- Tytuł:
- Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
- Autorzy:
-
Wlodawer, Alexander
Li, Mi
Gustchina, Alla
Oyama, Hiroshi
Dunn, Ben
Oda3, Kohei - Powiązania:
- https://bibliotekanauki.pl/articles/1043650.pdf
- Data publikacji:
- 2003
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
enzyme families
sequence conservation
active site
enzymatic machanism
protein structure - Opis:
- 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.
- Źródło:
-
Acta Biochimica Polonica; 2003, 50, 1; 81-102
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł