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Literature summary for 3.4.24.19 extracted from

  • Wermter, C.; Hoewel, M.; Hintze, V.; Bombosch, B.; Aufenvenne, K.; Yiallouros, I.; Stoecker, W.
    The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains (2007), Biol. Chem., 388, 513-521.
    View publication on PubMed

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the protease domain cleaves other matrix proteins such as fibronectin, collagen I and collagen IV, which are left intact by the full-length enzyme Homo sapiens ?
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thrombospondin-1 + H2O thrombospondin-1 is differently cleaved by both BMP1 and its catalytic domain Homo sapiens ?
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?
truncated procollagen VII + H2O the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. The C-terminal domains of BMP1 are important for substrate recognition and for controlling and restricting its proteolytic activity via exosite binding Homo sapiens ?
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Synonyms

Synonyms Comment Organism
BMP1
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Homo sapiens