Wyniki wyszukiwania

Sortuj według:

Ogranicz wyniki do:

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

100%

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

Acta Biochimica Polonica

2003

tom 50

nr 1

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 aspar- tic 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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Dunn B. M.

1 Gustchina A.

1 Li M.

1 Oda K.

1 Oyama H.

1 Wlodawer A.

1 2003

Wyniki wyszukiwania

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