Literature summary extracted from

Bhat, R.; Vyas, D.
Myrosinase insights on structural, catalytic, regulatory, and environmental interactions (2019), Crit. Rev. Biotechnol., 39, 508-523 .

Activating Compound

EC Number	Activating Compound	Comment	Organism
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Aspergillus sydowii
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Crambe hispanica subsp. abyssinica
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Armoracia rusticana
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Lepidium latifolium
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Brassica napus
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Eutrema halophilum
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Arabidopsis thaliana
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Carica papaya
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Brassica oleracea var. italica
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Brassica juncea
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Eutrema japonicum
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid	Capparis spinosa var. ovata
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid, mechanism of ascorbic acid activation, overview	Sinapis alba
3.2.1.147	ascorbic acid	all the plant myrosinases are reported to be activated by ascorbic acid, uncompetitive activation by ascorbic acid	Raphanus sativus
3.2.1.147	ascorbic acid	dependent on, all the plant myrosinases are reported to be activated by ascorbic acid	Lepidium sativum
3.2.1.147	additional information	isozyme TGG1 is an ascorbate independent O-beta-glucosidase activity	Carica papaya
3.2.1.147	additional information	no effect on activity by ascorbic acid	Aspergillus niger
3.2.1.147	additional information	redox-regulated, the reduced form is more active	Lepidium latifolium

General Stability

EC Number	General Stability	Organism
3.2.1.147	the enzyme is heat and pressure sensitive	Brassica oleracea var. italica
3.2.1.147	the enzyme is stable only in presence of 2-mercapethanol and ascorbic acid	Aspergillus niger
3.2.1.147	the enzyme is temperature sensitive but quite pressure stable	Sinapis alba

Inhibitors

EC Number	Inhibitors	Comment	Organism
3.2.1.147	2-deoxy-glucotropaeolin	a strong competitive inhibitor	Sinapis alba
3.2.1.147	ascorbic acid	inhibits the enzyme, ascorbic acid addition resulted in production of hydroxylated degradation products	Brevicoryne brassicae
3.2.1.147	ascorbic acid	-	Enterobacter cloacae
3.2.1.147	castanospermine	the alkaloidal glycosidase inhibitor acts as competitive inhibitor	Lepidium sativum
3.2.1.147	Cu2+	-	Enterobacter cloacae
3.2.1.147	D-glucose	inhibits at 5 mM	Lepidium latifolium
3.2.1.147	delta-gluconolactone	-	Aspergillus niger
3.2.1.147	EDTA	strong inhibition	Enterobacter cloacae
3.2.1.147	Fe2+	-	Enterobacter cloacae
3.2.1.147	Hg2+	-	Aspergillus niger
3.2.1.147	Hg2+	-	Enterobacter cloacae
3.2.1.147	additional information	no effect on activity by ascorbic acid	Aspergillus niger
3.2.1.147	additional information	sugars and glucosides act as competitive inhibitors	Brassica juncea
3.2.1.147	additional information	the enzyme shows substrate inhibition via a binding site mechanisms, and is sensitive against heat and pressure	Brassica oleracea var. italica
3.2.1.147	Sn2+	-	Aspergillus niger

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.2.1.147	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

EC Number	Metals/Ions	Comment	Organism
3.2.1.147	Co2+	activates	Aspergillus niger
3.2.1.147	Cu2+	activates	Aspergillus niger
3.2.1.147	Mg2+	-	Escherichia coli
3.2.1.147	Mg2+	-	Enterococcus casseliflavus
3.2.1.147	Mg2+	-	Ligilactobacillus agilis
3.2.1.147	Mn2+	activates	Aspergillus niger
3.2.1.147	additional information	Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production	Escherichia coli
3.2.1.147	additional information	Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production	Enterococcus casseliflavus
3.2.1.147	additional information	Fe2+ ions promotes nitriles production from glucosinolates while Mg2+ ions stimulates isothiocyanate production	Ligilactobacillus agilis

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
3.2.1.147	120000	-	-	Brevicoryne brassicae
3.2.1.147	120000	-	-	Raphanus sativus
3.2.1.147	124000	-	about	Arabidopsis thaliana
3.2.1.147	126000	-	-	Arabidopsis thaliana
3.2.1.147	130000	-	-	Lepidium sativum
3.2.1.147	130000	-	-	Armoracia rusticana
3.2.1.147	130000	-	-	Arabidopsis thaliana
3.2.1.147	135000	-	-	Sinapis alba
3.2.1.147	150000	-	-	Arabidopsis thaliana
3.2.1.147	156000	-	-	Brassica napus
3.2.1.147	157000	-	-	Brassica oleracea var. italica
3.2.1.147	160000	-	-	Lepidium latifolium
3.2.1.147	188000	-	-	Brassica napus
3.2.1.147	470000	-	-	Crambe hispanica subsp. abyssinica
3.2.1.147	580000	-	-	Eutrema japonicum

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.147	Arabidopsis thaliana	P37702	-	-
3.2.1.147	Arabidopsis thaliana	Q3ECS3	-	-
3.2.1.147	Arabidopsis thaliana	Q8GRX1	-	-
3.2.1.147	Arabidopsis thaliana	Q9C5C2	-	-
3.2.1.147	Armoracia rusticana	Q5PXK2	-	-
3.2.1.147	Aspergillus niger	-	-	-
3.2.1.147	Aspergillus sydowii	-	-	-
3.2.1.147	Brassica juncea	Q9ZP01	-	-
3.2.1.147	Brassica napus	Q42629	-	-
3.2.1.147	Brassica napus	Q9STD7	-	-
3.2.1.147	Brassica oleracea var. italica	A0A343IQS8	-	-
3.2.1.147	Brevicoryne brassicae	Q95X01	isozyme 1	-
3.2.1.147	Capparis spinosa var. ovata	-	-	-
3.2.1.147	Carica papaya	C9WCQ0	-	-
3.2.1.147	Carica papaya	C9WCQ1	-	-
3.2.1.147	Crambe hispanica subsp. abyssinica	-	-	-
3.2.1.147	Enterobacter cloacae	-	-	-
3.2.1.147	Enterococcus casseliflavus	-	-	-
3.2.1.147	Enterococcus casseliflavus CP1	-	-	-
3.2.1.147	Escherichia coli	-	-	-
3.2.1.147	Escherichia coli VL8	-	-	-
3.2.1.147	Eutrema halophilum	-	isozymes TGG1 and TGG2	-
3.2.1.147	Eutrema japonicum	Q4AE75	i.e. Wasabia japonica	-
3.2.1.147	Lepidium latifolium	-	-	-
3.2.1.147	Lepidium sativum	-	-	-
3.2.1.147	Ligilactobacillus agilis	-	-	-
3.2.1.147	Ligilactobacillus agilis R16	-	-	-
3.2.1.147	Raphanus sativus	V9PVN6	-	-
3.2.1.147	Sinapis alba	P29736	isozyme MA1	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
3.2.1.147	glycoprotein	-	Arabidopsis thaliana
3.2.1.147	glycoprotein	deglycosylation affects TGG1 activity	Arabidopsis thaliana
3.2.1.147	glycoprotein	deglycosylation does not affect TGG2 activity	Arabidopsis thaliana
3.2.1.147	glycoprotein	the isoforms differ in carbohydrate content	Brassica napus
3.2.1.147	no glycoprotein	-	Brevicoryne brassicae

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.2.1.147	native enzyme	Brevicoryne brassicae
3.2.1.147	native enzyme from leaves	Lepidium latifolium
3.2.1.147	native enzyme from roots	Armoracia rusticana
3.2.1.147	native enzyme from roots	Eutrema japonicum
3.2.1.147	native enzyme from seedlings or roots	Raphanus sativus
3.2.1.147	native enzyme from seedlings or seeds	Lepidium sativum
3.2.1.147	native enzyme from seedlings, partially from seed	Brassica napus
3.2.1.147	native enzyme from seeds	Crambe hispanica subsp. abyssinica
3.2.1.147	native enzyme from seeds	Sinapis alba
3.2.1.147	native enzyme from sprouts	Brassica oleracea var. italica
3.2.1.147	native enzyme partially	Aspergillus sydowii
3.2.1.147	native isozyme CpTGG1 from leaves	Carica papaya
3.2.1.147	native isozyme CpTGG2 from roots	Carica papaya
3.2.1.147	native isozyme TGG1 from leaves	Arabidopsis thaliana
3.2.1.147	native isozyme TGG2 from leaves	Arabidopsis thaliana
3.2.1.147	native isozyme TGG4 from roots	Arabidopsis thaliana
3.2.1.147	native isozyme TGG5 from roots	Arabidopsis thaliana
3.2.1.147	partial purification of the seed enzyme	Brassica juncea

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
3.2.1.147	a thioglucoside + H2O = a sugar + a thiol	reaction mechanism	Sinapis alba	a

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.2.1.147	flower	-	Eutrema halophilum	-
3.2.1.147	flower	-	Capparis spinosa var. ovata	-
3.2.1.147	leaf	-	Lepidium latifolium	-
3.2.1.147	leaf	-	Eutrema halophilum	-
3.2.1.147	leaf	-	Arabidopsis thaliana	-
3.2.1.147	leaf	-	Carica papaya	-
3.2.1.147	leaf	-	Capparis spinosa var. ovata	-
3.2.1.147	additional information	the TGG2 orthologue is present in different organs, but not in roots	Capparis spinosa var. ovata	-
3.2.1.147	petiole	-	Eutrema halophilum	-
3.2.1.147	root	-	Armoracia rusticana	-
3.2.1.147	root	-	Eutrema halophilum	-
3.2.1.147	root	-	Carica papaya	-
3.2.1.147	root	-	Raphanus sativus	-
3.2.1.147	root	-	Arabidopsis thaliana	-
3.2.1.147	root	-	Eutrema japonicum	-
3.2.1.147	seed	-	Crambe hispanica subsp. abyssinica	-
3.2.1.147	seed	-	Sinapis alba	-
3.2.1.147	seed	-	Brassica juncea	-
3.2.1.147	seedling	-	Lepidium sativum	-
3.2.1.147	seedling	-	Brassica napus	-
3.2.1.147	seedling	-	Raphanus sativus	-
3.2.1.147	sprout	-	Brassica oleracea var. italica	-
3.2.1.147	stem	-	Capparis spinosa var. ovata	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
3.2.1.147	epigoitrin + H2O	-	Crambe hispanica subsp. abyssinica	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Aspergillus niger	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Enterobacter cloacae	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Aspergillus sydowii	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Lepidium sativum	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Enterococcus casseliflavus	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Armoracia rusticana	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Lepidium latifolium	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Eutrema halophilum	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Arabidopsis thaliana	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Carica papaya	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Sinapis alba	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Brevicoryne brassicae	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Brassica oleracea var. italica	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Raphanus sativus	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Brassica juncea	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Eutrema japonicum	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Capparis spinosa var. ovata	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Ligilactobacillus agilis	?	-	?
3.2.1.147	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	?	-	?
3.2.1.147	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	?	-	?
3.2.1.147	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	?	-	?
3.2.1.147	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	?	-	?
3.2.1.147	additional information	the enzyme produces nitriles from desulfoglucosinolates	Escherichia coli	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Ligilactobacillus agilis R16	?	-	?
3.2.1.147	additional information	the enzyme produces nitriles from desulfoglucosinolates	Escherichia coli VL8	?	-	?
3.2.1.147	additional information	myrosinase catalyzes hydrolysis of the S-glycosyl bond, O-beta glycosyl bond, and O-glycosyl bonds of glucosinolates	Enterococcus casseliflavus CP1	?	-	?
3.2.1.147	progoitrin + H2O	-	Crambe hispanica subsp. abyssinica	(1E,3S)-3-hydroxy-n-(sulfooxy)pent-4-enimidothioic acid + D-glucose	-	?
3.2.1.147	sinigrin + H2O	-	Crambe hispanica subsp. abyssinica	(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose	-	?
3.2.1.147	sinigrin + H2O	best substrate	Brevicoryne brassicae	(1Z)-N-(sulfooxy)but-3-enimidothioic acid + D-glucose	-	?

Subunits

EC Number	Subunits	Comment	Organism
3.2.1.147	?	x * 65000	Capparis spinosa var. ovata
3.2.1.147	?	x * 65000, isozyme CpTGG2	Carica papaya
3.2.1.147	?	x * 70000, isozyme CpTGG1	Carica papaya
3.2.1.147	dimer	2 * 70000	Lepidium latifolium
3.2.1.147	dimer	2 * 75000	Brassica napus
3.2.1.147	dimer	2 * 75000	Arabidopsis thaliana
3.2.1.147	dimer	2 * 65000	Armoracia rusticana
3.2.1.147	dimer	2 * 65000	Arabidopsis thaliana
3.2.1.147	dimer	2 * 62000	Arabidopsis thaliana
3.2.1.147	dimer	2 * 57000-60000	Brevicoryne brassicae
3.2.1.147	dimer	2 * 61000-62000	Raphanus sativus
3.2.1.147	dimer	2 * 62000-65000	Lepidium sativum
3.2.1.147	dimer	2 * 63000	Arabidopsis thaliana
3.2.1.147	dimer	2 * 71700	Sinapis alba
3.2.1.147	dimer or trimer	x * 62000	Brassica napus
3.2.1.147	dodecamer	12 * 45000-47000	Eutrema japonicum
3.2.1.147	More	existence of different oligomeric states in different redox environments	Lepidium latifolium
3.2.1.147	More	the enzyme contains about 19% alpha-helix and 35% beta-sheets, the rest being conformationally aperiodic	Sinapis alba
3.2.1.147	oligomer	x * 75000	Crambe hispanica subsp. abyssinica
3.2.1.147	trimer	50000-55000	Brassica oleracea var. italica

Synonyms

EC Number	Synonyms	Comment	Organism
3.2.1.147	beta-thioglucosidase	-	Brevicoryne brassicae
3.2.1.147	beta-thioglucosidase glucohydrolase	-	Brevicoryne brassicae
3.2.1.147	beta-thioglucoside glucohydrolase	-	Carica papaya
3.2.1.147	CpTGG1	-	Carica papaya
3.2.1.147	CpTGG2	-	Carica papaya
3.2.1.147	Myr1.Bn1	-	Brassica napus
3.2.1.147	Myr2.Bn1	-	Brassica napus
3.2.1.147	MYRI	-	Brassica napus
3.2.1.147	MYRII	-	Brassica napus
3.2.1.147	myrosinase	-	Escherichia coli
3.2.1.147	myrosinase	-	Aspergillus niger
3.2.1.147	myrosinase	-	Enterobacter cloacae
3.2.1.147	myrosinase	-	Aspergillus sydowii
3.2.1.147	myrosinase	-	Lepidium sativum
3.2.1.147	myrosinase	-	Crambe hispanica subsp. abyssinica
3.2.1.147	myrosinase	-	Enterococcus casseliflavus
3.2.1.147	myrosinase	-	Armoracia rusticana
3.2.1.147	myrosinase	-	Lepidium latifolium
3.2.1.147	myrosinase	-	Brassica napus
3.2.1.147	myrosinase	-	Eutrema halophilum
3.2.1.147	myrosinase	-	Arabidopsis thaliana
3.2.1.147	myrosinase	-	Carica papaya
3.2.1.147	myrosinase	-	Sinapis alba
3.2.1.147	myrosinase	-	Brevicoryne brassicae
3.2.1.147	myrosinase	-	Brassica oleracea var. italica
3.2.1.147	myrosinase	-	Raphanus sativus
3.2.1.147	myrosinase	-	Brassica juncea
3.2.1.147	myrosinase	-	Eutrema japonicum
3.2.1.147	myrosinase	-	Capparis spinosa var. ovata
3.2.1.147	myrosinase	-	Ligilactobacillus agilis
3.2.1.147	sinigrinase	-	Brevicoryne brassicae
3.2.1.147	TGG1	-	Arabidopsis thaliana
3.2.1.147	TGG2	-	Arabidopsis thaliana
3.2.1.147	TGG4	-	Arabidopsis thaliana
3.2.1.147	TGG5	-	Arabidopsis thaliana
3.2.1.147	WjMYR	-	Eutrema japonicum

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
3.2.1.147	37	-	-	Raphanus sativus
3.2.1.147	37	-	-	Eutrema japonicum
3.2.1.147	37	-	substrate epigoitrin	Crambe hispanica subsp. abyssinica
3.2.1.147	37	45	-	Armoracia rusticana
3.2.1.147	40	-	-	Brevicoryne brassicae
3.2.1.147	40	-	-	Brassica oleracea var. italica
3.2.1.147	40	-	isozyme CpTGG1	Carica papaya
3.2.1.147	40	-	isozyme CpTGG2	Carica papaya
3.2.1.147	50	-	-	Lepidium latifolium
3.2.1.147	50	-	-	Arabidopsis thaliana
3.2.1.147	50	-	substrate sinigrin	Crambe hispanica subsp. abyssinica
3.2.1.147	55	-	-	Brassica napus
3.2.1.147	60	-	-	Arabidopsis thaliana
3.2.1.147	70	-	-	Arabidopsis thaliana

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
3.2.1.147	additional information	-	low pressure retards thermal inactivation	Brassica oleracea var. italica

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.2.1.147	4	-	-	Brassica oleracea var. italica
3.2.1.147	5	6	-	Brassica napus
3.2.1.147	5.5	-	-	Lepidium sativum
3.2.1.147	5.5	-	-	Arabidopsis thaliana
3.2.1.147	5.5	6	-	Brassica napus
3.2.1.147	5.5	10.5	-	Arabidopsis thaliana
3.2.1.147	5.7	-	-	Armoracia rusticana
3.2.1.147	6	6.5	-	Raphanus sativus
3.2.1.147	6	-	-	Lepidium latifolium
3.2.1.147	6	-	-	Arabidopsis thaliana
3.2.1.147	6.5	-	substrate epigoitrin	Crambe hispanica subsp. abyssinica
3.2.1.147	6.5	7.7	-	Eutrema japonicum
3.2.1.147	7.5	-	isozyme CpTGG1	Carica papaya
3.2.1.147	7.5	-	substrate sinigrin	Crambe hispanica subsp. abyssinica
3.2.1.147	8	-	isozyme CpTGG2	Carica papaya
3.2.1.147	8.5	-	substrate progoitrin	Crambe hispanica subsp. abyssinica

pH Range

EC Number	pH Minimum	pH Maximum	Comment	Organism
3.2.1.147	4	7.5	high activity	Brassica napus
3.2.1.147	5	8	high activity	Brassica napus

pI Value

EC Number	Organism	Comment	pI Value Maximum	pI Value
3.2.1.147	Lepidium sativum	-	4.9	4.7
3.2.1.147	Brevicoryne brassicae	-	-	4.9
3.2.1.147	Brassica napus	-	-	5.7
3.2.1.147	Brassica napus	-	-	6.2

General Information

EC Number	General Information	Comment	Organism
3.2.1.147	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
3.2.1.147	additional information	structure modeling	Brassica oleracea var. italica
3.2.1.147	additional information	analysis of substrate recognition and mechanism of reaction	Sinapis alba
3.2.1.147	additional information	redox-regulated, the reduced form is more active	Lepidium latifolium
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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
3.2.1.147	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