KEGG   ENZYME: 4.8.1.8
Entry
EC 4.8.1.8                  Enzyme                                 
Name
N-(sulfonatooxy)prop-2-enimidothioate sulfolyase;
TFP (gene name) (ambiguous);
thiocyanate-forming protein (ambiguous)
Class
Lyases;
Nitrogen-oxygen lyases;
Hydro-lyases
Sysname
N-(sulfonatooxy)prop-2-enimidothioate sulfate-lyase (prop2-enylthiocyanate-forming)
Reaction(IUBMB)
(1) N-(sulfonatooxy)prop-2-enimidothioate = prop-2-enylthiocyanate + sulfate [RN:R13133];
(2) N-(sulfonatooxy)prop-2-enimidothioate = 2-(thiiran-2-yl)acetonitrile + sulfate [RN:R13134]
Reaction(KEGG)
R13133 R13134
Substrate
N-(sulfonatooxy)prop-2-enimidothioate [CPD:C22641]
Product
prop-2-enylthiocyanate [CPD:C22642];
sulfate [CPD:C00059];
2-(thiiran-2-yl)acetonitrile [CPD:C22643]
Comment
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).
History
EC 4.8.1.8 created 2022
Orthology
K26383  N-(sulfonatooxy)prop-2-enimidothioate sulfolyase
Genes
ALY: 9327847
BRP: 103827899
BNA: 106415866 111207173
BOE: 106306810 106306884
Reference
1  [PMID:21783213]
  Authors
Kuchernig JC, Backenkohler A, Lubbecke M, Burow M, Wittstock U.
  Title
A thiocyanate-forming protein generates multiple products upon allylglucosinolate breakdown in Thlaspi arvense.
  Journal
Phytochemistry 72:1699-709 (2011)
DOI:10.1016/j.phytochem.2011.06.013
  Sequence
[ag:AEL16674]
Reference
2  [PMID:26260516]
  Authors
Gumz F, Krausze J, Eisenschmidt D, Backenkohler A, Barleben L, Brandt W, Wittstock U.
  Title
The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown.
  Journal
Plant Mol Biol 89:67-81 (2015)
DOI:10.1007/s11103-015-0351-9
  Sequence
[ag:AEL16674]
Reference
3  [PMID:30900313]
  Authors
Eisenschmidt-Bonn D, Schneegans N, Backenkohler A, Wittstock U, Brandt W.
  Title
Structural diversification during glucosinolate breakdown: mechanisms of thiocyanate, epithionitrile and simple nitrile formation.
  Journal
Plant J 99:329-343 (2019)
DOI:10.1111/tpj.14327
  Sequence
[ag:AEL16674]
Other DBs
ExplorEnz - The Enzyme Database: 4.8.1.8
IUBMB Enzyme Nomenclature: 4.8.1.8
ExPASy - ENZYME nomenclature database: 4.8.1.8
BRENDA, the Enzyme Database: 4.8.1.8

  All links  
Chemical substance (4)   
   KEGG COMPOUND (4)   
Chemical reaction (2)   
   KEGG REACTION (2)   
Gene (8)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (7)   
Protein sequence (4)   
   UniProt (2)   
   SWISS-PROT (2)   
Protein domain (2)   
   InterPro (2)   
All databases (20)   

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