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Literature summary for 3.4.21.78 extracted from

  • Van Damme, P.; Maurer-Stroh, S.; Hao, H.; Colaert, N.; Timmerman, E.; Eisenhaber, F.; Vandekerckhove, J.; Gevaert, K.
    The substrate specificity profile of human granzyme A (2010), Biol. Chem., 391, 983-997.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
commercial preparation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information characterization of substrate specificity using an N-terminal peptide-centric proteomics technology. Among 260 cleavage sites, a basic residue at P1 position is favored, and P1 arginine is preferred over lysine. P4 shows a preference for Pro, Ala and Val. In P1' position, long linear amino acids with significant hydrophobic character are enriched. Gly is highly favored at P2' position. The substrate repertoires of granzyme A and granzyme B are partially overlapping Homo sapiens ?
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