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Literature summary for 3.4.21.98 extracted from

  • Archer, S.J.; Camac, D.M.; Wu, Z.J.; Farrow, N.A.; Domaille, P.J.; Wasserman, Z.R.; Bukhtiyarova, M.; Rizzo, C.; Jagannathan, S.; Mersinger, L.J.; Kettner, C.A.
    Hepatitis C virus NS3 protease requires its NS4A cofactor peptide for optimal binding of a boronic acid inhibitor as shown by NMR (2002), Chem. Biol., 9, 79-92.
    View publication on PubMed
Search for more literature for 3.4.21.98

Activating Compound

Activating Compound Comment Organism Structure
NS4A
-
 Hepacivirus C

Inhibitors

Inhibitors Comment Organism Structure
acetyl-Asp-Glu-Val-Val-Pro-boroAlg-OH the inhibitor binds in an antiparrallel manner to beta-strand E2 and interacts with the unprimed sites of the substrate binding pocket. In the NS3/NS4 inhibitor complex, the inhibitor behaves like a reaction intermediate analog. In the absence of the cofactor, inhibitor binding is an order of magnitude weaker Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Asp-Glu-Asp-(5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid)-Glu-Glu-(alpha-aminobutyryl)PSI[COO]Ala-Ser-Lys-(4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid)-NH2 + H2O
-
 Hepacivirus C ?
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000013
-
 acetyl-Asp-Glu-Val-Val-Pro-boroAlg-OH
-
 Hepacivirus C