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Literature summary for 3.4.22.28 extracted from

  • Wanga, Q.M.; Chen, S.H.
    Human rhinovirus 3C protease as a potential target for the development of antiviral agents (2007), Curr. Protein Pept. Sci., 8, 19-27.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
SO42- activates at high concentrations Human rhinovirus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
SDS-PAGE Human rhinovirus sp.

Organic Solvent Stability

Organic Solvent Comment Organism
additional information 3C protease activity is insensitive against up to 10% organic solvents Human rhinovirus sp.

Organism

Organism UniProt Comment Textmining
Human rhinovirus sp.
-
serotype 14
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cAMP-responsible element binding protein + H2O
-
Human rhinovirus sp. ?
-
?
histone H3 protein + H2O
-
Human rhinovirus sp. ?
-
?
TATA binding protein + H2O
-
Human rhinovirus sp. ?
-
?
transcription factor OCT-1 + H2O
-
Human rhinovirus sp. ?
-
?

Synonyms

Synonyms Comment Organism
3C protease
-
Human rhinovirus sp.
3Cpro
-
Human rhinovirus sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
22 37
-
Human rhinovirus sp.

Cofactor

Cofactor Comment Organism Structure
additional information 3C protease requires neither cofactors nor metals for activity Human rhinovirus sp.