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Literature summary for 3.4.21.39 extracted from

  • Kokkonen, J.O.; Vartiainen, M.; Kovanen, P.T.
    Low density lipoprotein degradation by secretory granules of rat mast cells. Sequential degradation of apolipoprotein B by granule chymase and carboxypeptidase A (1986), J. Biol. Chem., 261, 16067-16072.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus proteolytic degradation of low density lipoproteins by mast cell granules results from coordinated action of the two granule-bound enzymes - chymase and carboxypeptidase A. The chymase first cleaves peptides from the apolipoprotein B of low density lipoproteins, and thereafter the carboxypeptidase A cleaves amino acids from the peptides formed ?
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Source Tissue

Source Tissue Comment Organism Textmining
mast cell
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 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information proteolytic degradation of low density lipoproteins by mast cell granules results from coordinated action of the two granule-bound enzymes - chymase and carboxypeptidase A. The chymase first cleaves peptides from the apolipoprotein B of low density lipoproteins, and thereafter the carboxypeptidase A cleaves amino acids from the peptides formed Rattus norvegicus ?
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