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

Acta Biochim Pol. 2003;50(1):81-102.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacillus / enzymology*
  • Binding Sites
  • Calcium / metabolism
  • Carboxypeptidases / chemistry*
  • Carboxypeptidases / metabolism*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Humans
  • Mammals
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Pseudomonas / enzymology*
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Carboxypeptidases
  • serine carboxypeptidase
  • sedolisin
  • Calcium