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A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae

Samo za registrovane korisnike
2013
1430.pdf (247.4Kb)
Autori
Pavlović, M.
Dimitrijevic, A.
Trbojević-Ivić, Jovana
Milosavic, N.
Gavrović-Jankulović, Marija
Bezbradica, D.
Velickovic, D.
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentu
Apstrakt
alpha-1,4-Glucosidase from Saccharomyces cerevisiae is an enzyme which is widely used in synthesis of different drugs. Glucosidase inhibitors are studied as potential drugs for prevention of HIV and diabetes. For understanding of these processes it is very important to have insights in the transglucosylation activity of this enzyme. In this paper the kinetics of transglucosylation reaction catalyzed by this enzyme in the synthesis of benzyl alcohol glucoside was studied and all relevant kinetic constants for this system are found. It was shown one additional property of transglycosylation reactions catalyzed by glycosidases-inhibition by both, glucose acceptor and glucose donor, and mechanisms for these inhibitions were proposed.
Ključne reči:
alpha-glucosidase / transglucosylation / benzyl alcohol glucoside / substrate inhibition / ping-pong mechanisam
Izvor:
Russian Journal of Physical Chemistry A, 2013, 87, 13, 2285-2288
Izdavač:
  • Maik Nauka/Interperiodica/Springer, New York
Projekti:
  • Alergeni, antitela, enzimi i mali fiziološki značajni molekuli: dizajn, struktura, funkcija i značaj (RS-172049)
  • Razvoj novih inkapsulacionih i enzimskih tehnologija za proizvodnju biokatalizatora i biološki aktivnih komponenata hrane u cilju povećanja njene konkurentnosti, kvaliteta i bezbednosti (RS-46010)
  • Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)

DOI: 10.1134/S0036024413130207

ISSN: 0036-0244

WoS: 000326718200028

Scopus: 2-s2.0-84888146485
[ Google Scholar ]
URI
http://cherry.chem.bg.ac.rs/handle/123456789/1432
Kolekcije
  • Radovi
  • Radovi
Institucija
Hemijski fakultet

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