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Literature summary for 3.4.21.39 extracted from

  • Andersson, M.K.; Enoksson, M.; Gallwitz, M.; Hellman, L.
    The extended substrate specificity of the human mast cell chymase reveals a serine protease with well-defined substrate recognition profile (2009), Int. Immunol., 21, 95-104.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens chymase only accepts aromatic amino acids in position P1, with a strong preference for Tyr and Phe over Trp. Aliphatic amino acids are preferred in positions P2 to P4 N-terminal of the cleaved bond. In the P1' position C-terminal of the cleaved bond, Ser is clearly over-represented and acidic amino acids Asp and Glu are strongly preferred in the P2' position. In P3', the small aliphatic amino acids Ala, Val and Gly are frequently observed. ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining
mast cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
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 Homo sapiens methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
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additional information chymase only accepts aromatic amino acids in position P1, with a strong preference for Tyr and Phe over Trp. Aliphatic amino acids are preferred in positions P2 to P4 N-terminal of the cleaved bond. In the P1' position C-terminal of the cleaved bond, Ser is clearly over-represented and acidic amino acids Asp and Glu are strongly preferred in the P2' position. In P3', the small aliphatic amino acids Ala, Val and Gly are frequently observed. Homo sapiens ?
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