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Literature summary for 3.4.22.38 extracted from

  • Ljusberg, J.; Wang, Y.; Lang, P.; Norgard, M.; Dodds, R.; Hultenby, K.; Ek-Rylander, B.; Andersson, G.
    Proteolytic excision of a repressive loop domain in tartrate-resistant acid phosphatase by cathepsin K in osteoclasts (2005), J. Biol. Chem., 280, 28370-28381.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
tartrate-resistant acid phosphatase + H2O Homo sapiens cathepsin K, colocalizes with tartrate-resistant acid phosphatase in osteoclast-resorptive compartments, supporting a role for cathepsin K in the extracellular processing of monomeric tartrate-resistant acid phosphatase in the resorption lacuna ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining
osteoclast cathepsin K, colocalizes with tartrate-resistant acid phosphatase in osteoclast-resorptive compartments, supporting a role for cathepsin K in the extracellular processing of monomeric tartrate-resistant acid phosphatase in the resorption lacuna Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tartrate-resistant acid phosphatase + H2O cathepsin K, colocalizes with tartrate-resistant acid phosphatase in osteoclast-resorptive compartments, supporting a role for cathepsin K in the extracellular processing of monomeric tartrate-resistant acid phosphatase in the resorption lacuna Homo sapiens ?
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tartrate-resistant acid phosphatase + H2O processing by cathepsin K occurs sequentially by an initial excision of the loop peptide Gly143–Gly160 followed by the removal of a Val161–Ala162 dipeptide at the N-terminus of the C-terminal 16-kDa subunit of tartrate-resistant acid phosphatase Homo sapiens ?
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