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Literature summary for 3.4.22.28 extracted from

  • Yin, J.; Bergmann, E.M.; Cherney, M.M.; Lall, M.S.; Jain, R.P.; Vederas, J.C.; James, M.N.
    Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site (2005), J. Mol. Biol., 354, 854-871.
    View publication on PubMed

Application

Application Comment Organism
medicine attractive target for antiviral drugs Hepatovirus A

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method at room temperature, to 1.5 A resolution Hepatovirus A

Protein Variants

Protein Variants Comment Organism
C24S intact active site Cys172, displays the same catalytic properties as the wild-type enzyme Hepatovirus A

Inhibitors

Inhibitors Comment Organism Structure
13C-labeled beta-lactone
-
Hepatovirus A
N-Cbz-L-serine beta-lactone irreversible inhibitor, associated with His 102 of the enzyme Hepatovirus A
N-iodoacetyl-Val-Phe-amide irreversible inhibitor, alkylates the active site cysteine 172 Hepatovirus A

Organism

Organism UniProt Comment Textmining
Hepatovirus A
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Dabcyl-GLRTQSFS-EDANS + H2O fluorogenic substrate, hydrolysis at the glutamine residue Hepatovirus A ?
-
?

Synonyms

Synonyms Comment Organism
3C protease
-
Hepatovirus A