Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
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.
Wlodawer
Alexander
A
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA. wlodawer@ncifcrf.gov
Li
Mi
M
Gustchina
Alla
A
Oyama
Hiroshi
H
Dunn
Ben M
BM
Oda
Kohei
K
D000595:Amino Acid Sequence; D000818:Animals; D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002268:Carboxypeptidases / Q000737:chemistry* / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D008322:Mammals; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011549:Pseudomonas / Q000201:enzymology*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D000091346:Tripeptidyl-Peptidase 1
D000091346:Tripeptidyl-Peptidase 1; D002268:Carboxypeptidases; C000717267:TPP1 protein, human; C022633:serine carboxypeptidase; C479198:sedolisin; D002118:Calcium