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Hydrolysis of dipeptide derivatives reveals the diversity in M49 family (CROSBI ID 190887)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Jajčanin Jozić, Nina ; Abramić, Marija Hydrolysis of dipeptide derivatives reveals the diversity in M49 family // Biological chemistry, 394 (2013), 6; 767-771. doi: 10.1515/hsz-2012-0347

Podaci o odgovornosti

Jajčanin Jozić, Nina ; Abramić, Marija

engleski

Hydrolysis of dipeptide derivatives reveals the diversity in M49 family

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.

arylamide substrate; dipeptidyl peptidase III; Saccharomyces cerevisiae; site-directed mutagenesis; zinc-peptidase

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Podaci o izdanju

394 (6)

2013.

767-771

objavljeno

1431-6730

10.1515/hsz-2012-0347

Povezanost rada

Kemija

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