inhibition
Cu2+
-
1 mM CuCl2, 25% inhibition
Cu2+
-
1 mM CuSO4, 30% inhibition
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
delta-gluconolactone
-
-
delta-gluconolactone
-
1 mM, 62% inhibition
delta-gluconolactone
-
10 mM, 68% inhibition
delta-gluconolactone
-
poor noncompetitive inhibitor
diisopropyl fluorophosphate
-
1 mM, 18% inhibition
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
EDTA
Eutrema wasabi
-
-
EDTA
-
1 mM, 20% inhibition
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
-
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+
-
1 mM, FeCl2, 68% inhibition
-
Fe2+
-
1 mM FeSO4, 42% inhibition
-
Fe2+
-
1 mM FeSO4, 61% inhibition
-
Fe3+
Eutrema wasabi
-
1 mM FeCl3, 16% inhibition
-
Fe3+
-
1 mM, FeCl3, 18% inhibition
-
Fe3+
-
1 mM FeCl3, 26% inhibition
-
Fluorodinitrobenzene
Sinapis sp.
-
rate of inhibition is accelerated by 1 mM ascorbic acid
-
fructose
-
1.0 M, 16% inhibition in presence of ascorbate
galactose
-
1.0 M, 22% inhibition in presence of ascorbate
glucose
-
1.0 M, 22% inhibition in presence of ascorbate, competitive. No inhibition in absence of ascorbate
glucose
-
very weak inhibition
HgCl2
Eutrema wasabi
-
1 mM HgCl2, 93% inhibition
HgCl2
-
1 mM, HgCl2, 87% inhibition
HgCl2
-
1 mM HgCl2, 95% inhibition
HgCl2
-
1 mM HgCl2, 89% inhibition
K2SO4
-
1 mM, complete inhibition
KNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM 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
Mannose
-
1.0 M, 13% inhibition in presence of ascorbate
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
methyl jasmonate
-
decrease in enzyme activity, concommitant increase in levels of 4-methylsulfinylbutylglucosinolate and 8-methylsulfinylbutylglucosinolate in hypocotyl
methyl-beta-D-glucopyranoside
-
-
methyl-beta-D-glucopyranoside
-
0.1 M, 21% inhibition
Mg2+
-
1 mM, MgCl2, 22% inhibition
Mg2+
-
1 mM MgCl2, 23% inhibition
Mg2+
-
1 mM MgSO4, 93% inhibition
NaBr
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
NaBr
-
1 mM, 16% inhibition
NaCl
-
0.5 M, 30% inhibition, 2 M, complete inhibition
NaCl
C9WCQ1
inhibits, completely at 1 M
NaCl
C9WCQ0
enzyme activity is progressively inhibited by NaCl addition to the reactions and is completely inhibited at 1 M NaCl
NaNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
Ni2+
-
1 mM, NiCl2, 30% inhibition
p-diazabenzenesulfonic acid
Sinapis sp.
-
-
p-mercuribenzoate
Eutrema wasabi
-
-
p-mercuribenzoate
-
0.1 mM, strong inhibition
p-mercuribenzoate
Sinapis sp.
-
-
p-nitrophenyl-beta-D-glucopyranoside
-
-
p-nitrophenyl-beta-D-glucopyranoside
-
0.05 M, 31% inhibition
Pb2+
-
1 mM Pb-acetate, 60% inhibition
PCMB
-
0.06 mM, 91% inhibition
PCMB
Sinapis sp.
-
-
phenyl-beta-D-glucopyranoside
-
-
phenyl-beta-D-glucopyranoside
-
0.1 M, 52% inhibition
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
Salicin
-
0.1 M, 15% inhibition
Salicin
-
0.1 M, 22% inhibition
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
Sn2+
-
1 mM, SnCl2, 66% inhibition
Sr2+
-
1 mM, SrCl2, 21% inhibition
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
Trinitrobenzenesulfonic acid
Eutrema wasabi
-
-
Trinitrobenzenesulfonic acid
Sinapis sp.
-
rate of inhibition is accelerated by 1 mM ascorbic acid
xylose
-
1.0 M, 13% inhibition
Zn2+
-
1 mM, ZnCl2, 45% inhibition
Zn2+
-
1 mM ZnCl2, 28% inhibition
Zn2+
-
1 mM ZnSO4, 37% inhibition
Monochlorotrifluoro-p-benzoquinone
Sinapis sp.
-
-
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
-
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
-
no inhibition at 10 mM 2'-sulfatophenyl-1-thio-beta-D-glucopyranoside
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, activates
2-mercaptoethanol
-
1 mM, slight activation
ascorbate
C9WCQ1
stimulates 9fold at 0.2 mM, maximally 18fold at 00.8 mM
ascorbic acid
-
maximal activation at 0.3-0.5 mM
ascorbic acid
-
maximal activation at 1.57 mM
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
Eutrema wasabi
-
active only in presence of L-ascorbic acid, maximal activation at 2 mM
ascorbic acid
-
activates, enzyme is conformationally changed, no activation by analogs
ascorbic acid
-
activates; relatively unresponsible to ascorbic acid
ascorbic acid
-
1 mM, activation of isoenzyme RA, RB and RC; 1 mM, activation of isoenzyme SA, SB, very low activation of isoenzyme SC
ascorbic acid
-
considerable activation in the pH range 5.7-7.5, maximal activation at 0.375 mM
ascorbic acid
-
activates; 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
-
-
ascorbic acid
Eutrema wasabi
-
activates
ascorbic acid
-
-
ascorbic acid
-
activates; maximal activation at 0.7 mM
ascorbic acid
-
activates
ascorbic acid
-
activates
ascorbic acid
-
activates
ascorbic acid
-
a combination of MgCl2 and ascorbic acid enhances activity
ascorbic acid
-
1 mM, 100fold activation
ascorbic acid
-
the myrosinase isozymes show different activationinhibition responses towards ascorbic acid with maximal activity around 0.7-1 mM
ascorbyl palmitate
Eutrema wasabi
-
lower activation than with ascorbic acid
ascorbyl stearate
Eutrema wasabi
-
lower activation than with ascorbic acid
D-araboascorbate
Eutrema wasabi
-
lower activation than with ascorbic acid
EDTA
-
0.04 M, 70% activation
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
-
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; 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.; 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.; 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
-
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
-
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.; 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
-
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.
-
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
-
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
-
no activation by ascorbic acid
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.033
-
4-deoxyglucotropaeolin
-
-
28
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG4
34
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG1
80
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG5
0.068
-
6-deoxyglucotropaeolin
-
-
0.24
-
epi-progoitrin
-
37C, without ascorbic acid
0.43
-
epi-progoitrin
-
37C, with 20 mM ascorbic acid
0.075
-
glucotropaeolin
-
-
0.52
-
glucotropaeolin
-
37C, pH 4.5
0.71
-
p-nitrophenyl beta-D-glucopyranoside
-
-
1.5
-
p-nitrophenyl-beta-D-glucopyranoside
-
-
4
-
p-nitrophenyl-beta-D-glucopyranoside
-
with dioxane as solvent
12
-
p-nitrophenyl-beta-D-glucopyranoside
-
with 12.5 M methanol as solvent
14
-
p-nitrophenyl-beta-D-glucopyranoside
-
in absence of ascorbate
17
-
p-nitrophenyl-beta-D-glucopyranoside
-
with acetonitrile as solvent
30
-
p-nitrophenyl-beta-D-glucopyranoside
-
with 6.25 M methanol as solvent
49
-
p-nitrophenyl-beta-D-glucopyranoside
-
with 0.2 M methanol as solvent
51
-
p-nitrophenyl-beta-D-glucopyranoside
-
with 6.25 M ethanol as solvent
61
-
p-nitrophenyl-beta-D-glucopyranoside
-
with water as solvent
0.1
-
p-nitrophenyl-beta-D-glucoside
-
-
0.14
-
progoitrin
-
37C, without ascorbic acid
1.1
-
progoitrin
-
37C, with 20 mM ascorbic acid
0.96
-
singrin
-
free enzyme, at pH 6.5 and 37C
-
6.28
-
singrin
-
enzyme immobilized into Ca-polygalacturonate, at pH 6.5 and 37C
-
0.023
-
sinigrin
-
in absence of ascorbate
0.03
-
sinigrin
-
isoenzyme RC, without ascorbic acid
0.045
-
sinigrin
-
-
0.045
-
sinigrin
-
pH 5.5, isozyme TGG1
0.05
-
sinigrin
-
isoenzyme RA, without ascorbic acid
0.06
-
sinigrin
-
isoenzyme RB, without ascorbic acid
0.06
-
sinigrin
-
isoenzyme SB, without ascorbic acid
0.07
-
sinigrin
-
-
0.094
-
sinigrin
-
in presence of 0.05 M NaCl
0.115
-
sinigrin
-
-
0.156
-
sinigrin
-
at pH 7.0, at 30C
0.17
-
sinigrin
-
isoenzyme SC, without ascorbic acid
0.17
-
sinigrin
-
37C, without ascorbic acid
0.18
-
sinigrin
-
in presence of 0.5 M NaCl
0.18
-
sinigrin
-
in absence of ascorbate
0.245
-
sinigrin
-
pH 5.5, isozyme TGG4
0.25
-
sinigrin
-
isoenzyme SA, in presence of 1 mM ascorbic acid
0.25
-
sinigrin
-
in presence of 0.5 mM ascorbate
0.26
-
sinigrin
-
in presence of 0.05 M NaCl and 1 mM ascorbate
0.3
-
sinigrin
-
isoenzyme RC in presence of 1 mM ascorbic acid
0.3
-
sinigrin
-
isoenzyme SB, in presence of 1 mM ascorbic acid
0.37
-
sinigrin
-
-
0.4
-
sinigrin
-
isoenzyme RA and RB, in presence of 1 mM ascorbic acid
0.4
-
sinigrin
-
isoenzyme SC, in presence of 1 mM ascorbic acid
0.41
-
sinigrin
-
37C, pH 4.5
0.42
-
sinigrin
-
with H2O or 6.25 M methanol as solvent
0.47
-
sinigrin
Eutrema wasabi
-
-
0.47
-
sinigrin
-
-
0.54
-
sinigrin
-
with acetonitrile as solvent
0.547
-
sinigrin
-
pH 5.5, isozyme TGG5
0.57
-
sinigrin
-
with 12.5 M methanol as solvent; with 6.25 M ethanol as solvent
0.64
-
sinigrin
-
in presence of 2.5 M NaCl
0.87
-
sinigrin
-
with dioxane as solvent
0.92
-
sinigrin
-
in presence of 0.5 M NaCl and 1 mM ascorbate
0.93
-
sinigrin
-
in presence of 1 mM ascorbate
1
-
sinigrin
-
30C, pH 6.8
2.24
-
sinigrin
C9WCQ1
pH 6.0, 37C
2.78
-
sinigrin
-
in presence of 2.5 M NaCl and 1 mM ascorbate
2.82
-
sinigrin
C9WCQ0
pH not specified in the publication, at 37C
3.3
-
sinigrin
-
-
3.6
-
sinigrin
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.6
-
3-deoxyglucotropaeolin
-
-
3.1
-
4-deoxyglucotropaeolin
-
-
1.2
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG1
7.3
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG4
17
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG5
9.4
-
6-deoxyglucotropaeolin
-
-
22.8
-
glucotropaeolin
-
37C, pH 4.5
65.6
-
glucotropaeolin
-
-
2.11
-
sinigrin
-
in absence of ascorbate
2.3
-
sinigrin
-
pH 5.5, isozyme TGG1
3
6
sinigrin
-
37C, pH 4.5
12
-
sinigrin
-
pH 5.5, isozyme TGG4
28.4
-
sinigrin
C9WCQ1
pH 6.0, 37C
46
-
sinigrin
-
pH 5.5, isozyme TGG5
65.3
-
sinigrin
C9WCQ0
pH not specified in the publication, at 37C
187
-
sinigrin
-
30C, pH 6.8
287
-
sinigrin
-
in presence of 0.5 mM ascorbate
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.035
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG1
80189
0.21
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG5
80189
0.26
-
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, isozyme TGG4
80189
13
-
sinigrin
C9WCQ1
pH 6.0, 37C
16574
23
-
sinigrin
C9WCQ0
pH not specified in the publication, at 37C
16574
48
-
sinigrin
-
pH 5.5, isozyme TGG4
16574
53
-
sinigrin
-
pH 5.5, isozyme TGG1
16574
85
-
sinigrin
-
pH 5.5, isozyme TGG5
16574
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5
-
(3-sulfato)propyl 1-thio-beta -D-glucopyranoside
-
IC50: 5 mM
0.44
-
S-(3-hydroxypropyl)phenylacetothiohydroximate-O -sulfate
-
1 mM, 70% inhibition. IC50: 0.44 mM
0.25
-
S-(4-hydroxybutyl)phenylacetothiohydroximate-O-sulfate
-
1 mM, 88% inhibition. IC50: 0.25 mM
0.58
-
S-ethyl phenylacetothiohydroximate-O -sulfate
-
1 mM, 67% inhibition. IC50: 0.58 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.58
-
-
hydrolysis of p-nitrophenyl beta-glucoside
1.916
-
-
hydrolysis of sinigrin
5.26
-
-
hydrolysis of p-nitrophenyl beta-glucoside
24.3
-
C9WCQ1
purified recombinant enzyme
25.33
-
-
enzyme form Cc
28.94
-
-
enzyme form Ca
32.11
-
-
enzyme form Cb
60
-
-
myrosinase C
111
-
-
hydrolysis of sinigrin
114
-
-
myrosinase I
283
-
-
myrosinase II
additional information
-
-
direct ultraviolet spectrophotometric assay
additional information
-
Eutrema wasabi
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
the specific myrosinase activity in wild type seeds ranges from 0.1186-0.4263 micromol glucose/min/mg protein
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
isoenzyme SA
4.3
-
-
isoenzyme RC
4.4
-
-
and a second isoenzyme with pH-optimum 8.0
4.5
5.5
-
isoenzyme SB
4.5
7.8
-
hydrolysis of sinigrin, in citrate and phosphate buffer
5
6
-
myrosinase I and II
5
-
-
isoenzyme RA and RB
5.2
5.5
-
-
5.5
10.5
-
isozymes TGG1 and TGG4
5.5
-
-
hydrolysis of sinigrin
5.5
-
-
isoenzyme SC
5.5
-
-
-
5.5
-
Q9STD7
assay at
5.5
-
-
isozyme TGG5
5.8
-
-
-
6
6.5
-
at 37C
6
7
-
recombinant enzyme
6.5
7
Eutrema wasabi
-
-
6.5
8.5
C9WCQ0
-
6.5
-
-
hydrolysis of p-nitrophenyl-beta-D-glucopyranoside
6.5
-
-
at 37C, hydrolysis of epi-progoitrin
6.5
-
-
hydrolysis of epiprogoitrin
6.5
-
-
assay at
6.5
-
P37702, Q9C5C2
assay at; assay at
7.5
-
-
at 37C, hydrolysis of sinigrin
7.5
-
C9WCQ1
-
8
-
-
and a second isoenzyme with pH-optimum 8.0
8.5
-
-
hydrolysis of progoitrin
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
Eutrema wasabi
-
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 37C, 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
-
pH 5.0: about 70% of maximal activity, pH 10: about 40% of maximal activity, hydrolysis of progoitrin
5
11
C9WCQ1
CpTGG2 is active in broad pH range, almost inactive below pH 3.0 and above pH 13.0
5
7.5
-
about 35% of maximal activity at pH 5.0 and at pH 7.5
5
8.5
-
pH 5.0: about 40% of maximal activity, pH 8.5: about 45% of maximal activity, hydrolysis of epiprogoitrin
5.2
6.5
-
pH 5.2: about 50% of maximal activity, pH 6.0-6.5: optimum
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 37C, hydrolysis of sinigrin
5.5
7.5
-
pH 5.5: about 40% of maximal activity, pH 7.5: about 60% of maximal activity
5.5
9
C9WCQ0
more than 60% of maximum activity around pH 5.5 and 9.0
6
7.2
-
activity in presence of ascorbic acid is greater in sodium phosphate buffer than in citric acid /Na2HPO4 buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
35
-
-
in presence of L-ascorbic acid
36
60
-
recombinant enzyme
37
-
Eutrema wasabi
-
-
37
-
-
at 37C, hydrolysis of epi-progoitrin
37
-
-
assay at
40
-
-
hydrolysis of sinigrin
40
-
-
isozyme TGG1
40
-
C9WCQ1
-
40
-
C9WCQ0
-
50
-
-
at 37C, hydrolysis of sinigrin
55
-
-
in absence of L-ascorbic acid
60
-
-
isoenzyme RA, RB, RC and RD
60
-
-
isoenzyme SA, SB and SC
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
90
C9WCQ1
CpTGG2 is active in broad temperature range, peaks at 40C, gradually decreases between 40C and 90C, and shows 13% residual activity at 80C and 1% at 90C
20
60
-
isozyme TGG1, 65% of maximal activity at 20C, progressive increase that peaks at 40C, high activity at 50C, inactivation above 60C
20
65
-
20C: about 85% of maximal activity, 65C: about 45% of maximal activity, recombinant enzyme
20
65
-
20C: about 70% of maximal activity, 65C: about 65% of maximal activity at 37C, hydrolysis of sinigrin; 20C: about 75% of maximal activity, 65C: about 60% of maximal activity, at 37C, hydrolysis of epi-progoitrin
20
80
-
20% of maximal activity at 20C, progressive increase that peaks at 70C, 30% of maximal activity at 80C
20
90
-
20% of maximal activity at 20C, progressive increase that peaks at 60C, 5% of maximal activity at 90C
25
50
-
about 45% of maximal activity at 25C and at 50C, in presence of 1 mM ascorbic acid
30
50
Eutrema wasabi
-
about 40% of maximal activity at 30C and at 50C
30
70
-
30C, about 60% of maximal activity of the enzyme from white cabbage, about 45% of maximal activity of the enzyme from red cabbage, 70C: about 75% of maximal activity of the enzyme from red cabbage, about 50% of maximal activity of the enzyme from white cabbage
40
80
-
40C: 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, 80C: 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 50-60C. Beyond this value range it decreases to about 75% of the maximal activity at 70C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
5.6
-
enzyme complex is formed by isoenzymes with isoelectric points between 4.8 and 5.6
4.9
-
-
isoelectric focusing, pH-range 3-9
4.95
-
-
isoelectric focusing, pH-range 2.5-6.5
6.35
-
C9WCQ1
TGG2 sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
vascular cambium of root
Manually annotated by BRENDA team
-
low expression of isoform TGG1, no expression of isoform TGG2. Monitoring of the levels of glucosinolates
Manually annotated by BRENDA team
-
myrosinase B isoforms
Manually annotated by BRENDA team
-
recombinant enzyme is secreted by Pichia pastoris
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Eutrema wasabi
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
no activity found in latex
Manually annotated by BRENDA team
-
enzyme activity is restricted to guard cells and phloem idioblasts
Manually annotated by BRENDA team
P37702, Q9C5C2
; TGG1 is a strikingly abundant protein in guard cells
Manually annotated by BRENDA team
-
hypocotyl of seedling, high expression of isoform TGG1, no expression of isoform TGG2
Manually annotated by BRENDA team
Q9STD7
myrosinase-storing cells, i.e. myrosin cells
Manually annotated by BRENDA team
-
activity is 4-5 times higher in the outer leaves than in the stalk, the inner leaves and the centre of the Brussels sprouts
Manually annotated by BRENDA team
-
myrosinase B isoforms
Manually annotated by BRENDA team
-
myrosin cells of phloem parenchyma
Manually annotated by BRENDA team
-
myrosin cells of phloem parenchyma and ground tissue
Manually annotated by BRENDA team
-
expression of isoform TGG2
Manually annotated by BRENDA team
-
isozymne TGG1
Manually annotated by BRENDA team
-
of head and thorax
Manually annotated by BRENDA team
Aspergillus niger AKU 3302
-
-
-
Manually annotated by BRENDA team
-
exclusively localized to the interior of the myrosin grains
Manually annotated by BRENDA team
-
of the embryo axis and the cotyledons
Manually annotated by BRENDA team
-
myrosin cells are different from companion cells and the glucosinolate-containing S-cells
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
parenchyma, myrosin cells
Manually annotated by BRENDA team
-
enzyme activity is restricted to guard cells and phloem idioblasts
Manually annotated by BRENDA team
-
highest activity 2 days after germination; seedling roots, highest activity
Manually annotated by BRENDA team
-
highest activity 1 day after germination; seedling roots, highest activity
Manually annotated by BRENDA team
-
highest activity 2 days after germination; seedling roots, highest activity
Manually annotated by BRENDA team
-
highest activity 1 day after germination; seedling roots, highest activity
Manually annotated by BRENDA team
-
highest activity 2 days after germination; seedling roots, highest activity
Manually annotated by BRENDA team
-
epidermis and vascular cambium
Manually annotated by BRENDA team
-
isozymnes TGG4 and TGG5
Manually annotated by BRENDA team
C9WCQ1
CpTGG2 is specifically expressed in the root
Manually annotated by BRENDA team
-
found in sarcotestae but not in endosperms
Manually annotated by BRENDA team
-
Myr1 encodes seed myrosinase
Manually annotated by BRENDA team
-
myrosinase A isoforms are expressed only in seed tissue; myrosinase B isoforms
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
cotyledon; hypocotyl; leaf; myrosinase gene MYR2 is transcribed in all organs of the seedling, myrosinase gene Myr1 shows no transcription in seedling; root
Manually annotated by BRENDA team
-
hypocotyl of seedling, high expression of isoform TGG1, no expression of isoform TGG2
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
Myr2 encodes vegetative type myrosinase
Manually annotated by BRENDA team
additional information
-
defatted meal
Manually annotated by BRENDA team
additional information
-
no myrosin cells are detected in the ground tissue
Manually annotated by BRENDA team
additional information
-
no activity in root or seed
Manually annotated by BRENDA team
additional information
-
in intact plant tissues, the enzyme is physically separated from its GSL substrates
Manually annotated by BRENDA team
additional information
-
glucosinolate profiles in different tissues, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Aspergillus niger AKU 3302
-
-
-
Manually annotated by BRENDA team
-
associated with the cytoplasmic side of internal membranes
Manually annotated by BRENDA team
-
the specific activity of the protoplast is less than that of the intact root tissue
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
61000
-
-
gel filtration
62000
-
-
gel filtration
97000
-
-
gel filtration
120000
-
-
gel filtration
124000
-
Sinapis sp.
-
myrosinase F-IIB, equilibrium sedimentation
125000
-
Sinapis sp.
-
myrosinase F-IIB, gel filtration
126000
-
-
sucrose density gradient sedimentation
130000
-
-
gel filtration
133000
135000
-
gel filtration, ultracentrifugation
140000
200000
-
enzyme forms complexes of different molecular weight with several protein subunits
140000
-
-
M75 myrosinase, gel filtration
150000
151000
-
gel filtration, equilibrium sedimentation
150000
-
Sinapis sp.
-
myrosinase F-IB, gel filtration
152000
-
Sinapis sp.
-
myrosinase F-IB, equilibrium sedimentation
154000
-
-
non-denaturing PAGE
156000
-
-
myrosinase I, gel filtration
188000
-
-
myrosinase II, gel filtration
270000
350000
-
enzyme forms complexes of different molecular weight with several protein subunits
470000
-
-
gel filtration
500000
600000
-
enzyme forms complexes of different molecular weight with several protein subunits
580000
-
Eutrema wasabi
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Sinapis sp.
-
x * 30000, enzyme consists of at least 4 subunits, myrosinase F-IIB, SDS-PAGE; x * 40000, enzyme consists of at least 4 subunits, myrosinase F-IA, F-IB and F-IIA, SDS-PAGE
?
-
x * 65000, myrosinase B, SDS-PAGE; x * 70000, myrosinase C, SDS-PAGE; x * 75000, myrosinase A, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
-
enzyme consists of complexes of several subunits with molecular weights between 10000 Da and 110000 Da, SDS-PAGE
?
Q5PXK2
x * 59700, calculated for mature protein, x * 65000, SDS-PAGE
?
C9WCQ1
x * 70000, recombinant TGG2, SDS-PAGE, x * 59500, about, TGG2 sequence calculation
?
-
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
?
C9WCQ0
x * 65000, SDS-PAGE
?
-
x * 140000, SDS-PAGE
dimer
-
2 * 77000, SDS-PAGE
dimer
-
1 * 62000 + 1 * 65000, SDS-PAGE
dimer
-
2 * 65000, SDS-PAGE
dimer
-
2 * 66000, SDS-PAGE
dimer
-
2 * 75000, myrosinase I, SDS-PAGE
dimer
-
1 * 61000 + 1 * 62000, SDS-PAGE
dimer
-
2 * 75000, M75 myrosinase, SDS-PAGE
dimer
-
2 * 57000-58000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dodecamer
Eutrema wasabi
-
12 * 45000-47000, SDS-PAGE
hexamer
-
6 * 75000, SDS-PAGE
trimer
-
3 * 62000, myrosinase II, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Q5PXK2
sequence contains a signal peptide of 1900 Da
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
-
myrosinase C1 contains 9.3% carbohydrate, myrosinase C2 contains 15.2% carbohydrate, myrosinase C3 contains 17.4% carbohydrate
glycoprotein
-
N-linked glycosylation sites, myrosinase I contains 18% carbohydrate
glycoprotein
-
size differences between the different myrosinases are mainly due to differences in glycosylation
glycoprotein
C9WCQ1
CpTGG2 may have 5 N-glycosylation sites
glycoprotein
C9WCQ0
-
glycoprotein
-
carbohydrate chains distributed over the surface of the enzyme
glycoprotein
-
-
glycoprotein
-
both subunits contain carbohydrate
glycoprotein
-
-
glycoprotein
-
contains 18% carbohydrate: 4% glucosamine, 12% hexose and 2% pentose
glycoprotein
-
contains 13000 Da carbohydrate per dimer, the carbohydrate is required to maintain molecular stability and solubility in the dehydrated environment of the seed
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
-
signal peptide
additional information
-
does not appear to be a glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of recombinant enzyme at 1.1 A
-
native myrosinase and stable glycosyl-enzyme intermediate
-
purified enzyme in 20 mM HEPES, pH 6.5, 150 mM NaCl, and 0.02 mM ZnSO4, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
Eutrema wasabi
-
5C, 41 h, about 60% loss of activity
5
7
-
below 40C, 24 h, stable
5.5
8.5
-
below 45C, stable
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
6
11
-
37C, 30 min, stable
6
9
-
30C, 1 h, stable
6
-
Eutrema wasabi
-
5C, 41 h, about 10% loss of activity
6
-
-
maximal stability
7
-
Eutrema wasabi
-
5C, 41 h, stable
7
-
-
5C, 24 h, about 20% loss of activity
7.6
8
-
5C, 24 h, stable
9
-
-
5C, 24 h, about 55% loss of activity
10
-
Eutrema wasabi
-
5C, 41 h, about 25% loss of activity
11
-
Eutrema wasabi
-
5C, 41 h, about 30% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Eutrema wasabi
-
pH 7.0, 20 min, stable
30
-
-
pH 6.8, 30 min, stable
30
-
-
pH 7.8, 20 min, stable
30
-
-
90 min, stable
30
-
-
60 min, 24% loss of activity
30
-
-
myrosinase of the mutant strain NR463U4 retains activity 3.5times longer than wild-type enzyme
35
-
-
pH 7.8, 20 min, about 40% loss of activity
40
-
Eutrema wasabi
-
pH 7.0, 20 min, about 25% loss of activity
40
-
-
pH 6.8, 30 min, about 20% loss of activity
40
-
-
pH 7.8, 20 min, complete inactivation
40
-
-
pH 7.0, 15 min, stable
40
-
-
45 min, 18% loss of activity
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
50
-
Eutrema wasabi
-
pH 7.0, 20 min, about 60% loss of activity
50
-
-
pH 6.8, 30 min, about 50% loss of activity
50
-
-
pH 7.0, 15 min, complete loss of activity
50
-
-
30 min, stable
60
-
-
pH 6.8, 30 min, about 90% loss of activity
60
-
-
30 min, enzyme from red cabbage is stable, enzyme from white cabbage loses about 60% of its activity
60
-
-
inactivation at or above
70
-
Eutrema wasabi
-
pH 7.0, 20 min, about 80% loss of activity
70
-
-
30 min, 90% loss of activity
80
-
C9WCQ1
purified recombinant TGG2, 20 min, 50% activity remaining
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 50C and above. Isothiocyanates formed by enzyme are relatively thermolabile and pressure stable
additional information
-
-
the isozymes are rather thermostable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
some loss of activity upon freezing
-
good static and operational stability after immobilization on gamma-alumina
-
the enzyme is quite pressure stable, as its activity is retained after pressure treatment up to 600 MPa combined with temperatures up to 60C. At low pressures there is an antagonistic effect between pressure and thermal treatment, since the activity of the enzyme is retained after treatment at 70C up to 300 MPa
-
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 45C and 22 MPa for 60 min, while only 1% of myrosinase activity remains at 22 MPa and 65C for 5 min. As the pressure increases from 8 to 22 MPa at 55C for 60 min, the relative residual activity is significantly reduced from 37.04 to 18.18%
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
photooxidation by methylene blue
Sinapis sp.
-
208568
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for several months
-
4C, stable for more than 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged root isozymes TGG4 and TGG5 and His-tagged leaf isozyme TGG1 from Pichia pastoris by nickel affinity chromatography to homogeneity
-
fast and gentle procedure for hte isolation of enzyme complex from seed
-
at least 2 isoenzymes
-
complexes with myrosinase and myrosinase-binding protein
-
fast and gentle procedure for the isolation of enzyme complex from seed
-
myrosinase C1, C2 and C3
-
myrosinase I and II
-
recombinant
-
three different forms of enzyme: Ca, Cb and Cc
-
fast and gentle procedure for the isolation of enzyme complex from seed
-
immobilized metal affinity chromatography
C9WCQ0
recombinant TGG2 from Pichia pastoris
C9WCQ1
-
Eutrema wasabi
-
2 isoenzymes
-
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
-
myrosinase A, B and C
-
native enzyme from seeds
-
-
Sinapis sp.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
expression in Sf9 cell
Q5PXK2
expression and secretion by Pichia pastoris
-
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
-
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
-
recombinant gene Myr1.Bn1, expressionin transgenic Brassica napus plants
Q9STD7
expressed in Pichia pastoris
C9WCQ0
gene pTGG2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Pichia pastoris
C9WCQ1
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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 herbovore attack, 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
-
inhibition of the glucosinolate-myrosinase system is observed when oxalic acid with a pH of 3.0 or below is used
-
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 glucosinolate-myrosinase system is activated in the presence of oxalic acid at pH 4.0-7.0
-
the enzyme is not induced by phytohormones jasmonic acid and salicylate
-
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 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 cultivars with the highest vitamin C content have the lowest myrosinase activity
-
cabbage cultivars grown in the northern area of Spain with low temperatures and radiation lead to higher mean values of myrosinase activity
-
myrosinase activity in leaves of significantly decreases when Nakajimana leaves are heated over 70C
-
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
-
in crushed heat-treated leaves of Nakajimana (70C for 30 s), myrosinase activity increases 4fold
-
the enzyme is induced by phytohormone jasmonic acid, overview
-
the enzyme is induced by phytohormones jasmonic acid and salicylate, overview
-
significant losses of myrosinase activity are observed during the post-harvest drying stage
-
at harvest, myrosinase activity considerably increases in the yellow and red hypocotyls compared to the black ecotype
-
the enzyme is not induced by herbivore attack with Pieris rapae, overview
-
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 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 phytohormones, such as jasmonic acid and salicylate, overview
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D174A
-
generated mutant, shows no activity toward pNP-S-GlcNAc
D175A
-
generated mutant, D175A mutant shows significant activity toward pNP-S-GlcNAc
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
P37702, Q9C5C2
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; 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
Q9STD7
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
analysis
-
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
Brassica carinata BRK-147-A
-
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
-
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
nutrition
-
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
-
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 50C and above. Isothiocyanates formed by enzyme are relatively thermolabile and pressure stable
agriculture
-
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