Velickovic, D.

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Authority KeyName Variants
45dda478-0671-4417-aeb6-46e7566aaf7c
  • Velickovic, D. (1)
  • Velickovic, D. V. (1)
Projects

Author's Bibliography

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

Pavlović, Marijana; Dimitrijevic, A.; Trbojević-Ivić, Jovana; Milosavic, N.; Gavrović-Jankulović, Marija; Bezbradica, Dejan; Velickovic, D.

(Maik Nauka/Interperiodica/Springer, New York, 2013)

TY  - JOUR
AU  - Pavlović, Marijana
AU  - Dimitrijevic, A.
AU  - Trbojević-Ivić, Jovana
AU  - Milosavic, N.
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Velickovic, D.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1432
AB  - 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.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Russian Journal of Physical Chemistry A
T1  - A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae
VL  - 87
IS  - 13
SP  - 2285
EP  - 2288
DO  - 10.1134/S0036024413130207
ER  - 
@article{
author = "Pavlović, Marijana and Dimitrijevic, A. and Trbojević-Ivić, Jovana and Milosavic, N. and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Velickovic, D.",
year = "2013",
abstract = "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.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Russian Journal of Physical Chemistry A",
title = "A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae",
volume = "87",
number = "13",
pages = "2285-2288",
doi = "10.1134/S0036024413130207"
}
Pavlović, M., Dimitrijevic, A., Trbojević-Ivić, J., Milosavic, N., Gavrović-Jankulović, M., Bezbradica, D.,& Velickovic, D.. (2013). A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae. in Russian Journal of Physical Chemistry A
Maik Nauka/Interperiodica/Springer, New York., 87(13), 2285-2288.
https://doi.org/10.1134/S0036024413130207
Pavlović M, Dimitrijevic A, Trbojević-Ivić J, Milosavic N, Gavrović-Jankulović M, Bezbradica D, Velickovic D. A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae. in Russian Journal of Physical Chemistry A. 2013;87(13):2285-2288.
doi:10.1134/S0036024413130207 .
Pavlović, Marijana, Dimitrijevic, A., Trbojević-Ivić, Jovana, Milosavic, N., Gavrović-Jankulović, Marija, Bezbradica, Dejan, Velickovic, D., "A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae" in Russian Journal of Physical Chemistry A, 87, no. 13 (2013):2285-2288,
https://doi.org/10.1134/S0036024413130207 . .
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Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase

Velickovic, D. V.; Dimitrijevic, A. S.; Bihelović, Filip; Jankov, Ratko M.; Milosavic, N.

(Maik Nauka/Interperiodica/Springer, New York, 2011)

TY  - JOUR
AU  - Velickovic, D. V.
AU  - Dimitrijevic, A. S.
AU  - Bihelović, Filip
AU  - Jankov, Ratko M.
AU  - Milosavic, N.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1231
AB  - One of the key elements for understanding enzyme reactions is determination of its kinetic parameters. Since transglucosylation is kinetically controlled reaction, besides the reaction of synthesis, very important is the reaction of enzymatic hydrolysis of created product. Therefore, in this study, kinetic parameters for synthesis and secondary hydrolysis of pharmacologically active alpha isosalicin by baker's yeast maltase were calculated, and it was shown that specifity of maltase for hydrolysis is approximately 150 times higher then for synthesis.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Russian Journal of Physical Chemistry A
T1  - Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase
VL  - 85
IS  - 13
SP  - 2317
EP  - 2321
DO  - 10.1134/S0036024411130346
ER  - 
@article{
author = "Velickovic, D. V. and Dimitrijevic, A. S. and Bihelović, Filip and Jankov, Ratko M. and Milosavic, N.",
year = "2011",
abstract = "One of the key elements for understanding enzyme reactions is determination of its kinetic parameters. Since transglucosylation is kinetically controlled reaction, besides the reaction of synthesis, very important is the reaction of enzymatic hydrolysis of created product. Therefore, in this study, kinetic parameters for synthesis and secondary hydrolysis of pharmacologically active alpha isosalicin by baker's yeast maltase were calculated, and it was shown that specifity of maltase for hydrolysis is approximately 150 times higher then for synthesis.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Russian Journal of Physical Chemistry A",
title = "Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase",
volume = "85",
number = "13",
pages = "2317-2321",
doi = "10.1134/S0036024411130346"
}
Velickovic, D. V., Dimitrijevic, A. S., Bihelović, F., Jankov, R. M.,& Milosavic, N.. (2011). Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase. in Russian Journal of Physical Chemistry A
Maik Nauka/Interperiodica/Springer, New York., 85(13), 2317-2321.
https://doi.org/10.1134/S0036024411130346
Velickovic DV, Dimitrijevic AS, Bihelović F, Jankov RM, Milosavic N. Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase. in Russian Journal of Physical Chemistry A. 2011;85(13):2317-2321.
doi:10.1134/S0036024411130346 .
Velickovic, D. V., Dimitrijevic, A. S., Bihelović, Filip, Jankov, Ratko M., Milosavic, N., "Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase" in Russian Journal of Physical Chemistry A, 85, no. 13 (2011):2317-2321,
https://doi.org/10.1134/S0036024411130346 . .
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