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

• Autorzy: Wlodawer A. , Li M. , Gustchina A. , Oyama H. , Dunn B.M. , Oda K.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

enzyme family; sedolisin; serine-carboxyl peptidase; enzymatic property; protein structure; sequence conservation; enzymatic mechanism; structural property

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 1
• Opis fizyczny: p.81-102,fig.

Twórcy

autor

Wlodawer A.

• National Cancer Institute at Frederick, Frederick, MD 21702, USA

autor

Li M.

autor

Gustchina A.

autor

Oyama H.

autor

Dunn B.M.

autor

Oda K.

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