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Literature summary for 3.2.1.147 extracted from

  • Besle, A.; Brazzolotto, X.; Tatibouet, A.; Cerniauskaite, D.; Gallienne, E.; Rollin, P.; Burmeister, W.P.
    A micromolar O-sulfated thiohydroximate inhibitor bound to plant myrosinase (2010), Acta Crystallogr. Sect. F, 66, 152-155.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in 20 mM HEPES, pH 6.5, 150 mM NaCl, and 0.02 mM ZnSO4, X-ray diffraction structure determination and analysis at 1.6 A resolution Sinapis alba

Inhibitors

Inhibitors Comment Organism Structure
(Z)-(1-((2-(dimethylammonio)ethyl)thio)-2-phenylethylidene)amino sulfate a competitive inhibitor. The sulfate group and the phenyl group of the inhibitor bind to the aglycon-binding site of the enzyme, whereas the N,N-dimethyl group binds to the glucose-binding site, binding structure, overview Sinapis alba

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Sinapis alba myrosinase is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates ?
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?

Organism

Organism UniProt Comment Textmining
Sinapis alba P29736
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-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from seeds Sinapis alba

Source Tissue

Source Tissue Comment Organism Textmining
seed
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Sinapis alba
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information myrosinase is a unique enzyme which catalyzes the hydrolysis of sulfur-containing secondary metabolites called glucosinolates Sinapis alba ?
-
?

Synonyms

Synonyms Comment Organism
myrosinase
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Sinapis alba

General Information

General Information Comment Organism
physiological function myrosinase and its substrates, the glucosinolates, are part of the plant's defense system Sinapis alba