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Literature summary for 3.4.22.28 extracted from

  • Sun, D.; Wang, M.; Wen, X.; Mao, S.; Cheng, A.; Jia, R.; Yang, Q.; Wu, Y.; Zhu, D.; Chen, S.; Liu, M.; Zhao, X.; Zhang, S.; Chen, X.; Liu, Y.; Yu, Y.; Zhang, L.
    Biochemical characterization of recombinant Avihepatovirus 3C protease and its localization (2019), Virol. J., 16, 54 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged DHAV 3C protease in Escherichia coli strain BL21, method optimization. Recombinant expression of N-terminally GFP-tagged wild-type enzyme and enzyme mutants in DEF cells with localization in the cytoplasm Avihepatovirus A

Protein Variants

Protein Variants Comment Organism
C144A site-directed mutagenesis, the mutant is localized in the cytoplasm Avihepatovirus A
H38A site-directed mutagenesis, the mutant is localized in the cytoplasm Avihepatovirus A

Inhibitors

Inhibitors Comment Organism Structure
rupintrivir i.e. AG7088 Avihepatovirus A

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis for DHAV 3C protease Avihepatovirus A
0.05078
-
 4-(4-dimethylaminophenylazo)benzoyl-ASFMNQSKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid pH 7.0, 37°C, recombinant enzyme Avihepatovirus A

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information localization of the 3C protease in infected and transfected cells is determined using immunofluorescence and confocal microscopy. The DHAV 3C protease is found in the nucleus during infection. In addition, the DHAV 3C protease can enter into the nucleus without cooperation of viral proteins Avihepatovirus A
-
-

Organism

Organism UniProt Comment Textmining
Avihepatovirus A YP_007969882 DHAV
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged DHAV 3C protease from Escherichia coli strain BL21 by nickel affinity chromatography Avihepatovirus A

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-(4-dimethylaminophenylazo)benzoyl-ASFMNQSKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid + H2O the fluorometric substrate is cleaved by the 3C protease at the 2C-3A junction, which is derived from the native protease cleavage site within the DHAV polyprotein Avihepatovirus A 4-(4-dimethylaminophenylazo)benzoyl-ASFMNQ + SKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid
-
 ?
additional information optimization of in vitro cleavage assay method with a fluorogenic peptide substrate derived from the cleavage site of the DHAV polyprotein, overview Avihepatovirus A ?
-
 ?

Synonyms

Synonyms Comment Organism
3C protease
-
 Avihepatovirus A
3Cpro
-
 Avihepatovirus A
Avihepatovirus 3C protease
-
 Avihepatovirus A
DHAV 3C protease
-
 Avihepatovirus A
picornaviral 3C protease
-
 Avihepatovirus A

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Avihepatovirus A

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Avihepatovirus A

General Information

General Information Comment Organism
evolution evolutionary analysis of the picornaviral 3C protease Avihepatovirus A
additional information predicted protease cleavage sites of the DHAV polyprotein, overview. The 3C position in the polyprotein is determined to be at residues 1614-1794 (181 aa). Its cleavage site is PVFNQ/GKVVS. The DHAV 3C protease possesses a 3C cysteine protease domain and a typical Cys-His-Asp catalytic triad Avihepatovirus A