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- W560096189 abstract "Publisher Summary This chapter presents an overview of the structural chemistry of procollagen N-endopeptidase. Procollagen N-endopeptidase was initially identified with the help of a genetic disease in cattle, dermatosparaxis. The enzyme removes the N-terminal propeptide from procollagen I and procollagen II prior to deposition of the collagen molecule in fibrils in the extracellular space. Because of an alternative splicing mechanism, the human enzyme can be synthesized under two different forms. The long form (1,211 amino acids) is composed, among other domains, of a signal peptide, a pro domain, a metalloprotease domain and a disintegrin module displaying homology with similar domains in ADAMs, and four domains homologous to thrombospondin type I repeats. The short form (566 amino acids) possess the metalloprotease domain but lacks the C-terminal half of the protein (His544-Phel211), which is replaced by a different 23-amino acid sequence. This truncated enzyme does not display procollagen I/II N-endopeptidase activity, suggesting a role for the missing domains either in the correct folding of the enzyme or in its interaction with the substrate." @default.
- W560096189 created "2016-06-24" @default.
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- W560096189 date "2004-01-01" @default.
- W560096189 modified "2023-10-13" @default.
- W560096189 title "Procollagen N-endopeptidase, ADAMTS2" @default.
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- W560096189 doi "https://doi.org/10.1016/b978-0-12-079611-3.50224-x" @default.
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