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Molecular basis for the thiol sensitivity of yeast dipeptidyl peptidase III (CROSBI ID 566962)

Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija

Jajčanin-Jozić, Nina ; Abramić, Marija Molecular basis for the thiol sensitivity of yeast dipeptidyl peptidase III // The FEBS journal / Perham, Richard (ur.). 2010. str. 283-284

Podaci o odgovornosti

Jajčanin-Jozić, Nina ; Abramić, Marija

engleski

Molecular basis for the thiol sensitivity of yeast dipeptidyl peptidase III

Dipeptidyl peptidases III (DPP III) are zinc-dependent enzymes that cleave dipeptides sequentially from the N-terminus of its substrates. In vitro metallopeptidases of this family (DPP III family, peptidase family M49) display a broad specificity towards peptides, but their in vivo substrates are mostly unknown, although physiological role in intracellular protein catabolism, pain-regulation and endogenous defense against oxidative stress is indicated. General feature of all DPPs III is inhibition by thiol reagents, implying the presence of reactive cysteine residues in, or near their active site. Since there is no absolutely conserved Cys in M49 family, and all known members are multi cysteine proteins, the identity of sulfhydryl group(s) important for activity is still speculative and could be species-specific. To address this topic, we conducted a mutational analysis of all five cysteine residues within the yeast ortholog of this family. Yeast Saccharomyces cerevisiae DPP III is a two-domain protein, highly sensitive to sulfhydryl-blocking reagents. Two cysteine residues are located in lower domain (position 113 and 130), and three in the upper domain (position 518, 626 and 639). Although there was no significant change in catalytic efficiency between the wild-type and any of Cys to Ser mutated forms, dramatic difference in sensitivity towards thiol-blocking reagents was observed. Our results showed that inactivation of wild-type yeast DPP III with 4, 4'-dithiodipyridine (DTDP) was a result of modification of two SH-groups, belonging to Cys518 and Cys639. However, only C639S protein variant showed high resistance to inactivation by para-hydroxy-mercuribenzoate (pHMB). Inspection of 1.95 Å-crystal structure of yeast DPP III revealed that Cys639 is situated in a positively charged environment which presumably enhances its ionization to thiolate anion and thereby influences its reactivity.

yeast dipeptidyl peptidase III; reactive cysteine residues; crystal structure

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Podaci o prilogu

283-284.

2010.

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objavljeno

Podaci o matičnoj publikaciji

The FEBS journal

Perham, Richard

Oxford: Wiley-Blackwell

1742-464X

Podaci o skupu

35th FEBS Congress: Molecules of life

poster

26.06.2010-01.07.2010

Göteborg, Švedska

Povezanost rada

Kemija

Indeksiranost