Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.22.28 extracted from

  • Schultheiss, T.; Sommergruber, W.; Kusov, Y.Y.; Gauss-Müller, V.
    Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates (1995), J. Virol., 69, 1727-1733.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hepatovirus A

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 enzyme structure Hepatovirus A
26000
-
 x * 26000, SDS-PAGE Hepatovirus A

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hepatitis A virus polyprotein + H2O Hepatovirus A processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner ?
-
 ?

Organism

Organism UniProt Comment Textmining
Hepatovirus A
-
 recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
2 isoforms, as expressed in Escherichia coli Hepatovirus A
recombinant enzymes Hepatovirus A

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hepatitis A virus deltaP1-2AB polyprotein fragment + H2O C-terminally truncated protein Hepatovirus A hepatitis A virus protein 2A + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2BC + hepatitis A virus protein 2 + hepatitis A virus protein 2B
-
 ?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O deltaVP1-P2-P3*, C-terminally truncated protein Hepatovirus A hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
 ?
hepatitis A virus deltaVP1-P2-P3*my polyprotein fragment + H2O C-terminally truncated protein, proteolytically inactive substrate, kinetics, yields the same products as active polyprotein precursor deltaVP1-P2-P3* Hepatovirus A hepatitis A virus protein 2BC + hepatitis A virus proteins P3*my + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A P3my and deltaVP1-2A are intermediates ?
hepatitis A virus P1-2AB* polyprotein fragment + H2O C-terminally truncated protein, cleavage sites: VPO/VP3, VP3/VP1, 2A/2B, less efficient are VP1/2A and 2B/2C, via 2BC Hepatovirus A hepatitis A virus protein VP3 + hepatitis A virus proteins VP0 + hepatitis A virus proteins VP1-2A + hepatitis A virus proteins VP0-VP3 + hepatitis A virus proteins P1-2A + hepatitis A virus proteins 2A
-
 ?
hepatitis A virus P1-2ABC* polyprotein fragment + H2O C-terminally truncated protein, cleavage sites: VPO/VP3, VP3/VP1, 2A/2B, less efficient are VP1/2A and 2B/2C, via 2BC Hepatovirus A hepatitis A virus protein VP3 + hepatitis A virus proteins VP0 + hepatitis A virus proteins VP1-2A + hepatitis A virus proteins VP0-VP3 + hepatitis A virus proteins P1-2A + hepatitis A virus proteins 2A + hepatitis A virus proteins 2BC
-
 ?
hepatitis A virus P1-P2 precursor polyprotein + H2O most effective cleavage at 2A/2B and 2C/3A sites Hepatovirus A hepatitis A virus protein 2A + hepatitis A virus protein 2B + hepatitis A virus protein 2C + hepatitis A virus protein 3ABC + hepatitis A virus protein 3D via respective intermediate products ?
hepatitis A virus polyprotein + H2O cleavage of P2-P3 domain, cleaves primary cleavage site and all secondary sites within P2 as well as the 3C/3D junction Hepatovirus A hepatitis A virus protein P1-2A + hepatitis A virus protein P3 + hepatitis A virus protein 2BC + hepatitis A virus protein 3D + hepatitis A virus protein 3ABC followed by hepatitis A virus protein 2B and hepatitis A virus protein 2C and later by hepatitis A virus protein VP0 and hepatitis A virus protein VP3, enzyme-concentration dependent product formation ?
hepatitis A virus polyprotein + H2O processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner Hepatovirus A ?
-
 ?
Lys-Gly-Leu-Phe-Ser-Gln-Ala-Lys-Ile-Ser-Leu-Phe-Tyr-Thr + H2O
-
 Hepatovirus A Lys-Gly-Leu-Phe-Ser-Gln + Ala-Lys-Ile-Ser-Leu-Phe-Tyr-Thr
-
 ?

Subunits

Subunits Comment Organism
? x * 26000, SDS-PAGE Hepatovirus A