prikaz prve stranice dokumenta Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1
Access restricted to students and staff of home institution
master's thesis
Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1
2016. urn:nbn:hr:166:014141
Raboteg, Marina
University of Split
Faculty of Science
Department of Chemistry

Cite this document

Raboteg, M. (2016). Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1 (Master's thesis). Split: University of Split, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:166:014141

Raboteg, Marina. "Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1." Master's thesis, University of Split, Faculty of Science, 2016. https://urn.nsk.hr/urn:nbn:hr:166:014141

Raboteg, Marina. "Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1." Master's thesis, University of Split, Faculty of Science, 2016. https://urn.nsk.hr/urn:nbn:hr:166:014141

Raboteg, M. (2016). 'Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1', Master's thesis, University of Split, Faculty of Science, accessed 13 November 2024, https://urn.nsk.hr/urn:nbn:hr:166:014141

Raboteg M. Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1 [Master's thesis]. Split: University of Split, Faculty of Science; 2016 [cited 2024 November 13] Available at: https://urn.nsk.hr/urn:nbn:hr:166:014141

M. Raboteg, "Hidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1", Master's thesis, University of Split, Faculty of Science, Split, 2016. Available at: https://urn.nsk.hr/urn:nbn:hr:166:014141

Please login to the repository to save this object to your list.
Metadata
TitleHidroksilamin kao akceptor aminoacilne skupine kod adenilacijske domene tirocidin-sintetaze 1
Title (english)Hydroxylamine as an acceptor of the aminoacyl group from adenylation domain of tyrocidine synthetase 1
AuthorMarina Raboteg
MentorViljemka Bučević Popović (mentor)
MentorMatilda Šprung (pomoć pri izradi, neposredni voditelj)
Committee memberViljemka Bučević Popović (predsjednik povjerenstva)
Committee memberMatilda Šprung (član povjerenstva)
Committee memberMaja Pavela Vrančić (član povjerenstva)
GranterUniversity of Split
Faculty of Science
(Department of Chemistry)
Split
Defense date and country2016-11-03, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Neribosomske peptid-sintetaze (NRPS) su multifunkcionalni proteini koji nizom enzimskih reakcija kataliziraju sintezu različitih peptidnih spojeva. Prvi korak u biosintezi neribosomski sintetiziranih peptida odabir je i aktivacija aminokiselinskog supstrata od strane adenilacijske (A) domene uz utrošak ATP-a, a drugi korak je prijenos aminokiseline na susjednu tiolacijsku (T) domenu. U ovom radu, A domena proteina TycA (TycA-A), eksprimirana je kao zasebni protein i pročišćena uz pomoć agaroznih zrnaca s ionima kobalta. Ispitana je enzimska aktivnost pročišćenog proteina TycA-A, u prisustvu pripadajućeg (L-Phe) i nepripadajućeg aminokiselinskog supstrata (D-Phe). Nadalje, ispitan je utjecaj hidroksilamina, kao akceptora aktivirane aminokiseline, na brzinu oslobađanja \(PP_{i}\) iz ATP. Ovo istraživanje pokazalo je da se brzina enzimske reakcije u prisustvu hidroksilamina ubrzava za otprilike pet puta, što pokazuje da hidroksilamin može poslužiti kao pogodan nukleofilni akceptor aktivirane aminokiseline.
Abstract (english)
Nonribosomal peptide synthetases (NRPS) are large multifunctional proteins, which via a series of enzymatic reactions catalyse the synthesis of peptide compounds. The first step in nonribosomal peptide biosynthesis is the selection and activation of an amino acid substrate by the adenylation (A) domain, at the expense of ATP. In the second step, the activated amino acid is transferred to the adjacent tiolation (T) domain. In this study, the A domain of tyrocidine synthetase 1 (TycA-A) was expressed as a separate protein and purified using agarose beads containing cobalt ions. The enzyme activity of purified TycA-A was assayed in the presence of cognate (L-Phe) and noncognate (D-Phe) amino acid substrate. In addition, the influence of hydroxylamine as an acceptor of the activated aminoacyl moiety, on \(PP_{i}\) release from ATP was also examined. The results show a fivefold increase of the reaction rate in the presence of hydroxylamine, suggesting that hydroxylamine can be used as a nucleophilic acceptor of the activated amino acid.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:166:014141
Study programmeTitle: Biology and Chemistry; specializations in: major in teaching
Course: major in teaching
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra edukacije biologije i kemije (magistar/magistra edukacije biologije i kemije)
Type of resourceText
File originBorn digital
Access conditionsAccess restricted to students and staff of home institution
Terms of useLicence In copyright icon
Created on2017-06-01 14:34:47