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Literature summary for 3.4.21.113 extracted from

  • Lamp, B.; Riedel, C.; Wentz, E.; Tortorici, M.A.; Ruemenapf, T.
    Autocatalytic cleavage within classical swine fever virus NS3 leads to a functional separation of protease and helicase (2013), J. Virol., 87, 11872-11883.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.113

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Classical swine fever virus autocatalytic intramolecular cleavages of the enzyme, overview. Intramolecular cleavage of the peptide bond occurs between Leu1781 and Met1782 is required for activity, but cleavage of the Leu1748/Lys1749 peptide bond yields a proteolytically inactive NS3 fragment ?
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 ?
non-structural protein 4-5 + H2O Classical swine fever virus in trans-cleavage assays using NS4-5 as a substrate, NS3p acts as a fully functional protease that is able to process the polyprotein ?
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 ?

Organism

Organism UniProt Comment Textmining
Classical swine fever virus P19712
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification autocatalytic intramolecular cleavages of the enzyme, overview. One cleavable peptide bond occurs between Leu1781 and Met1782, giving rise to a helicase subunit of 55 kDa and, depending on the substrate, a NS2-3 fragment of 78 kDa, or a NS3 protease subunit of 26 kDa. A second intramolecular cleavage is mapped to the Leu1748/Lys1749 peptide bond that yields a proteolytically inactive NS3 fragment. Deletion of either of the cleavage site residues resultsin a loss ofRNAinfectivity, indicating the functional importance of amino acid identity at the respective positions Classical swine fever virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information autocatalytic intramolecular cleavages of the enzyme, overview. Intramolecular cleavage of the peptide bond occurs between Leu1781 and Met1782 is required for activity, but cleavage of the Leu1748/Lys1749 peptide bond yields a proteolytically inactive NS3 fragment Classical swine fever virus ?
-
 ?
non-structural protein 4-5 + H2O in trans-cleavage assays using NS4-5 as a substrate, NS3p acts as a fully functional protease that is able to process the polyprotein Classical swine fever virus ?
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 ?

Synonyms

Synonyms Comment Organism
nonstructural protein 3
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 Classical swine fever virus
NS3
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 Classical swine fever virus

General Information

General Information Comment Organism
malfunction deletion of Leu1781 results in enzyme inactivation Classical swine fever virus
metabolism internal cleavage within the NS3 moiety is a common process that further extends the functional repertoires of the multifunctional NS2-3 or NS3 and represents another level of the complex polyprotein processing of Flaviviridae Classical swine fever virus
physiological function pivotal for processing of a large portion of the viral polyprotein is a serine protease activity within nonstructural protein 3 that also harbors helicase and NTPase activities essential forRNA replication Classical swine fever virus