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Literature summary for 3.2.1.147 extracted from
- Myrosinase in Brassicaceae the most important issue for glucosinolate turnover and food quality (2015), Phytochem. Rev., 14, 1045-1051 .
No PubMed abstract available
General Stability
| General Stability | Organism |
|---|---|
| extrinsic factors, during postharvest and food processing such as pH, temperature, and pressure | Sinapis alba |
| Zn2+ stabilizes the enzyme structure, the myrosinase structure also has a substantial number of salt bridges and hydrogen bonds between charged and neutral atoms that confers additional stability to the enzyme. The activity of myrosinase is influenced by some intrinsic and | Sinapis alba |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | stabilizes the enzyme structure | Sinapis alba |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Brassica napus | - |
- |
- |
| Brassica oleracea var. alboglabra | - |
- |
- |
| Brassica rapa | - |
- |
- |
| Brassica rapa subsp. pekinensis | - |
- |
- |
| Raphanus sativus | - |
- |
- |
| Sinapis alba | - |
- |
- |
| Thellungiella | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | glycosylated dimer | Sinapis alba |
| glycoprotein | N-linked sugar binding sites of the myrosinase are implicated in the binding of myrosinase-binding proteins (MBPs) | Brassica napus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific | Raphanus sativus | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific | Brassica rapa subsp. pekinensis | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific | Sinapis alba | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific | Brassica oleracea var. alboglabra | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. In the halophyte Thellungiella salt stress enhances myrosinase activity during the vegetative phase in the rosette leaves, with no relation between the changes in glucosinolate content and myrosinase activity in the roots | Thellungiella | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression | Arabidopsis thaliana | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression | Brassica napus | - |
| additional information | distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific. Tissue-specific and temporal enzyme expression | Brassica rapa | - |
| root | - |
Thellungiella | - |
| rosette leaf | - |
Thellungiella | - |
| seed | - |
Sinapis alba | - |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | the enzyme protein folds into a (beta/alpha)8 barrel structure forming a glycosylated dimer stabilized by a Zn2+ ion | Sinapis alba |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| myrosinase | - |
Arabidopsis thaliana |
| myrosinase | - |
Brassica napus |
| myrosinase | - |
Raphanus sativus |
| myrosinase | - |
Brassica rapa subsp. pekinensis |
| myrosinase | - |
Brassica rapa |
| myrosinase | - |
Sinapis alba |
| myrosinase | - |
Brassica oleracea var. alboglabra |
| myrosinase | - |
Thellungiella |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Thellungiella | in the halophyte Thellungiella salt stress enhances myrosinase activity during the vegetative phase in the rosette leaves, with no relation between the changes in glucosinolate content and myrosinase activity in the roots | up |
| Arabidopsis thaliana | water stress increases abscisic acid levels that enhanced glucosinolates delivery from the vacuole, myrosinase activity or its substrate affinity | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Arabidopsis thaliana |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Brassica napus |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Raphanus sativus |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Brassica rapa subsp. pekinensis |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Brassica rapa |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Sinapis alba |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Brassica oleracea var. alboglabra |
| evolution | myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) | Thellungiella |
| 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 | Arabidopsis thaliana |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew | Raphanus sativus |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew | Brassica rapa subsp. pekinensis |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew | Brassica rapa |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew | Sinapis alba |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew | Brassica oleracea var. alboglabra |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew. A clear genotype and plant developmental stage-dependence is associated to the correspondence between glucosinolates content and myrosinase activity in Thellungiella | Thellungiella |
| physiological function | plant myrosinase, is an enzyme found in Brassicaceae family with an essential role on the glucosinolates conversion to isothiocyanates. Myrosinase is an enzyme found in all glucosinolate-containing Brassicaceae family (cabbage, brussels sprout, radish, turnip, water cress, and mustard). All isoenzymes of myrosinases are observed to catalyze the hydrolysis of glucosinolates, into D-glucose and an aglucone. The latter compounds are spontaneously converted into isothiocyanates or indoles depending on the side chain, which are the biologically active forms of glucosinolates. The enzyme is part of the glucosinolate-myrosinase system that is a defense machinery against both biotic and abiotic stress where glucosinolates are modulated to respond to different environmental factors, i.e. pathogens/endophytic fungi, heat, water, salt and pressure stresses, overiew. Other proteins can interact with the myrosinase forming myrosinase-binding proteins (MBPs) and myrosinase associated proteins (MyAP). They have been identified as complexes contributing to the plant defense system in different Brassica species such as Brassica napus or Arabidopsis thaliana. Potential N-linked sugar binding sites of the myrosinase are implicated in the binding of MBP | Brassica napus |
| 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 | Arabidopsis thaliana |
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