Pregled bibliografske jedinice broj: 619103
Hydrolysis of dipeptide derivatives reveals the diversity in M49 family
Hydrolysis of dipeptide derivatives reveals the diversity in M49 family // Biological chemistry, 394 (2013), 6; 767-771 doi:10.1515/hsz-2012-0347 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 619103 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Hydrolysis of dipeptide derivatives reveals the diversity in M49 family
Autori
Jajčanin Jozić, Nina ; Abramić, Marija
Izvornik
Biological chemistry (1431-6730) 394
(2013), 6;
767-771
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
arylamide substrate; dipeptidyl peptidase III; Saccharomyces cerevisiae; site-directed mutagenesis; zinc-peptidase
Sažetak
Dipeptidyl peptidase III (DPP III), a metallopeptidase of the family M49, was first identified (in the pituitary) by its specific cleavage of diarginyl arylamides which have been used as preferred assay substrates until now. Here we examined in parallel the activity of the yeast and human DPP III. Human enzyme preferred Arg2-β- naphthylamide (β-NA) and showed 620-fold higher kcat/Km for this substrate. In contrast, yeast enzyme did not display preference for any of X- Arg-βNA analyzed. The replacement of Gly505 with Asp, resulted in less active, but more selective yeast enzyme form. These results indicate diversity in cleavage specificity in M49 family.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
098-1191344-2938 - Molekularna enzimologija i proteinske interakcije hidrolaza (Abramić, Marija, MZOS ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE
