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Literature summary for 3.2.1.147 extracted from
- Myrosinase insights on structural, catalytic, regulatory, and environmental interactions (2019), Crit. Rev. Biotechnol., 39, 508-523 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Aspergillus sydowii |  |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Crambe hispanica subsp. abyssinica | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Armoracia rusticana | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Lepidium latifolium | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Brassica napus | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Eutrema halophilum | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Arabidopsis thaliana | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Carica papaya | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Brassica oleracea var. italica | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Brassica juncea | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Eutrema japonicum | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid | Capparis spinosa var. ovata | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid, mechanism of ascorbic acid activation, overview | Sinapis alba | |
| ascorbic acid | all the plant myrosinases are reported to be activated by ascorbic acid, uncompetitive activation by ascorbic acid | Raphanus sativus | |
| ascorbic acid | dependent on, all the plant myrosinases are reported to be activated by ascorbic acid | Lepidium sativum | |
| additional information | isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity | Carica papaya | |
| additional information | no effect on activity by ascorbic acid | Aspergillus niger | |
| additional information | redox-regulated, the reduced form is more active | Lepidium latifolium |
General Stability
| General Stability | Organism |
|---|---|
| the enzyme is heat and pressure sensitive | Brassica oleracea var. italica |
| the enzyme is stable only in presence of 2-mercapethanol and ascorbic acid | Aspergillus niger |
| the enzyme is temperature sensitive but quite pressure stable | Sinapis alba |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-deoxy-glucotropaeolin | a strong competitive inhibitor | Sinapis alba | |
| ascorbic acid | inhibits the enzyme, ascorbic acid addition resulted in production of hydroxylated degradation products | Brevicoryne brassicae | |
| ascorbic acid | - |
Enterobacter cloacae | |
| castanospermine | the alkaloidal glycosidase inhibitor acts as competitive inhibitor | Lepidium sativum | |
| Cu2+ | - |
Enterobacter cloacae | |
| D-glucose | inhibits at 5 mM | Lepidium latifolium | |
| delta-gluconolactone | - |
Aspergillus niger | |
| EDTA | strong inhibition | Enterobacter cloacae | |
| Fe2+ | - |
Enterobacter cloacae | |
| Hg2+ | - |
Aspergillus niger | |
| Hg2+ | - |
Enterobacter cloacae | |
| additional information | no effect on activity by ascorbic acid | Aspergillus niger | |
| additional information | sugars and glucosides act as competitive inhibitors | Brassica juncea | |
| additional information | the enzyme shows substrate inhibition via a binding site mechanisms, and is sensitive against heat and pressure | Brassica oleracea var. italica | |
| Sn2+ | - |
Aspergillus niger | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the Km value of the fungus myrosinase is 20fold higher compared to the non-activated plant myrosinase | Aspergillus sydowii |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates | Aspergillus niger | |
| Cu2+ | activates | Aspergillus niger | |
| Mg2+ | - |
Escherichia coli | |
| Mg2+ | - |
Enterococcus casseliflavus | |
| Mg2+ | - |
Ligilactobacillus agilis | |
| Mn2+ | activates | Aspergillus niger | |
| additional information | Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production | Escherichia coli | |
| additional information | Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production | Enterococcus casseliflavus | |
| additional information | Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production | Ligilactobacillus agilis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 120000 | - |
- |
Brevicoryne brassicae |
| 120000 | - |
- |
Raphanus sativus |
| 124000 | - |
about | Arabidopsis thaliana |
| 126000 | - |
- |
Arabidopsis thaliana |
| 130000 | - |
- |
Lepidium sativum |
| 130000 | - |
- |
Armoracia rusticana |
| 130000 | - |
- |
Arabidopsis thaliana |
| 135000 | - |
- |
Sinapis alba |
| 150000 | - |
- |
Arabidopsis thaliana |
| 156000 | - |
- |
Brassica napus |
| 157000 | - |
- |
Brassica oleracea var. italica |
| 160000 | - |
- |
Lepidium latifolium |
| 188000 | - |
- |
Brassica napus |
| 470000 | - |
- |
Crambe hispanica subsp. abyssinica |
| 580000 | - |
- |
Eutrema japonicum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| 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 | isozyme 1 | - |
| 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 | - |
isozymes TGG1 and TGG2 | - |
| Eutrema japonicum | Q4AE75 | i.e. Wasabia japonica | - |
| Lepidium latifolium | - |
- |
- |
| Lepidium sativum | - |
- |
- |
| Ligilactobacillus agilis | - |
- |
- |
| Ligilactobacillus agilis R16 | - |
- |
- |
| Raphanus sativus | V9PVN6 | - |
- |
| Sinapis alba | P29736 | isozyme MA1 | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Arabidopsis thaliana |
| glycoprotein | deglycosylation affects TGG1 activity | Arabidopsis thaliana |
| glycoprotein | deglycosylation does not affect TGG2 activity | Arabidopsis thaliana |
| glycoprotein | the isoforms differ in carbohydrate content | Brassica napus |
| no glycoprotein | - |
Brevicoryne brassicae |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme | Brevicoryne brassicae |
| native enzyme from leaves | Lepidium latifolium |
| native enzyme from roots | Armoracia rusticana |
| native enzyme from roots | Eutrema japonicum |
| native enzyme from seedlings or roots | Raphanus sativus |
| native enzyme from seedlings or seeds | Lepidium sativum |
| native enzyme from seedlings, partially from seed | Brassica napus |
| native enzyme from seeds | Crambe hispanica subsp. abyssinica |
| native enzyme from seeds | Sinapis alba |
| native enzyme from sprouts | Brassica oleracea var. italica |
| native enzyme partially | Aspergillus sydowii |
| native isozyme CpTGG1 from leaves | Carica papaya |
| native isozyme CpTGG2 from roots | Carica papaya |
| native isozyme TGG1 from leaves | Arabidopsis thaliana |
| native isozyme TGG2 from leaves | Arabidopsis thaliana |
| native isozyme TGG4 from roots | Arabidopsis thaliana |
| native isozyme TGG5 from roots | Arabidopsis thaliana |
| partial purification of the seed enzyme | Brassica juncea |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a thioglucoside + H2O = a sugar + a thiol | reaction mechanism | Sinapis alba |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| flower | - |
Eutrema halophilum | - |
| flower | - |
Capparis spinosa var. ovata | - |
| leaf | - |
Lepidium latifolium | - |
| leaf | - |
Eutrema halophilum | - |
| leaf | - |
Arabidopsis thaliana | - |
| leaf | - |
Carica papaya | - |
| leaf | - |
Capparis spinosa var. ovata | - |
| additional information | the TGG2 orthologue is present in different organs, but not in roots | Capparis spinosa var. ovata | - |
| petiole | - |
Eutrema halophilum | - |
| root | - |
Armoracia rusticana | - |
| root | - |
Eutrema halophilum | - |
| root | - |
Carica papaya | - |
| root | - |
Raphanus sativus | - |
| root | - |
Arabidopsis thaliana | - |
| root | - |
Eutrema japonicum | - |
| seed | - |
Crambe hispanica subsp. abyssinica | - |
| seed | - |
Sinapis alba | - |
| seed | - |
Brassica juncea | - |
| seedling | - |
Lepidium sativum | - |
| seedling | - |
Brassica napus | - |
| seedling | - |
Raphanus sativus | - |
| sprout | - |
Brassica oleracea var. italica | - |
| stem | - |
Capparis spinosa var. ovata | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| epigoitrin + H2O | - |
Crambe hispanica subsp. abyssinica | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Aspergillus niger | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Enterobacter cloacae | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Aspergillus sydowii | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Lepidium sativum | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Enterococcus casseliflavus | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Armoracia rusticana | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Lepidium latifolium | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Eutrema halophilum | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Arabidopsis thaliana | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Carica papaya | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Sinapis alba | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Brevicoryne brassicae | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Brassica oleracea var. italica | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Raphanus sativus | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Brassica juncea | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Eutrema japonicum | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Capparis spinosa var. ovata | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Ligilactobacillus agilis | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Ioszyme MYRI is maximally active against aliphatic glucosinolate followed by aromatic glucosinolates, and indole glucosinolates | Brassica napus | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Ioszyme MYRII is maximally active against aliphatic glucosinolate followed by aromatic glucosinolates, and indole glucosinolates | Brassica napus | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. The enzyme from Crambe abyssinica is highly specific for epi-progoitrin | Crambe hispanica subsp. abyssinica | ? | - |
? | |
| additional information | myrosinase in general catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates. Isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity | Carica papaya | ? | - |
? | |
| additional information | the enzyme produces nitriles from desulfoglucosinolates | Escherichia coli | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Ligilactobacillus agilis R16 | ? | - |
? | |
| additional information | the enzyme produces nitriles from desulfoglucosinolates | Escherichia coli VL8 | ? | - |
? | |
| additional information | myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates | Enterococcus casseliflavus CP1 | ? | - |
? | |
| progoitrin + H2O | - |
Crambe hispanica subsp. abyssinica | (1E,3S)-3-hydroxy-n-(sulfooxy)pent-4-enimidothioic acid + D-glucose | - |
? | |
| sinigrin + H2O | - |
Crambe hispanica subsp. abyssinica | (1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose | - |
? | |
| sinigrin + H2O | best substrate | Brevicoryne brassicae | (1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 65000 | Capparis spinosa var. ovata |
| ? | x * 65000, isozyme CpTGG2 | Carica papaya |
| ? | x * 70000, isozyme CpTGG1 | Carica papaya |
| dimer | 2 * 70000 | Lepidium latifolium |
| dimer | 2 * 75000 | Brassica napus |
| dimer | 2 * 75000 | Arabidopsis thaliana |
| dimer | 2 * 65000 | Armoracia rusticana |
| dimer | 2 * 65000 | Arabidopsis thaliana |
| dimer | 2 * 62000 | Arabidopsis thaliana |
| dimer | 2 * 57000-60000 | Brevicoryne brassicae |
| dimer | 2 * 61000-62000 | Raphanus sativus |
| dimer | 2 * 62000-65000 | Lepidium sativum |
| dimer | 2 * 63000 | Arabidopsis thaliana |
| dimer | 2 * 71700 | Sinapis alba |
| dimer or trimer | x * 62000 | Brassica napus |
| dodecamer | 12 * 45000-47000 | Eutrema japonicum |
| More | existence of different oligomeric states in different redox environments | Lepidium latifolium |
| More | the enzyme contains about 19% alpha-helix and 35% beta-sheets, the rest being conformationally aperiodic | Sinapis alba |
| oligomer | x * 75000 | Crambe hispanica subsp. abyssinica |
| trimer | 50000-55000 | Brassica oleracea var. italica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-thioglucosidase | - |
Brevicoryne brassicae |
| beta-thioglucosidase glucohydrolase | - |
Brevicoryne brassicae |
| beta-thioglucoside glucohydrolase | - |
Carica papaya |
| CpTGG1 | - |
Carica papaya |
| CpTGG2 | - |
Carica papaya |
| Myr1.Bn1 | - |
Brassica napus |
| Myr2.Bn1 | - |
Brassica napus |
| MYRI | - |
Brassica napus |
| MYRII | - |
Brassica napus |
| myrosinase | - |
Escherichia coli |
| myrosinase | - |
Aspergillus niger |
| myrosinase | - |
Enterobacter cloacae |
| myrosinase | - |
Aspergillus sydowii |
| myrosinase | - |
Lepidium sativum |
| myrosinase | - |
Crambe hispanica subsp. abyssinica |
| myrosinase | - |
Enterococcus casseliflavus |
| myrosinase | - |
Armoracia rusticana |
| myrosinase | - |
Lepidium latifolium |
| myrosinase | - |
Brassica napus |
| myrosinase | - |
Eutrema halophilum |
| myrosinase | - |
Arabidopsis thaliana |
| myrosinase | - |
Carica papaya |
| myrosinase | - |
Sinapis alba |
| myrosinase | - |
Brevicoryne brassicae |
| myrosinase | - |
Brassica oleracea var. italica |
| myrosinase | - |
Raphanus sativus |
| myrosinase | - |
Brassica juncea |
| myrosinase | - |
Eutrema japonicum |
| myrosinase | - |
Capparis spinosa var. ovata |
| myrosinase | - |
Ligilactobacillus agilis |
| sinigrinase | - |
Brevicoryne brassicae |
| TGG1 | - |
Arabidopsis thaliana |
| TGG2 | - |
Arabidopsis thaliana |
| TGG4 | - |
Arabidopsis thaliana |
| TGG5 | - |
Arabidopsis thaliana |
| WjMYR | - |
Eutrema japonicum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Raphanus sativus |
| 37 | - |
- |
Eutrema japonicum |
| 37 | - |
substrate epigoitrin | Crambe hispanica subsp. abyssinica |
| 37 | 45 | - |
Armoracia rusticana |
| 40 | - |
- |
Brevicoryne brassicae |
| 40 | - |
- |
Brassica oleracea var. italica |
| 40 | - |
isozyme CpTGG1 | Carica papaya |
| 40 | - |
isozyme CpTGG2 | Carica papaya |
| 50 | - |
- |
Lepidium latifolium |
| 50 | - |
- |
Arabidopsis thaliana |
| 50 | - |
substrate sinigrin | Crambe hispanica subsp. abyssinica |
| 55 | - |
- |
Brassica napus |
| 60 | - |
- |
Arabidopsis thaliana |
| 70 | - |
- |
Arabidopsis thaliana |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
low pressure retards thermal inactivation | Brassica oleracea var. italica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | - |
- |
Brassica oleracea var. italica |
| 5 | 6 | - |
Brassica napus |
| 5.5 | - |
- |
Lepidium sativum |
| 5.5 | - |
- |
Arabidopsis thaliana |
| 5.5 | 6 | - |
Brassica napus |
| 5.5 | 10.5 | - |
Arabidopsis thaliana |
| 5.7 | - |
- |
Armoracia rusticana |
| 6 | 6.5 | - |
Raphanus sativus |
| 6 | - |
- |
Lepidium latifolium |
| 6 | - |
- |
Arabidopsis thaliana |
| 6.5 | - |
substrate epigoitrin | Crambe hispanica subsp. abyssinica |
| 6.5 | 7.7 | - |
Eutrema japonicum |
| 7.5 | - |
isozyme CpTGG1 | Carica papaya |
| 7.5 | - |
substrate sinigrin | Crambe hispanica subsp. abyssinica |
| 8 | - |
isozyme CpTGG2 | Carica papaya |
| 8.5 | - |
substrate progoitrin | Crambe hispanica subsp. abyssinica |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 7.5 | high activity | Brassica napus |
| 5 | 8 | high activity | Brassica napus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Lepidium sativum | - |
4.9 | 4.7 |
| Brevicoryne brassicae | - |
- |
4.9 |
| Brassica napus | - |
- |
5.7 |
| Brassica napus | - |
- |
6.2 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Arabidopsis thaliana |
| additional information | structure modeling | Brassica oleracea var. italica |
| additional information | analysis of substrate recognition and mechanism of reaction | Sinapis alba |
| additional information | redox-regulated, the reduced form is more active | Lepidium latifolium |
| 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 | Lepidium sativum |
| 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 | Crambe hispanica subsp. abyssinica |
| 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 | Armoracia rusticana |
| 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 | Lepidium latifolium |
| 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 | Brassica napus |
| 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 | Eutrema halophilum |
| 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 | Arabidopsis thaliana |
| 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 | Carica papaya |
| 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 | Sinapis alba |
| 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 | Brassica oleracea var. italica |
| 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 | Raphanus sativus |
| 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 | Brassica juncea |
| 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 | Eutrema japonicum |
| 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 | Capparis spinosa var. ovata |
| physiological function | the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain | Aspergillus niger |
| physiological function | the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain | Enterobacter cloacae |
| physiological function | the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain | Aspergillus sydowii |
| physiological function | the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain | Enterococcus casseliflavus |
| physiological function | the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain | Brevicoryne brassicae |
| physiological function | the myrosinase-catalyzed reaction starts with cleavage of the thioglucosidic linkage resulting in release of a D-glucose and an unstable thiohydroximate-O-sulfate. The outcome of this thiohydroximate-O-sulfate has been shown to depend on the structure of the glucosinolate side chain | Ligilactobacillus agilis |
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Release 2023.1 (January 2023)
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