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Information on EC 3.2.1.147 - thioglucosidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9C5C2
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3.2.1.147 thioglucosidaseIUBMB Comments
Has a wide specificity for thioglycosides.
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Word Map
- 3.2.1.147
- glucosinolates
- isothiocyanate
- brassica
- broccoli
- brassicaceae
- sulforaphane
-
cruciferous
-
nitril
- glucoraphanin
- mustard
- sprout
- oleracea
-
herbivore
- napus
-
cook
-
chemopreventive
- sinapis
- cabbage
- radish
- juncea
-
crucifer
-
epithiospecifier
-
anticarcinogenic
- italica
- brassicales
-
3.2.3.1
- glucotropaeolin
-
generalist
-
armoraciae
- rusticana
- watercress
-
bomb
- floret
- idioblasts
-
cyclocondensation
- kale
- abyssinica
- glucobrassicin
-
4-hydroxybenzyl
- raphanus
- analysis
- pharmacology
-
tuscan
- gluconasturtiin
- erucin
-
mercapturic
-
brussels
- nutrition
- agriculture
- moringa
- lepidium
-
pungen
- crambe
-
blanch
- biotechnology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
myrosinase, myrosin, thioglucosidase, myrosinase a, thioglucoside glucohydrolase, cptgg1, myr ii, myr1.bn1, myrii, atypical myrosinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-thioglucosidase
-
-
-
-
beta-thioglucoside glucohydrolase
glucosidase, thio-
-
-
-
-
glucosinolase
-
-
-
-
myrosin
-
-
-
-
myrosinase
sinigrase
-
-
-
-
sinigrinase
-
-
-
-
TGG1
Thioglucosidase
-
-
-
-
beta-thioglucoside glucohydrolase
-
-
-
-
myrosinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of S-glycosyl bond
-
-
-
-
hydrolysis of O-beta-glucosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thioglucoside glucohydrolase
Has a wide specificity for thioglycosides.
CAS REGISTRY NUMBER
COMMENTARY
9025-38-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
i.e. 2-propenyl glucosinolate
-
-
?
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
2-hydroxy-3-butenylglucosinolate + H2O
5-vinyl-2-oxazolidine thione + D-glucose
-
-
-
-
?
2-phenylethylglucosinolate + H2O
2-phenylethyl-isothiocyanate + D-glucose
-
-
-
-
?
2-propenylglucosinolate + H2O
2-propenyl-isothiocyanate + D-glucose
-
epithiospecifier protein and nitrile-specifier protein can switch myrosinase-catalyzed degradation of 2-propenylglucosinolate from isothiocyanate to nitrile, only epithiospecifier protein generates the corresponding epithionitrile
-
-
?
3-benzyloxypropylglucosinolate + H2O
3-benzyloxypropyl-isothiocyanate + D-glucose
-
-
-
-
?
3-butenylglucosinolate + H2O
3-butenyl-isothiocyanate + D-glucose
-
-
-
-
?
3-methylthiopropylglucosinolate + H2O
3-methylthiopropyl-isothiocyanate + D-glucose
-
-
-
-
?
4-benzyloxybutylglucosinolate + H2O
4-benzyloxybutyl-isothiocyanate + D-glucose
-
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
4-methylsulfinylbutylglucosinolate + H2O
4-methylsulfinylbutyl-isothiocyanate + D-glucose
-
-
-
-
?
4-methylthiobutylglucosinolate + H2O
4-methylthiobutyl-isothiocyanate + D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-pentenylglucosinolate + H2O
4-pentenyl-isothiocyanate + D-glucose
-
-
-
-
?
5-methylthiopentylglucosinolate + H2O
5-methylthiopentyl-isothiocyanate + D-glucose
-
-
-
-
?
6-methylthiohexylglucosinolate + H2O
6-methylthiohexyl-isothiocyanate + D-glucose
-
-
-
-
?
7-methylthioheptylglucosinolate + H2O
7-methylthioheptyl-isothiocyanate + D-glucose
-
-
-
-
?
8-methylthiooctylglucosinolate + H2O
8-methylthiooctyl-isothiocyanate + D-glucose
-
-
-
-
?
benzylglucosinolate + H2O
benzylisothiocyanate + D-glucose + ?
-
nitrile-specifier proteins, especially nitrile-specifier protein 2, NSP2, in conjunction with myrosinase enable the enzyme to generate nitriles, overview
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indo-3-ylmethyl isothiocyanate + D-glucose
-
high activity
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
indolyl-3-methylglucosinolate + H2O
indolyl-3-methyl-isothiocyanate + D-glucose
-
-
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
-
i.e. 2-propenyl glucosinolate
-
-
?
sinigrin + H2O
allyl isothiocyanate + D-glucose + ?
i.e. 2-propenyl glucosinolate
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
-
-
?
additional information
?
-
-
differences in basal activity of myrosinase isozymes, no activity with desulfosinigrin
-
-
?
additional information
?
-
-
myrosinase acts on glucosinolates to form an unstable aglycone intermediate that can rearrange spontaneously to form an isothiocyanate. Interaction of a protein called epithiospecifier protein with myrosinase diverts the reaction toward the production of epithionitriles or nitriles depending on the glucosinolate structure, while nitrile-specifier proteins, especially nitrile-specifier protein 2, NSP2, enable to generate nitriles in conjunction with myrosinase, tissue distributions of the specifier proteins, overview
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
indole glucosinolates are in planta substrates for PYK10
-
-
?
additional information
?
-
-
enzyme PYK10 has in vitro myrosinase activity toward indole glucosinolates. PYK10 exhibits both O-glucosidase and S-glucosidase activity. No activity against sinigrin. PYK10 hydrolyzes both coumarin glucosides and glucosinolates, and accounts for the bulk of total myrosinase activity against indol-3-ylmethyl glucosinolate in Arabidopsis thaliana roots
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates
-
-
?
additional information
?
-
the enzyme is active with indole and aliphatic glucosinolates
-
-
?
additional information
?
-
the enzyme is active with indole and aliphatic glucosinolates
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methoxyindol-3-ylmethyl-glucosinolate + H2O
1-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
4-methoxyindol-3-ylmethyl-glucosinolate + H2O
4-methoxyindol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
indol-3-ylmethyl glucosinolate + H2O
indol-3-ylmethyl isothiocyanate + D-glucose
-
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
myrosinases catalyze the hydrolysis of glucosinolates, a structurally distinct group of nitrogen- and sulfur-containing secondary metabolites
-
-
?
additional information
?
-
-
indole glucosinolates are in planta substrates for PYK10
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
shifts the enzyme to nitril fomration with increasing concentration
additional information
-
the isozymes are active in a wide range of salt concentrations but sensitive to high salt concentrations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methyl jasmonate
-
decrease in enzyme activity, concommitant increase in levels of 4-methylsulfinylbutylglucosinolate and 8-methylsulfinylbutylglucosinolate in hypocotyl
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
all the plant myrosinases are reported to be activated by ascorbic acid
ascorbic acid
-
the myrosinase isozymes show different activationinhibition responses towards ascorbic acid with maximal activity around 0.7-1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
sinigrin
recombinant enzyme TGG2, pH 5.5, 37°C, in presence of ascorbate
0.108
sinigrin
recombinant enzyme TGG1, pH 5.5, 37°C, in presence of ascorbate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.04
sinigrin
recombinant enzyme TGG2, pH 5.5, 37°C, in presence of ascorbate
10.7
sinigrin
recombinant enzyme TGG1, pH 5.5, 37°C, in presence of ascorbate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.5
5.5 - 10.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 12
-
isozymes TGG4 and TGG5 are active at pH 2.5, and TGG4 shows a broad optimum at pH 5.5-10.5, while TGG5 peaks at pH 5.5 and than loses activity at pH 6.5 and 8.5, both show 50% of maximal activity at pH 11.5
4.5 - 12
-
isozyme TGG1, inactive below pH 4.5, rather unaffected by differences in pH above 5.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
isozyme TGG1, 65% of maximal activity at 20°C, progressive increase that peaks at 40°C, high activity at 50°C, inactivation above 60°C
20 - 80
-
20% of maximal activity at 20°C, progressive increase that peaks at 70°C, 30% of maximal activity at 80°C
20 - 90
-
20% of maximal activity at 20°C, progressive increase that peaks at 60°C, 5% of maximal activity at 90°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme TGG2; ecotype Columbia, Col-0, isozyme TGG2, gene tgg2
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
low expression of isoform TGG1, no expression of isoform TGG2. Monitoring of the levels of glucosinolates
-
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
-
hypocotyl of seedling, high expression of isoform TGG1, no expression of isoform TGG2
-
myrosin cells are different from companion cells and the glucosinolate-containing S-cells
-
hypocotyl of seedling, high expression of isoform TGG1, no expression of isoform TGG2
additional information
-
enzyme activity is restricted to guard cells and phloem idioblasts
TGG1 is a strikingly abundant protein in guard cells
TGG1 is highly abundant in guard cells of leaves
TGG1 is cell type-specific expressed in specialized myrosin cells
-
enzyme activity is restricted to guard cells and phloem idioblasts
additional information
TGG2 accumulates abnormally in mns mutants
additional information
TGG2 accumulates abnormally in mns mutants
additional information
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
additional information
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
additional information
-
no myrosin cells are detected in the ground tissue
additional information
TGG1 accumulates abnormally in mns mutants
additional information
TGG1 accumulates abnormally in mns mutants
additional information
-
distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression
additional information
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
additional information
isozyme TGG1 is expressed in guard cells and phloem cells and and isozyme TGG1 protein is highly abundant in guard cells. In contrast, TGG2 is only expressed in phloem-associated cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
endoplasmic reticulum (ER) bodies in Arabidopsis thaliana contain large amounts of beta-glucosidases, and PYK10 is the most abundant beta-glucosidase in root ER bodies
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the tgg1, single and tgg1 tgg2 double mutants show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
physiological function
evolution
malfunction
metabolism
physiological function
additional information
physiological function
myrosinase TGG2 redundantly functions in abscisic acid and methyl jasmonate signaling in guard cells
physiological function
Brassicaceae, including Arabidopsis thaliana and Brassica crop species comprise the glucosinolate-myrosinase system, in which myrosinase thioglucosidase (TGG) catalyses glucosinolate breakdown into various biologically active molecules upon tissue disruption or insect attac. The glucosinolate-myrosinase system represents a chemical-based plant defence system. A close association between chemical defence systems and physical defence barriers, represented by the cuticle, exists
physiological function
glucosinolate-myrosinase is a substrate-enzyme defense mechanism present in Brassica crops. This binary system provides the plant with an efficient system against herbivores and pathogens. Glucosinolate and myrosinase are spatially present in different cells that upon tissue disruption come together and result in the formation of a variety of hydrolysis products with diverse physicochemical and biological properties. The myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain, the presence of supplementary proteins known as specifier proteins and/or on the physiochemical condition
evolution
-
in silico three-dimensional modeling, combined with phylogenomic analysis, suggests that PYK10 represents a clade of 16 myrosinases that arose independently from the other well-documented class of six thioglucoside glucohydrolases. Phylogenomic and three-dimensional structural modeling analysis identified the presence of two independent classes of myrosinases, represented by PYK10/PEN2 and thioglucoside glucohydrolases (TGGs). Analysis of evolutionary origin of myrosinases, overview. Gene modules composed of IG modification, hydrolysis and catabolism genes may facilitate a functional differentiation among myrosinases
evolution
most of the MYR I clustered myrosinase genes use GC-AG intron splice donor site for intron 1 whereas TGG4, TGG5, and TGG6 of Arabidopsis thaliana (AtTGG4-6) and Arabidopsis lyrata (AlTGG4-6) genes in the MYR II cluster contain a GC-AG splice donor for intron 10. AtTGG5 also has a GC splice donor site for intron 3
evolution
-
myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC)
malfunction
-
the degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates
malfunction
the classic myrosinase beta-thioglucoside glucohydrolase (TGG)-deficient double mutant tgg1 tgg2, rather than atypical myrosinase-deficient mutant pen2-2, is more sensitive to the mycotoxin fumonisin B1 (FB1) than wild-type Col-0, and the elevated expression of isozyme TGG1, but not of PEN2, correlates with the decrease in indole glucosinolate (IGS), TGG-dependent IGS hydrolysis is involved in FB1-induced programmed cell death (PCD)
malfunction
the tgg1, single and tgg1 tgg2 double mutants show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
metabolism
metabolism of tryptophan-derived indole glucosinolate (IGS), camalexin and indol-3-acetic acid (IAA) as well as methioninederived aliphatic glucosinolate (AGS) in Arabidopsis thaliana involving the myrosinase enzymes TGG1 and PEN2, overview
metabolism
metabolism of tryptophan-derived indole glucosinolate (IGS), camalexin and indole-3-acetic acid (IAA) as well as methioninederived aliphatic glucosinolate (AGS) in Arabidopsis thaliana involving the myrosinase enzymes TGG1 and PEN2, overview. FB1-induced biosynthesis of glucosinolates. FB1 treatment triggers not only biosynthesis but also hydrolysis of IGS
physiological function
myrosinase TGG1 redundantly functions in abscisic acid and methyl jasmonate signaling in guard cells
physiological function
-
the enzyme is part of the glucosinolate-myrosinase defense system, physiological role of glucosinolate induction and enzyme induction, overview
physiological function
-
myrosinase is part of the plant chemical defense system (glucosinolate-myrosinase system). Upon tissue disruption, bioactivation of glucosinolates is initiated, i.e. myrosinases get access to their glucosinolate substrates, and glucosinolate hydrolysis results in the formation of toxic isothiocyanates and other biologically active products
physiological function
Brassicaceae, including Arabidopsis thaliana and Brassica crop species comprise the glucosinolate-myrosinase system, in which myrosinase thioglucosidase (TGG) catalyses glucosinolate breakdown into various biologically active molecules upon tissue disruption or insect attac. The glucosinolate-myrosinase system represents a chemical-based plant defence system. A close association between chemical defence systems and physical defence barriers, represented by the cuticle, exists
physiological function
classical TGG-dependent hydrolysis of indole glucosinolate (IGS) restricts FB1-induced programmed cell death (PCD). Mycotoxin fumonisin B1 (FB1) causes the accumulation of reactive oxygen species (ROS) which then leads to PCD in Arabidopsis thaliana. FB1-induced biosynthesis of glucosinolates. FB1 treatment triggers not only biosynthesis but also hydrolysis of IGS
physiological function
glucosinolate-myrosinase is a substrate-enzyme defense mechanism present in Brassica crops. This binary system provides the plant with an efficient system against herbivores and pathogens. Glucosinolate and myrosinase are spatially present in different cells that upon tissue disruption come together and result in the formation of a variety of hydrolysis products with diverse physicochemical and biological properties. The myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain, the presence of supplementary proteins known as specifier proteins and/or on the physiochemical condition
physiological function
-
plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overview. Other proteins can interact with the myrosinase forming myrosinase-binding proteins (MBPs) and myrosinase associated proteins (MyAP). They have been identified as complexes contributing to the plant defense system in different Brassica species such as Brassica napus or Arabidopsis thaliana. Three-dimensional analysis of the structure of this complex shows that the protein does not show affinity for sugar structures to link N-glycan, but a weak affinity for starch or glycolipid involved the lectin activity of the MBP family in the interaction between the myrosinase complex and other molecules. Important role of the myrosinase activity in guard cells of Arabidopsis plants. Water stress increases abscisic acid levels that enhance glucosinolates delivery from the vacuole, myrosinase activity or its substrate affinity. Hydrolyzed products of glucosinolates may induce inward K+-channel activity resulting in stomata closure
physiological function
-
PYK10, the most abundant beta-glucosidase in Arabidopsis thaliana root endoplasmic reticulum (ER) bodies, hydrolyzes indole glucosinolates (IGs) in addition to the previously reported in vitro substrate scopolin. PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in Arabidopsis thaliana. Variation of the myrosinase-glucosinolate system exists within individual plants. The co-expressed gene cluster of PYK10 is enriched in genes required for the production of glucosinolates. Glucosinolates are in planta substrates for PYK10 that are tightly linked to the physiological functions of ER bodies. ER bodies are potentially engaged in plant-microbe interactions via indole glucosinolate metabolism and in abiotic stress responses via coumarin metabolism
additional information
the enzyme is sensitive to endoglycosidase digestion
additional information
the enzyme is sensitive to endoglycosidase digestion
additional information
the enzyme is sensitive to endoglycosidase digestion
additional information
the enzyme is sensitive to endoglycosidase digestion
additional information
the cyp79B2 cyp79B3 mutant, which has a greatly reduced level of indole glucosinolates, is more sensitive to mycotoxin fumonisin B1 (FB1)
additional information
the cyp79B2 cyp79B3 mutant, which has a greatly reduced level of indole glucosinolates, is more sensitive to mycotoxin fumonisin B1 (FB1)
additional information
-
three-dimensional analysis of the structure of the enzyme-myrosinase-binding protein (MBP) complex in Arabidopsis thaliana shows that the protein does not show affinity for sugar structures to link N-glycan, but a weak affinity for starch or glycolipid involved the lectin activity of the MBP family in the interaction between the myrosinase complex and other molecules
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BGL37_ARATH
547
1
62732
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
126000
62700
x * 63000, glycosylated enzyme TGG2, SDS-PAGE, x * 62700, deglycosylated enzyme TGG2, SDS-PAGE
63000
x * 63000, glycosylated enzyme TGG2, SDS-PAGE, x * 62700, deglycosylated enzyme TGG2, SDS-PAGE
150000
61100
x * 75000, glycosylated enzyme TGG1, SDS-PAGE, x * 61100, deglycosylated enzyme TGG1, SDS-PAGE
75000
x * 75000, glycosylated enzyme TGG1, SDS-PAGE, x * 61100, deglycosylated enzyme TGG1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 63000, glycosylated enzyme TGG2, SDS-PAGE, x * 62700, deglycosylated enzyme TGG2, SDS-PAGE
?
x * 75000, glycosylated enzyme TGG1, SDS-PAGE, x * 61100, deglycosylated enzyme TGG1, SDS-PAGE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycoprotein
all four potential N-glycosylation sites are subjected to glycosylation and are occupied by oligomannosidic structures with Man5GlcNAc2 as the main oligosaccharide, found on the majority of TGG1 glycopeptides. In addition, Man6GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2 are also present on several glycosylation sites, while on Asn108 the predominant peak corresponds to Man9Glc-NAc2. TGG2 N-glycans are not altered in the mvp1 mutant
glycoprotein
deglycosylation under nondenaturing conditions has no effect on TGG2 activity
glycoprotein
deglycosylation does not affect TGG2 activity
glycoprotein
all nine potential N-glycosylation sites are subjected to glycosylation and are occupied by oligomannosidic structures with Man5GlcNAc2 as the main oligosaccharide, found on the majority of TGG1 glycopeptides. In addition, Man6GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2 are also present on several glycosylation sites, while on Asn108 the predominant peak corresponds to Man9Glc-NAc2. TGG1 from mns mutants displays incompletely processed oligomannosidic N-glycans, while TGG1 N-glycans are not altered in the mvp1 mutant
glycoprotein
deglycosylation under nondenaturing conditions has limited effect on TGG1 activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of isozyme mutants, tgg1-3, tgg2-1, and tgg1-3/tgg2-1. Abscisic acid, methyl jasmonate, and H2O2 induce stomatal closure in wild type, tgg1-3 and tgg2-1, but fail to induce stomatal closure in tgg1-3 tgg2-1. All mutants and wild-type show Ca2+-induced stomatal closure and abscisic acid-induced reactive oxygen species production
additional information
construction of isozyme mutants, tgg1-3, tgg2-1, and tgg1-3/tgg2-1. Abscisic acid, methyl jasmonate, and H2O2 induce stomatal closure in wild type, tgg1-3 and tgg2-1, but fail to induce stomatal closure in tgg1-3 tgg2-1. All mutants and wild-type show Ca2+-induced stomatal closure and abscisic acid-induced reactive oxygen species production
additional information
generation of tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg2 single mutant, the pavement cells appear bigger compared to wild-type, flattened and show an irregular jigsaw puzzle shape. Stomata in the tgg2 single mutant are also relatively bigger than the wild-type, and the stomatal aperture is mostly fully open. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
generation of tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg2 single mutant, the pavement cells appear bigger compared to wild-type, flattened and show an irregular jigsaw puzzle shape. Stomata in the tgg2 single mutant are also relatively bigger than the wild-type, and the stomatal aperture is mostly fully open. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
-
construction of isoform TGG1 and TGG2 single and double mutants. Glucosinolate breakdown in leaves of single mutant plants is comparable to wild-type, whereas the double mutant exhibits no catalytic activity in vitro and dmage-induce breakdown of endogenous glucosinolates is apparently absent for aliphatic and greatly slowed down for indole glucosinolates. Mature leaves of mutants have increased glucosinolate levels, but developmental decreases in glucosinolate content during senescence and germination are unaffected. Insect herbivores vary in their respones to mutants. Weight gain of Trichoplusia ni and Manduca sexta is significantly increased upon feeding with mutant leaves, while reproduction of Myzus persicae and Brevicoryne brassica is unaffected
additional information
construction of isozyme mutants, tgg1-3, tgg2-1, and tgg1-3/tgg2-1. Abscisic acid, methyl jasmonate, and H2O2 induce stomatal closure in wild type, tgg1-3 and tgg2-1, but fail to induce stomatal closure in tgg1-3 tgg2-1. All mutants and wild-type show Ca2+-induced stomatal closure and abscisic acid-induced reactive oxygen species production
additional information
construction of isozyme mutants, tgg1-3, tgg2-1, and tgg1-3/tgg2-1. Abscisic acid, methyl jasmonate, and H2O2 induce stomatal closure in wild type, tgg1-3 and tgg2-1, but fail to induce stomatal closure in tgg1-3 tgg2-1. All mutants and wild-type show Ca2+-induced stomatal closure and abscisic acid-induced reactive oxygen species production
additional information
generation of tgg1, single and tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg1 single mutant, the pavement cells are bigger in size, but still showing a regular jigsaw puzzle shape as in the wild-type. The stomata in the tgg1 single mutant also appear bigger. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
generation of tgg1, single and tgg1 tgg2 double mutants which show morphological changes compared to wild-type plants visible as changes in pavement cells, stomatal cells and the ultrastructure of the cuticle. Extensive metabolite analyses of leaves from tgg mutants and wild-type Arabidopsis plants show altered levels of cuticular fatty acids, fatty acid phytyl esters, glucosinolates, and indole compounds in tgg single and double mutants as compared to wild-type plants. No macroscopic growth/morphological differences are observed between the wild-type and tgg single and double mutants during during the four weeks of plant cultivation. In the tgg1 single mutant, the pavement cells are bigger in size, but still showing a regular jigsaw puzzle shape as in the wild-type. The stomata in the tgg1 single mutant also appear bigger. The pavement cells in the tgg1 tgg2 double mutant appear deformed, overlapping each other, collapse in some places, and hence show an irregular jigsaw puzzle shape. Additionally, in the tgg1 tgg2 double mutant, smaller, tightly closed and sunken stomata are observed. Wild-type, tgg1, tgg2 single mutants, and tgg1 tgg2 double mutant differ significantly for guard cell length. However, for guard cell width, only wild-type and tgg1 single mutant show significant differences. In the wild-type, hardly any wax crystals are observed, while a relatively higher amount of wax crystals is observed on the leaf surfaces of the tgg mutants, in particular for the tgg2 single mutant, and the tgg1 tgg2 double mutant. In both tgg single and double mutants the cuticle appear as disrupted with reduced electron density and appear to be discontinuous. The tgg mutations alter levels of glucosinolates. Among the nine glucosinolates detected, eight show reduced levels in the tgg1 tgg2 double mutant. Glucoerucin is the only glucosinolate that shows higher levels in tgg1 tgg2 double mutant compared to the tgg1 and tgg2 single mutants, while tgg1 and tgg2 single mutants show moderate to high levels for glucosinolates glucoiberin, glucoraphanin, glucoalyssin, glucoibarin, glucohirsutin, hexyl glucosinolate, and glucobrassicin as compared to the wild-type
additional information
mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
the costructed tgg1 tgg2 double mutant, which has greatly reduced TGG activity, shows more severe lesion formation and cell death symptoms than Col-0. Mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
additional information
the costructed tgg1 tgg2 double mutant, which has greatly reduced TGG activity, shows more severe lesion formation and cell death symptoms than Col-0. Mutant pen2-2, the mutant of atypical myrosinase PEN2 with highly reduced enzyme activity, shows fewer lesions compared with myrosinase double mutant tgg1 tgg2 and exhibits a symptoms similar to the wild-type in response to mycotoxin fumonisin B1 (FB1), indicating that deficiency of TGG instead of PEN2 renders plants significantly more sensitive to FB1
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 10.3
the purified recombinant enzyme TGG1 retains more than 50% of their maximal activity in buffers with pH values ranging from 4.8 to 10.3
732658
4.8 - 11
the purified recombinant enzyme TGG1 retains more than 50% of their maximal activity in buffers with pH values ranging from 4.8 to 11.0
732658
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 55
purified recombinant enzyme TGG2, retains over 70% activity at temperatures between 4°C and 55°C for 30 min
95
purified recombinant enzyme, 10 min, pH 5.8, inactivation
4 - 55
purified recombinant enzyme TGG1, retains over 70% activity at temperatures between 4°C and 55°C for 30 min
95
purified recombinant enzyme, 10 min, pH 5.8, inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TGG2 84.2fold from from T-DNA insertion lines of Arabidopsis using lectin affinity and anion exchange chromatography
recombinant His-tagged root isozymes TGG4 and TGG5 and His-tagged leaf isozyme TGG1 from Pichia pastoris by nickel affinity chromatography to homogeneity
-
TGG1 51.9fold from from T-DNA insertion lines of Arabidopsis using lectin affinity and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tgg2, recombinant expression of TGG2, sequence comparisons
gene tgg1, exxpression of recombinant TGG1, sequence comparisons
overexpression of His-tagged root isozymes TGG4 and TGG5 and His-tagged leaf isozyme TGG1 in Pichia pastoris
-
overexpression of nitrile-specifier protein 2, NSP2, in transgenic Arabidopsis thaliana plants leading to increased nitrile production
-
phylogenetic analysis and tree, recombinant expression of wild-type and mutant enzymes
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
TGG1 transcript levels are higher in leaves of mns1 mns2 mns3 plants
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
-
water stress increases abscisic acid levels that enhanced glucosinolates delivery from the vacuole, myrosinase activity or its substrate affinity
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Andreasson, E.; Bolt Jorgensen, L.; Hoeglund, A.S.; Rask, L.; Meijer, J.
Different myrosinase and idioblast distribution in Arabidopsis and Brassica napus
Plant Physiol.
127
1750-1763
2001
Arabidopsis thaliana, Brassica napus
Husebye, H.; Chadchawan, S.; Winge, P.; Thangstad, O.P.; Bones, A.M.
Guard cell- and phloem idioblast-specific expression of thioglucoside glucohydrolase 1 (myrosinase) in Arabidopsis
Plant Physiol.
128
1180-1188
2002
Arabidopsis thaliana
Alvarez, S.; He, Y.; Chen, S.
Comparative investigations of the glucosinolate-myrosinase system in Arabidopsis suspension cells and hypocotyls
Plant Cell Physiol.
49
324-333
2008
Arabidopsis thaliana
Barth, C.; Jander, G.
Arabidopsis myrosinases TGG1 and TGG2 have redundant function in glucosinolate breakdown and insect defense
Plant J.
46
549-562
2006
Arabidopsis thaliana
Kissen, R.; Bones, A.M.
Nitrile-specifier proteins involved in glucosinolate hydrolysis in Arabidopsis thaliana
J. Biol. Chem.
284
12057-12070
2009
Arabidopsis thaliana
Textor, S.; Gershenzon, J.
Herbivore induction of the glucosinolate-myrosinase defense system: major trends, biochemical bases and ecological significance
Phytochem. Rev.
8
149-170
2009
Arabidopsis thaliana, Brassica rapa subsp. oleifera, Brassica juncea, Brassica napus, Brassica nigra, Brassica oleracea, Brassica rapa, Carica papaya, Raphanus sativus, Raphanus raphanistrum, Sinapis alba, Tropaeolum majus, Athalia rosae, Lepidium virginicum
-
Andersson, D.; Chakrabarty, R.; Bejai, S.; Zhang, J.; Rask, L.; Meijer, J.
Myrosinases from root and leaves of Arabidopsis thaliana have different catalytic properties
Phytochemistry
70
1345-1354
2009
Arabidopsis thaliana
Islam, M.M.; Tani, C.; Watanabe-Sugimoto, M.; Uraji, M.; Jahan, M.S.; Masuda, C.; Nakamura, Y.; Mori, I.C.; Murata, Y.
Myrosinases, TGG1 and TGG2, redundantly function in ABA and MeJA signaling in Arabidopsis guard cells
Plant Cell Physiol.
50
1171-1175
2009
Arabidopsis thaliana (P37702), Arabidopsis thaliana (Q9C5C2)
Winde, I.; Wittstock, U.
Insect herbivore counteradaptations to the plant glucosinolate-myrosinase system
Phytochemistry
72
1566-1575
2011
Arabidopsis thaliana, Sinapis alba, Sinapis arvensis, Tropaeolum majus, Arabis hirsuta, Arabis soyeri
Liebminger, E.; Grass, J.; Jez, J.; Neumann, L.; Altmann, F.; Strasser, R.
Myrosinases TGG1 and TGG2 from Arabidopsis thaliana contain exclusively oligomannosidic N-glycans
Phytochemistry
84
24-30
2012
Arabidopsis thaliana (P37702), Arabidopsis thaliana (Q9C5C2), Arabidopsis thaliana Columbia-0 (P37702), Arabidopsis thaliana Columbia-0 (Q9C5C2)
Zhou, C.; Tokuhisa, J.G.; Bevan, D.R.; Esen, A.
Properties of beta-thioglucoside hydrolases (TGG1 and TGG2) from leaves of Arabidopsis thaliana
Plant Sci.
191-192
82-92
2012
Arabidopsis thaliana (P37702), Arabidopsis thaliana (Q9C5C2), Arabidopsis thaliana
Bhat, R.; Vyas, D.
Myrosinase insights on structural, catalytic, regulatory, and environmental interactions
Crit. Rev. Biotechnol.
39
508-523
2019
Arabidopsis thaliana (P37702), Arabidopsis thaliana (Q3ECS3), Arabidopsis thaliana (Q8GRX1), Arabidopsis thaliana (Q9C5C2), Armoracia rusticana (Q5PXK2), Aspergillus niger, Aspergillus sydowii, Brassica juncea (Q9ZP01), Brassica napus (Q42629), Brassica napus (Q9STD7), Brassica oleracea var. italica (A0A343IQS8), Brevicoryne brassicae (Q95X01), Brevicoryne brassicae, Capparis spinosa var. ovata, Carica papaya (C9WCQ0), Carica papaya (C9WCQ1), Crambe hispanica subsp. abyssinica, Enterobacter cloacae, Enterococcus casseliflavus, Enterococcus casseliflavus CP1, Escherichia coli, Escherichia coli VL8, Eutrema halophilum, Eutrema japonicum (Q4AE75), Lepidium latifolium, Lepidium sativum, Ligilactobacillus agilis, Ligilactobacillus agilis R16, Raphanus sativus (V9PVN6), Sinapis alba (P29736)
Martinez-Ballesta, M.; Carvajal, M.
Myrosinase in Brassicaceae the most important issue for glucosinolate turnover and food quality
Phytochem. Rev.
14
1045-1051
2015
Arabidopsis thaliana, Brassica rapa subsp. pekinensis, Brassica napus, Brassica rapa, Raphanus sativus, Sinapis alba, Brassica oleracea var. alboglabra, Thellungiella
-
Zhao, Y.; Wang, J.; Liu, Y.; Miao, H.; Cai, C.; Shao, Z.; Guo, R.; Sun, B.; Jia, C.; Zhang, L.; Gigolashvili, T.; Wang, Q.
Classic myrosinase-dependent degradation of indole glucosinolate attenuates fumonisin B1-induced programmed cell death in Arabidopsis
Plant J.
81
920-933
2015
Arabidopsis thaliana (O64883), Arabidopsis thaliana (P37702), Arabidopsis thaliana Col-0 (O64883), Arabidopsis thaliana Col-0 (P37702)
Nakano, R.T.; Pislewska-Bednarek, M.; Yamada, K.; Edger, P.P.; Miyahara, M.; Kondo, M.; Boettcher, C.; Mori, M.; Nishimura, M.; Schulze-Lefert, P.; Hara-Nishimura, I.; Bednarek, P.
PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in Arabidopsis thaliana
Plant J.
89
204-220
2017
Arabidopsis thaliana
Ahuja, I.; de Vos, R.C.; Rohloff, J.; Stoopen, G.M.; Halle, K.K.; Ahmad, S.J.; Hoang, L.; Hall, R.D.; Bones, A.M.
Arabidopsis myrosinases link the glucosinolate-myrosinase system and the cuticle
Sci. Rep.
6
38990
2016
Arabidopsis thaliana (P37702), Arabidopsis thaliana (Q9C5C2), Arabidopsis thaliana Col-0 (P37702), Arabidopsis thaliana Col-0 (Q9C5C2)
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