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Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases

  1. Author:
    Wlodawer, A.
    Li, M.
    Gustchina, A.
    Oyama, H.
    Dunn, B. M.
    Oda, K.

  2. Author Address

    Natl Canc Inst, Prot Structure Sect, Macromol Crystallog Lab, Ft Detrick, MD 21702 USA Natl Canc Inst, Prot Structure Sect, Macromol Crystallog Lab, Ft Detrick, MD 21702 USA Natl Canc Inst, SAIC Frederick Inc, Basic Res Program, Ft Detrick, MD 21702 USA Kyoto Inst Technol, Dept Appl Biol, Fac Text Sci, Sakyo Ku, Kyoto 6068585, Japan Univ Florida, Dept Biochem & Mol Biol, Gainesville, FL 32610 USA Wlodawer A Natl Canc Inst, Prot Structure Sect, Macromol Crystallog Lab, Ft Detrick, MD 21702 USA
    1. Year: 2003
  2. Journal: Acta Biochimica Polonica
    1. 50
    2. 1
    3. Pages: 81-102
  4. Type of Article: Review
  1. Abstract:

    Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus novo sp. MN-32. The availability of these crystal structures enabled us to model the structure of mammalian CLN2, an enzyme which, when mutated in humans, leads to a fatal neurodegenerative disease. This review compares the structural and enzymatic properties of this newly defined MEROPS family of peptidases, S53, and introduces their new nomenclature.

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