The Enzyme Database

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Accepted name: N-(sulfonatooxy)prop-2-enimidothioate sulfolyase
Reaction: (1) N-(sulfonatooxy)prop-2-enimidothioate = prop-2-enylthiocyanate + sulfate
(2) N-(sulfonatooxy)prop-2-enimidothioate = 2-(thiiran-2-yl)acetonitrile + sulfate
Other name(s): TFP (gene name) (ambiguous); thiocyanate-forming protein (ambiguous)
Systematic name: N-(sulfonatooxy)prop-2-enimidothioate sulfate-lyase (prop2-enylthiocyanate-forming)
Comments: 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, thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming) and EC, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kuchernig, J.C., Backenkohler, A., Lubbecke, M., Burow, M. and Wittstock, U. A thiocyanate-forming protein generates multiple products upon allylglucosinolate breakdown in Thlaspi arvense. Phytochemistry 72 (2011) 1699–1709. [DOI] [PMID: 21783213]
2.  Gumz, F., Krausze, J., Eisenschmidt, D., Backenkohler, A., Barleben, L., Brandt, W. and Wittstock, U. The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown. Plant Mol. Biol. 89 (2015) 67–81. [DOI] [PMID: 26260516]
3.  Eisenschmidt-Bonn, D., Schneegans, N., Backenkohler, A., Wittstock, U. and Brandt, W. Structural diversification during glucosinolate breakdown: mechanisms of thiocyanate, epithionitrile and simple nitrile formation. Plant J. 99 (2019) 329–343. [DOI] [PMID: 30900313]
[EC created 2022]

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