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Literature summary for 3.4.22.29 extracted from

  • Badorff, C.; Berkely, N.; Mehrotra, S.; Talhouk, J.W.; Rhoads, R.E.; Knowlton, K.U.
    Enteroviral protease 2A directly cleaves dystrophin and is inhibited by a dystrophin-based substrate analogue (2000), J. Biol. Chem., 275, 11191-11197.
    View publication on PubMed
Search for more literature for 3.4.22.29

Inhibitors

Inhibitors Comment Organism Structure
benzyloxycarbonyl-LSTL-fluoromethyl ketone IC50: 1050 nM coxsackievirus
benzyloxycarbonyl-LSTT-fluoromethyl ketone IC50: 550 nM coxsackievirus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dystrophin + H2O coxsackievirus functional impairment and morphological disruption of dystrophin ?
-
 ?

Organism

Organism UniProt Comment Textmining
coxsackievirus
-
 B3
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dystrophin + H2O cleavage of mouse dystrophin at residue 2427 and human dystrophin at residue 2434 coxsackievirus ?
-
 ?
dystrophin + H2O functional impairment and morphological disruption of dystrophin coxsackievirus ?
-
 ?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00055
-
 IC50: 550 nM coxsackievirus benzyloxycarbonyl-LSTT-fluoromethyl ketone
0.00105
-
 IC50: 1050 nM coxsackievirus benzyloxycarbonyl-LSTL-fluoromethyl ketone