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Literature summary for 3.4.22.28 extracted from

  • Bazan, J.F.; Fletterick, R.J.
    Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications (1988), Proc. Natl. Acad. Sci. USA, 85, 7872-7876.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Activating Compound

Activating Compound Comment Organism Structure
additional information no activation by Triton X-100 Enterovirus C

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli or BL21(D3) Enterovirus C

Inhibitors

Inhibitors Comment Organism Structure
1,3-Dibromoacetone
-
 Enterovirus C
additional information no inhibition by Triton X-100 Enterovirus C

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble recombinant enzyme Enterovirus C
-
-
soluble native enzyme: partial Enterovirus C
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
-
 Enterovirus C

Organism

Organism UniProt Comment Textmining
Enterovirus C
-
 type 2, i.e. Sabin strain
-
Enterovirus C Sabin
-
 type 2, i.e. Sabin strain
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Enterovirus C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B Enterovirus C dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
 ?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B Enterovirus C Sabin dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
 ?
poliovirus P1 precursor polyprotein + H2O trans-cleavage Enterovirus C capsid proteins
-
 ?
poliovirus P1 precursor polyprotein + H2O trans-cleavage Enterovirus C Sabin capsid proteins
-
 ?