The role of the cysteinyl and one of the tryptophyl residues in the neurotoxic action of suberitine.
The selective photooxidation of the single cysteinyl residue and one of the 3 tryptophyl residues of suberitine has been performed by irradiation using crystal violet and proflavine respectively as photosensitizers. Crystal violet and the protein form a 1:1 complex with a consequent partial inhibition of the neurotoxic activity. The latter is completely abolished by specific photooxidation of cysteine which is probably involved in the active site of the protein. The modification of the tryptophyl residue induces a large loss of the activity as a consequence of a photoinduced extensive denaturation of suberitine.
D003545:Cysteine; D005840:Gentian Violet / Q000494:pharmacology; D008027:Light; D008387:Marine Toxins / Q000494:pharmacology; D009498:Neurotoxins / Q000494:pharmacology; D011370:Proflavine / Q000494:pharmacology; D011489:Protein Denaturation; D011506:Proteins / Q000037:antagonists & inhibitors / Q000494:pharmacology* / Q000528:radiation effects; D013329:Structure-Activity Relationship; D014364:Tryptophan; D014508:Urea / Q000494:pharmacology
D008387:Marine Toxins; D009498:Neurotoxins; D011506:Proteins; C031284:suberitine protein, Suberites domuncula; D014364:Tryptophan; D014508:Urea; D011370:Proflavine; D005840:Gentian Violet; D003545:Cysteine