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 hide
3.2.1.147
-
RECOMMENDED NAME
GeneOntology No.
thioglucosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a thioglucoside + H2O = a sugar + a thiol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-beta-glucosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of S-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-38-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
-
-
Manually annotated by BRENDA team
strain BRK-147-A
-
-
Manually annotated by BRENDA team
Brassica caulorapa
i.e. kohlrabi
-
-
Manually annotated by BRENDA team
cultivars Hinova, Megaton, Alfredo, Candela, and Bronco
-
-
Manually annotated by BRENDA team
i.e. Chineses cabbage
-
-
Manually annotated by BRENDA team
strain 506
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ecotype Shandong, China
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
i.e. wild candytuft; var. coronaria, i.e. candytuft
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Paracolobactrum aerogenoides
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sinapis sp.
strain OTG1
-
-
Manually annotated by BRENDA team
strain OTG1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2-hydroxy-2-phenylethylglucosinolate + H2O
D-glucose + ?
show the reaction diagram
(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-hydroxy-3-butenylglucosinolate + H2O
5-vinyl-2-oxazolidine thione + D-glucose
show the reaction diagram
-
-
-
-
?
2-hydroxy-3-butenylglucosinolate + H2O
?
show the reaction diagram
-
-
-
?
2-hydroxybut-3-enylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
?
2-phenylethylglucosinolate + H2O
2-phenylethyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
2-phenylethylglucosinolate + H2O
?
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-butenylglucosinolate + H2O
?
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
4-methylsulfinylbutyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
4-methylsulfinylbutylglucosinolate + H2O
?
show the reaction diagram
4-methylthiobutylglucosinolate + H2O
4-methylthiobutyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
4-methylthiobutylglucosinolate + H2O
?
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-pentenylglucosinolate + H2O
4-pentenyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
4-pentenylglucosinolate + H2O
?
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
-
-
-
-
?
8-methylthiooctylglucosinolate + H2O
8-methylthiooctyl-isothiocyanate + D-glucose
show the reaction diagram
-
-
-
-
?
allyl glucosinolate + H2O
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
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
glucoapparin + H2O
?
show the reaction diagram
glucobrassicin + H2O
?
show the reaction diagram
glucocheirolin + H2O
?
show the reaction diagram
gluconasturtiin + H2O
?
show the reaction diagram
-
-
-
?
gluconasturtiin + H2O
D-glucose + ?
show the reaction diagram
glucoraphenin + H2O
?
show the reaction diagram
-
3.8% of the activity with epi-progoitrin
-
-
?
glucosinalbin + H2O
?
show the reaction diagram
glucosinolate + H2O
isothiocyanate + thiocyanate + nitrile + epithionitrile + ?
show the reaction diagram
-
-
-
-
?
glucotropaeolin + H2O
?
show the reaction diagram
glucotropaeolin + H2O
D-glucose + ?
show the reaction diagram
indol-3-ylmethyl glucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
indolyl-3-methylglucosinolate + H2O
indolyl-3-methyl-isothiocyanate + D-glucose
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
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
phenylethylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
progoitrin + H2O
?
show the reaction diagram
sinalbin + H2O
?
show the reaction diagram
sinigrin + H2O
?
show the reaction diagram
sinigrin + H2O
allyl isothiocyanate + D-glucose
show the reaction diagram
sinigrin + H2O
D-glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
sinigrin + H2O
D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
show the reaction diagram
sinigrin + H2O
D-glucose + isothiocyanate
show the reaction diagram
sinigrin + H2O
glucose + (1Z)-N-(sulfooxy)but-3-enimidothioic acid
show the reaction diagram
2-hydroxybut-3-enylglucosinolate + H2O
additional information
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-hydroxybut-3-enylglucosinolate + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
activation is stronger in presence of 1 mM ascorbate
Ba2+
-
activation is stronger in presence of 1 mM ascorbate
Cu+
-
1 mM, stimulates
Cu2+
-
1 mM, stimulates
Fe2+
-
shifts the enzyme to nitril fomration with increasing concentration
KNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
Li+
-
1 mM LiCl2, activates
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+
-
1 mM NiCl2, activates
Sn2+
-
1 mM SnCl2, activates
Sr2+
-
1 mM SrCl2, activates
additional information
-
the isozymes are active in a wide range of salt concentrations but sensitive to high salt concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-sulfato)ethyl 1-thio-beta-D-glucopyranoside
-
10mM, 30% inhibition
(2R,5R)-dihydroxymethyl-(3R,4R)-dihydroxypyrrolidine
(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
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
2-deoxy-2-fluoroglucotropaeolin
2-deoxyglucotropaeolin
-
-
2-methoxy-5-nitrotropone
5,5'-dithiobis(2-nitrobenzoic acid)
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
Arbutin
ascorbate
-
0.3 mM, strong activation
ascorbic acid
castanospermine
Cu+
-
1 mM, CuCl, 56% 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
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
Fluorodinitrobenzene
Sinapis sp.
-
rate of inhibition is accelerated by 1 mM ascorbic acid
-
fructose
galactose
glucose
K2SO4
-
1 mM, complete inhibition
KNO3
-
activates in absence of ascorbate, inhibits in presence of 1 mM ascorbate
maltose
mannose
methyl jasmonate
methyl-beta-D-glucopyranoside
Monochlorotrifluoro-p-benzoquinone
Sinapis sp.
-
-
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
p-nitrophenyl-beta-D-glucopyranoside
phenyl-beta-D-glucopyranoside
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
sinigrin
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
xylose
-
1.0 M, 13% inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
ascorbate
ascorbic acid
ascorbyl palmitate
-
lower activation than with ascorbic acid
ascorbyl stearate
-
lower activation than with ascorbic acid
D-araboascorbate
-
lower activation than with ascorbic acid
EDTA
-
0.04 M, 70% activation
epithiospecifier protein
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
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
4-deoxyglucotropaeolin
-
-
16.81 - 80
4-nitrophenyl beta-D-glucopyranoside
0.068
6-deoxyglucotropaeolin
-
-
0.24 - 0.43
epi-progoitrin
0.11
gluconasturtiin
recombinant enzyme, pH 5.5, 37C
0.075 - 0.52
glucotropaeolin
0.71
p-nitrophenyl beta-D-glucopyranoside
-
-
1.5 - 61
p-nitrophenyl-beta-D-glucopyranoside
0.1
p-nitrophenyl-beta-D-glucoside
-
-
0.14 - 1.1
progoitrin
0.0111 - 6.28
sinigrin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6
3-deoxyglucotropaeolin
Lepidium sativum
-
-
3.1
4-deoxyglucotropaeolin
Lepidium sativum
-
-
1.2 - 17
4-nitrophenyl beta-D-glucopyranoside
9.4
6-deoxyglucotropaeolin
Lepidium sativum
-
-
8.91
gluconasturtiin
Armoracia rusticana
I1TIJ2
pH 5.5, 37C
22.8 - 65.6
glucotropaeolin
0.26 - 287
sinigrin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035 - 0.26
4-nitrophenyl beta-D-glucopyranoside
83.13
gluconasturtiin
Armoracia rusticana
I1TIJ2
recombinant enzyme, pH 5.5, 37C
140126
13 - 85
sinigrin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.368
sinigrin
-
sinigrin substrate inhibition, Michaelis-Menten modelling, pH 7.0, 40C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
(3-sulfato)propyl 1-thio-beta -D-glucopyranoside
Sinapis alba
-
IC50: 5 mM
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
0.58
S-ethyl phenylacetothiohydroximate-O -sulfate
Sinapis alba
-
1 mM, 67% inhibition. IC50: 0.58 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.58
-
hydrolysis of p-nitrophenyl beta-glucoside
0.69 - 2.04
-
enzyme from florets of the different cultivars, pH not specified in the publication, glucose assay, 40C
0.73 - 0.86
-
enzyme from roots of the different cultivars, pH not specified in the publication, glucose assay, 40C
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, 40C
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, 40C
1.58
-
counter-current chromatography fraction, pH and temperature not specified in the publication
1.916
-
hydrolysis of sinigrin
1.96 - 2.39
-
enzyme from leaves of the different cultivars, pH not specified in the publication, glucose assay, 40C
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, 25C
5.26
-
hydrolysis of p-nitrophenyl beta-glucoside
5.8
-
purified enzyme, pH 7.0, 40C
6.37 - 15.3
-
enzyme from roots of the different cultivars, pH not specified in the publication, AITC assay, 25C
6.87 - 14.7
-
enzyme from leaves of the different cultivars, pH not specified in the publication, AITC assay, 25C
13.08 - 15.62
-
enzyme from florets of the different cultivars, pH not specified in the publication, AITC assay, 25C
14.46 - 20.6
-
enzyme from leaves of the different cultivars, pH not specified in the publication, AITC assay, 25C
24.3
purified recombinant enzyme
25.33
-
enzyme form Cc
28.94
-
enzyme form Ca
32.11
-
enzyme form Cb
60
-
myrosinase C
91
purified recombinant enzyme TGG2, pH 5.5, 37C
99.6
purified recombinant enzyme TGG1, pH 5.5, 37C
111
-
hydrolysis of sinigrin
114
-
myrosinase I
283
-
myrosinase II
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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 - 5.5
rather sharp maximum between pH 5.0-5.5
5 - 6
-
myrosinase I and II
5.2 - 5.5
-
-
5.5 - 10.5
-
isozymes TGG1 and TGG4
6 - 6.5
-
at 37C
6.5
assay at; assay at
8.5
-
hydrolysis of progoitrin
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 9
-
pH 3.0: about 60% of maximal activity, pH 9.0: 80-90% of maximal activity
3 - 8
-
pH 3.0: about 45% of maximal activity, pH 8.0: about 55% 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 - 9
-
pH 4.5: about 55% of maximal activity, pH 9.0: about 80% of maximal activity, recombinant enzyme
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
5 - 10
activity range; activity range
5 - 7.5
-
about 35% of maximal activity at pH 5.0 and at pH 7.5
5 - 11
CpTGG2 is active in broad pH range, almost inactive below pH 3.0 and above pH 13.0
5 - 10
-
pH 5.0: about 70% of maximal activity, pH 10: about 40% of maximal activity, hydrolysis of progoitrin
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 37C, hydrolysis of sinigrin
5.2 - 6.5
-
pH 5.2: about 50% of maximal activity, pH 6.0-6.5: optimum
5.5 - 9
more than 60% of maximum activity around pH 5.5 and 9.0
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
-
assay at
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
55
-
in absence of L-ascorbic acid
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 90
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 - 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
20 - 65
25 - 50
-
about 45% of maximal activity at 25C and at 50C, in presence of 1 mM ascorbic acid
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
30 - 50
-
about 40% of maximal activity at 30C and at 50C
37 - 58
70% of maximal activity between 37C and 58C; 70% of maximal activity between 37C and 58C
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
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 70C with 31% water content, overview
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 5.6
4.9
-
isoelectric focusing, pH-range 3-9
4.95
-
isoelectric focusing, pH-range 2.5-6.5
6.35
TGG2 sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low expression of isoform TGG1, no expression of isoform TGG2. Monitoring of the levels of glucosinolates
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
-
of head and thorax
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
Myr2 encodes vegetative type myrosinase
Manually annotated by BRENDA team
additional information