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Literature summary for 3.4.23.B13 extracted from

  • Konvalinka, J.; Heuser, A.M.; Hruskova-Heidingsfeldova, O.; Vogt, V.M.; Sedlacek, J.; Strop, P.; Krausslich, H.G.
    Proteolytic processing of particle-associated retroviral polyproteins by homologous and heterologous viral proteinases (1995), Eur. J. Biochem., 228, 191-198.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A100L/V104T/R105P/G106V/S107N the mutant with marked preference for HIC-derived peptide substrates does not cleave the HIV-1 polyprotein Avian myeloblastosis-associated virus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information cleavage of ALV PR76Gag and HIV-1 polyprotein is stimulated by high salt concentrations Avian myeloblastosis-associated virus

Organism

Organism UniProt Comment Textmining
Avian myeloblastosis-associated virus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ALV Pr76 Gag + H2O
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Avian myeloblastosis-associated virus ?
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HIV-1 polyprotein + H2O cleavage of the HIV-1 polyprotein only at concentrations above 0.001 mM. Cleavage products are very similar or identical to that of HIV-1 protease Avian myeloblastosis-associated virus ?
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