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Literature summary extracted from

  • Martinez-Ballesta, M.; Carvajal, M.
    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

EC Number General Stability Organism
3.2.1.147 extrinsic factors, during postharvest and food processing such as pH, temperature, and pressure Sinapis alba
3.2.1.147 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

EC Number Metals/Ions Comment Organism Structure
3.2.1.147 Zn2+ stabilizes the enzyme structure Sinapis alba

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.147 Arabidopsis thaliana
-
-
-
3.2.1.147 Brassica napus
-
-
-
3.2.1.147 Brassica oleracea var. alboglabra
-
-
-
3.2.1.147 Brassica rapa
-
-
-
3.2.1.147 Brassica rapa subsp. pekinensis
-
-
-
3.2.1.147 Raphanus sativus
-
-
-
3.2.1.147 Sinapis alba
-
-
-
3.2.1.147 Thellungiella
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.147 glycoprotein glycosylated dimer Sinapis alba
3.2.1.147 glycoprotein N-linked sugar binding sites of the myrosinase are implicated in the binding of myrosinase-binding proteins (MBPs) Brassica napus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.147 additional information distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific Raphanus sativus
-
3.2.1.147 additional information distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific Brassica rapa subsp. pekinensis
-
3.2.1.147 additional information distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific Sinapis alba
-
3.2.1.147 additional information distribution of myrosinase isoenzymes in Brassicaceae seems to be both plant organ- and species-specific Brassica oleracea var. alboglabra
-
3.2.1.147 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
-
3.2.1.147 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
-
3.2.1.147 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
-
3.2.1.147 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
-
3.2.1.147 root
-
 Thellungiella
-
3.2.1.147 rosette leaf
-
 Thellungiella
-
3.2.1.147 seed
-
 Sinapis alba
-

Subunits

EC Number Subunits Comment Organism
3.2.1.147 dimer the enzyme protein folds into a (beta/alpha)8 barrel structure forming a glycosylated dimer stabilized by a Zn2+ ion Sinapis alba

Synonyms

EC Number Synonyms Comment Organism
3.2.1.147 myrosinase
-
 Arabidopsis thaliana
3.2.1.147 myrosinase
-
 Brassica napus
3.2.1.147 myrosinase
-
 Raphanus sativus
3.2.1.147 myrosinase
-
 Brassica rapa subsp. pekinensis
3.2.1.147 myrosinase
-
 Brassica rapa
3.2.1.147 myrosinase
-
 Sinapis alba
3.2.1.147 myrosinase
-
 Brassica oleracea var. alboglabra
3.2.1.147 myrosinase
-
 Thellungiella

Expression

EC Number Organism Comment Expression
3.2.1.147 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
3.2.1.147 Arabidopsis thaliana water stress increases abscisic acid levels that enhanced glucosinolates delivery from the vacuole, myrosinase activity or its substrate affinity up

General Information

EC Number General Information Comment Organism
3.2.1.147 evolution myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) Arabidopsis thaliana
3.2.1.147 evolution myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) Brassica napus
3.2.1.147 evolution myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) Raphanus sativus
3.2.1.147 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
3.2.1.147 evolution myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) Brassica rapa
3.2.1.147 evolution myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) Sinapis alba
3.2.1.147 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
3.2.1.147 evolution myrosinase enzyme is encoded by a gene family that comprise three subfamilies, myrosinase A (MA), B (MB) and C (MC) Thellungiella
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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
3.2.1.147 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