Lysosomal cysteine proteinases: Structure and regulation View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999

AUTHORS

Vito Turk , Gregor Gunčar , Dušan Turk

ABSTRACT

Cysteine peptidases (EC 3.4.22) are widely distributed enzymes in animals, plants and microorganisms. There are many distinct families of cysteine peptidases (also called proteinases, proteases, proteolytic enzymes) the largest and best known being the papain family [1, 2]. The papain family consists of peptidases ubiquitous in plant and animal cells. Until recently, information about mammalian papain-like cysteine peptidases has been limited only to lysosomal cathepsins B, H, L and S. While human cathepsins B, H and L are expressed in all tissues, cathepsin S is selectively expressed in antigen presenting cells, indicating a specific role in the activation of the MHC-class II pathway. These enzymes have been purified from different tissues and species, including human, characterised, and their complete amino acid sequences determined [3-5]. They are synthesised as glycosylated precursors and then converted to the mature enzymes by limited proteolysis either by other proteinases or by autocatalysis. The proregion serves as a regulator of catalytic activity. The propeptides of cathepsins B and L have been shown to be potent inhibitors of the mature enzymes [6, 7]. The proregion is also required for the proper folding of the protein [8]. Cathepsins B, H, L and S differ in their specificity, cathepsin L and S being endopeptidases, cathepsin H acting as an aminopeptidase and cathepsin B as a dipeptidyl carboxypeptidase [5]. More... »

PAGES

211-224

References to SciGraph publications

  • 1997-02. Antigen presentation by MHC class II molecules in IMMUNOLOGY AND CELL BIOLOGY
  • 1997-02. Crystal structure of human cathepsin K complexed with a potent inhibitor in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1968-06. Structure of Papain in NATURE
  • 1997-02. Crystal structure of human osteoclast cathepsin K complex with E-64 in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • Book

    TITLE

    Proteases New Perspectives

    ISBN

    978-3-0348-9750-1
    978-3-0348-8737-3

    Author Affiliations

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/978-3-0348-8737-3_15

    DOI

    http://dx.doi.org/10.1007/978-3-0348-8737-3_15

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1044401125


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