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undergraduate thesis
Usmjerena evolucija triptofan-sintaze
Zagreb: University of Zagreb, Faculty of Science, 2019. urn:nbn:hr:217:581974
Buljan, Iva
University of Zagreb
Faculty of Science
Department of Biology

Institutional repository: Repository of the Faculty of Science

Cite this document

Buljan, I. (2019). Usmjerena evolucija triptofan-sintaze (Undergraduate thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:581974

Buljan, Iva. "Usmjerena evolucija triptofan-sintaze." Undergraduate thesis, University of Zagreb, Faculty of Science, 2019. https://urn.nsk.hr/urn:nbn:hr:217:581974

Buljan, Iva. "Usmjerena evolucija triptofan-sintaze." Undergraduate thesis, University of Zagreb, Faculty of Science, 2019. https://urn.nsk.hr/urn:nbn:hr:217:581974

Buljan, I. (2019). 'Usmjerena evolucija triptofan-sintaze', Undergraduate thesis, University of Zagreb, Faculty of Science, accessed 26 August 2024, https://urn.nsk.hr/urn:nbn:hr:217:581974

Buljan I. Usmjerena evolucija triptofan-sintaze [Undergraduate thesis]. Zagreb: University of Zagreb, Faculty of Science; 2019 [cited 2024 August 26] Available at: https://urn.nsk.hr/urn:nbn:hr:217:581974

I. Buljan, "Usmjerena evolucija triptofan-sintaze", Undergraduate thesis, University of Zagreb, Faculty of Science, Zagreb, 2019. Available at: https://urn.nsk.hr/urn:nbn:hr:217:581974

Metadata
TitleUsmjerena evolucija triptofan-sintaze
Title (english)Directed evolution of tryptophan synthase
AuthorIva Buljan
MentorIta Gruić-Sovulj (mentor)
GranterUniversity of Zagreb
Faculty of Science
(Department of Biology)
Zagreb
Defense date and country2019-07-04, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Biology
Abstract
Enzimi su jedne od najfascinantnijih bioloških makromolekula zbog ogromne efikasnosti i brzine kataliziranja velikog spektra kemijskih reakcija. Zbog raznovrsnih upotreba enzima u bioindustriji i molekularnoj biologiji, dizajn novih visokoefikasnih enzima je vrlo značajno područje istraživanja. Osobito je izazovno iskorištavanje oligomernih enzima sa složenom alosteričkom regulacijom čija moć drastično pada kada se katalitičke podjedinice odvoje od svojih proteinskih partnera. Modelni enzim za istraživanje alosterički reguliranih proteina je triptofan-sintaza, enzim koji sintetizira zadnji korak u biosintezi triptofana kod mnogih bakterija i kvasaca. Usmjerena evolucija je pristup dizajnu enzima s poboljšanim svojstvima koji se temelji na generiranju varijabilnosti i primjeni odabranog selektivnog pritiska. Ovim pristupom je dizajnirana samostalna katalitička beta podjedinica triptofan-sintaze koja ima veliki potencijal u sintezi nekanonskih aminokiselina.
Abstract (english)
Enzymes are one of the most fascinating macromolecules due to their high efficiency and broad range of catalytic abilities. Since enzymes have numerous applications in bioindustry and molecular biology, design of highly efficient enzymes is a significant area of research. Usage of oligomeric enzymes with complex allosterical regulation turned out to be especially challenging since catalytic power of the subunits drops dramatically when they are separated from their protein partners. A model enzyme for allosterically regulated enzymes is tryptophan synthase, which catalysis the last step in tryptophan biosynthesis in numerous bacteria and yeasts. Directed evolution is a novel approach in enzyme design that combines generation of genetic variations with use of defined selective pressure to generate protein library. By applying directed evolution, group of scientists succeeded in optimizing tryptophan synthase beta subunit to have stand-alone catalytic power.
Keywords
Languagecroatian
URN:NBNurn:nbn:hr:217:581974
Study programmeTitle: Molecular Biology
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) molekularne biologije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) molekularne biologije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
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Created on2019-12-02 13:45:40