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Literature summary for 3.4.22.B15 extracted from

  • Wirblich, C.; Sibilia, M.; Boniotti, M.B.; Rossi, C.; Thiel, H.J.; Meyers, G.
    3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity (1995), J. Virol., 69, 7159-7168.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
upon expression in Escherichia coli, the protease releases itself from larger precursors by proteolytic cleavages at its N and C termini. Cleavage at the N terminus of the protease occurs with low efficiency at E1108-G1109. Cleavage at the C terminus of the protease occurs with low efficiency at the E1251-T1252 bond Rabbit hemorrhagic disease virus

Organism

Organism UniProt Comment Textmining
Rabbit hemorrhagic disease virus
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification upon expression in Escherichia coli, the protease releases itself from larger precursors by proteolytic cleavages at ist N and C termini. Cleavage at the N terminus of the protease occurs with low efficiency at E1108-G1109. Cleavage at the C terminus of the protease occurs with low efficiency at the E1251-T1252 bond Rabbit hemorrhagic disease virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Rabbit hemorrhagic disease virus polyprotein + H2O amino acid at the P1 position is the most important determinant for substrate recognition. Only glutamic acid, glutamine and aspartic acid are tolerated at this position. At the P1' position, glycine, serine, and alanine are preferred, but a number of amino acids with larger side chains are also tolerated. Substitutions at P2 position have little effect on the cleavage efficiency Rabbit hemorrhagic disease virus ?
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