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Literature summary for 3.4.22.28 extracted from

  • Chernaia, M.M.; Malcolm, B.A.; Allaire, M.; James, M.N.G.
    Hepatitis A virus 3C proteinase: some properties, crystallization and preliminary crystallographic characterization (1993), J. Mol. Biol., 234, 890-893.
    View publication on PubMed
Search for more literature for 3.4.22.28

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hepatovirus A

Crystallization (Commentary)

Crystallization (Comment) Organism
double mutant C24S/C172A Hepatovirus A

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
 1 * 24000, SDS-PAGE, under reducing conditions, wild-type and C172A mutant enzyme each behave as dimers under nonreducing conditions Hepatovirus A

Organism

Organism UniProt Comment Textmining
Hepatovirus A
-
 recombinant enzyme
-
Hepatovirus A
-
 C172A and C24S/C172A
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzymes Hepatovirus A
wild-type and 3 mutant enzymes Hepatovirus A

Subunits

Subunits Comment Organism
monomer 1 * 24000, SDS-PAGE, under reducing conditions, wild-type and C172A mutant enzyme each behave as dimers under nonreducing conditions Hepatovirus A

pI Value

Organism Comment pI Value Maximum pI Value
Hepatovirus A isoform D from wild-type and active mutant C24S
-
 8.35
Hepatovirus A isoform C from wild-type and active mutant C24S and isoforms C from mutants C24S/C172A and C172A
-
 8.65
Hepatovirus A isoform B from wild-type and active mutant C24S
-
 8.85
Hepatovirus A isoform A from wild-type and active mutant C24S and isoforms A from mutants C24S/C172A and C172A
-
 9.1