The enzyme, characterized from the plant Thlaspi arvense, is involved in the breakdown of the glucosinolate sinigrin. Depending on the substrate, it can also form simple nitrile-containing products. cf. EC 4.8.1.5, thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming) and EC 4.8.1.6, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming).
The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the plant Thlaspi arvense, is involved in the breakdown of the glucosinolate sinigrin. Depending on the substrate, it can also form simple nitrile-containing products. cf. EC 4.8.1.5, thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming) and EC 4.8.1.6, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming).
Substrates: with substrates 4-methylthiobutylglucosinolate, 4-methylsulfinylbutylglucosinolate and benzylglucosinolate, a high proportion of the corresponding simple nitriles, but no organic thiocyanate, is formed in the presence of TFP, reaction of EC 4.8.1.5 Products: -
Substrates: TFP can also form simple nitrile- and epithionitrile-containing products from aliphatic glucosinolates, i.e. catalyze the reactions of EC 4.8.1.5, and EC 4.8.1.6 Products: -
activity in vitro is not strictly dependent on Fe2+ addition. Addition of Fe2+ causes a strong increase in the generation of allylthiocyanate and the corresponding epithionitrile at the expense of isothiocyanate formation. The proportion of thiocyanate to epithionitrile remained largely unchanged
total hydrolysis product formation strongly depends on the pH of the assay mixture. Above pH 6.0, the proportion of allylthiocyanate of the total amount of hydrolysis products decreases, at pH 7.5 and above, absolute amounts of allylthiocyanate also decrease. Epithionitrile formation is also highest at pH 5.5-6.0
TFP is able to bind the allylglucosinolate aglucone in two different ways with respect to Fe2+ cofactor co-ordination, this is an essential precondition for its broad product profile leading to nitrile-, epithionitrile and thiocyanate containing products. The inductive effect of Fe2+ affects the aglucone on specific sites and guides the reaction in a specific direction
TFP is involved in the breakdown of the glucosinolate sinigrin,forming allylthiocyanate, as well as the corresponding epithionitrile, reaction of EC 4.8.1.6, upon myrosinase-catalyzed hydrolysis of allylglucosinolate, respectively. All other glucosinolates tested are converted to their simple nitriles when hydrolyzed in the presence of TFP, reaction of EC 4.8.1.5
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure at a resolution of 1.4 A. TFP crystallizes as homodimer. Each monomer forms a six-blade beta-propeller with a wide top and a narrower bottom opening with distinct strand-connecting loops protruding far beyond the lower propeller surface
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