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Literature summary for 3.4.23.50 extracted from

  • Kraus, B.; Boller, K.; Reuter, A.; Schnierle, B.
    Characterization of the human endogenous retrovirus K Gag protein: Identification of protease cleavage sites (2011), Retrovirology, 8, 21.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
HERV-K Gag polyprotein + H2O processing of HERV-K Gag is dependent on the presence of the functional retroviral protease Homo sapiens ? HERV-K Gag is processed into matrix protein, a short spacer peptide, p15, capsid and nucelocapsid ?
additional information the N-terminal cleavage site for HERV-K capsid protein matches the sequence consistently found at the N-terminus of all retroviral capsid proteins. The other cleavage sites correspond well to the simplified version of a cleavage site as an amino acid stretch that is hydrophobic and both accessible and flexible, i.e. apparently the space between separately folded domainsof Gag Homo sapiens ?
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