Compact archived record and sequence evidence for G1FNI6
Electronic Gene Ontology annotations created by ARBA machine learning models
TreeGrafter-generated GO annotations
The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown.
A thiocyanate-forming protein generates multiple products upon allylglucosinolate breakdown in Thlaspi arvense.
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TaTFP catalyzes allylthiocyanate and epithionitrile formation from allylglucosinolate in the presence of myrosinase, is Fe(2+)-stimulated and EDTA-repressed, and is expressed constitutively across tissues.
Molecular models and mutational analyses of plant specifier proteins suggest active site residues and reaction mechanism.
Structural diversification during glucosinolate breakdown: mechanisms of thiocyanate, epithionitrile and simple nitrile formation.
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Specifier proteins, including TaTFP, are reclassified as Fe(2+)-dependent lyases; the iron-binding triad (E266/D270/H274) and substrate docking pose determine whether thiocyanate, epithionitrile, or simple nitrile is produced.
Falcon/Edison deep research report for TFP (TaTFP), Thlaspi arvense