prikaz prve stranice dokumenta Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron
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doctoral thesis
Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron
Zagreb: University of Zagreb, Faculty of Science, 2018. urn:nbn:hr:217:889715
Sabljić, Igor
University of Zagreb
Faculty of Science
Department of Chemistry

Institutional repository: Repository of the Faculty of Science

Cite this document

Sabljić, I. (2018). Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron (Doctoral thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:889715

Sabljić, Igor. "Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron." Doctoral thesis, University of Zagreb, Faculty of Science, 2018. https://urn.nsk.hr/urn:nbn:hr:217:889715

Sabljić, Igor. "Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron." Doctoral thesis, University of Zagreb, Faculty of Science, 2018. https://urn.nsk.hr/urn:nbn:hr:217:889715

Sabljić, I. (2018). 'Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron', Doctoral thesis, University of Zagreb, Faculty of Science, accessed 25 November 2024, https://urn.nsk.hr/urn:nbn:hr:217:889715

Sabljić I. Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron [Doctoral thesis]. Zagreb: University of Zagreb, Faculty of Science; 2018 [cited 2024 November 25] Available at: https://urn.nsk.hr/urn:nbn:hr:217:889715

I. Sabljić, "Strukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron", Doctoral thesis, University of Zagreb, Faculty of Science, Zagreb, 2018. Available at: https://urn.nsk.hr/urn:nbn:hr:217:889715

Metadata
TitleStrukturna karakterizacija dipeptidil-peptidaze III iz bakterije Bacteroides thetaiotaomicron
Title (english)Structural characterization of dipeptidyl peptidase III from the bacterium Bacteroides thetaiotaomicron
AuthorIgor Sabljić
MentorMarija Luić (mentor)
Committee memberMarko Močibob (predsjednik povjerenstva)
Committee memberMarija Luić (član povjerenstva)
Committee memberDubravka Matković-Čalogović (član povjerenstva)
MBZ: 108862
Committee memberMarija Abramić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2018-06-20, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Universal decimal classification
(UDC)		54 - Chemistry. Crystallography. Mineralogy
Abstract
Dipeptidil-peptidaza III (DPP III) je široko rasprostranjena citosolna metalopeptidaza iz porodice M49, koja odcjepljuje dipeptide s N-kraja peptidnih supstrata. Većina istraživanja o DPP III napravljena je na ortolozima iz eukariota koja ukazuju na njenu opću funkciju u intracelularnom katabolizmu proteina, ulogu u regulaciji boli te odgovoru na oksidativni stres. U ovom radu je strukturno karakterizirana prva prokariotska DPP III, i to iz bakterije Bacteroides thetaiotaomicron, ljudskog simbionta koji nastanjuje tanko i debelo crijevo. Kinetičkom analizom utvrđeno je da je Arg2-2-naftilamid njezin najbolji sintetski supstrat. Elektroforetskim metodama je utvrđeno da pročišćeni proteinski uzorak sadrži tri forme DPP III. Zamjenom svih cisteinskih ostataka u serinske pripremljen je dovoljno homogen uzorak za kristalizaciju bakterijske DPP III. Riješene su strukture u otvorenoj i zatvorenoj konformaciji proteina. Pokazalo se da ovaj protein pripada istoj strukturnoj klasi kao i ljudska i kvaščeva DPP III. S obzirom na gotovo jednako aktivno mjesto može se pretpostaviti i isti mehanizam djelovanja.
Abstract (english)
Dipeptidyl peptidase III (DPP III) is a widespread cytosolic metalopeptidase of the M49 family, which cleaves dipeptides from the N-terminus of its peptide substrates. Previous studies of the DPP III enzyme were focused on eukaryotic orthologs and indicate its general function in the intracellular protein catabolism, pain regulation as well as the response to oxidative stress. In this work, the first prokaryotic DPP III, that from the human gut symbiont bacterium Bacteroides thetaiotaomicron, was structurally characterized. Kinetic analysis showed that Arg2-2-naphthylamide is the preferred synthetic substrate. Electrophoretic methods revealed that the purified protein sample contains three forms. By replacing all cysteine residues with serines, homogeneity of the sample improved enough to enable successful crystallization of the bacterial DPP III. Structures in open and closed conformations were solved and they have the same protein fold as the human and yeast DPP III. Considering the fact that these three enzymes have almost identical active sites, the same mechanism of action can be assumed.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:889715
Study programmeTitle: Doctoral study in chemistry
Study programme type: university
Study level: postgraduate
Academic / professional title: doktor/doktorica znanosti, područje prirodnih znanosti, polje kemija (doktor/doktorica znanosti, područje prirodnih znanosti, polje kemija)
Type of resourceText
Extent105 str. ; 30 cm
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2018-07-10 09:17:59