Aleksandra, Dimitrijevic

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  • Aleksandra, Dimitrijevic (1)
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The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation

Dusan, Velickovic; Nenad, Milosavic; Dejan, Bezbradica; Bihelović, Filip; Segal, Ann Marie; Šegan, Dejan M.; Trbojević-Ivić, Jovana; Aleksandra, Dimitrijevic

(Springer, New York, 2014)

TY  - JOUR
AU  - Dusan, Velickovic
AU  - Nenad, Milosavic
AU  - Dejan, Bezbradica
AU  - Bihelović, Filip
AU  - Segal, Ann Marie
AU  - Šegan, Dejan M.
AU  - Trbojević-Ivić, Jovana
AU  - Aleksandra, Dimitrijevic
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1797
AB  - Our investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation
VL  - 98
IS  - 14
SP  - 6317
EP  - 6328
DO  - 10.1007/s00253-014-5587-9
ER  - 
@article{
author = "Dusan, Velickovic and Nenad, Milosavic and Dejan, Bezbradica and Bihelović, Filip and Segal, Ann Marie and Šegan, Dejan M. and Trbojević-Ivić, Jovana and Aleksandra, Dimitrijevic",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1797",
abstract = "Our investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation",
volume = "98",
number = "14",
pages = "6317-6328",
doi = "10.1007/s00253-014-5587-9"
}
Dusan, V., Nenad, M., Dejan, B., Bihelović, F., Segal, A. M., Šegan, D. M., Trbojević-Ivić, J.,& Aleksandra, D. (2014). The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation.
Applied Microbiology and Biotechnology
Springer, New York., 98(14), 6317-6328.
https://doi.org/10.1007/s00253-014-5587-9
Dusan V, Nenad M, Dejan B, Bihelović F, Segal AM, Šegan DM, Trbojević-Ivić J, Aleksandra D. The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation. Applied Microbiology and Biotechnology. 2014;98(14):6317-6328
Dusan Velickovic, Nenad Milosavic, Dejan Bezbradica, Bihelović Filip, Segal Ann Marie, Šegan Dejan M., Trbojević-Ivić Jovana, Aleksandra Dimitrijevic, "The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation" Applied Microbiology and Biotechnology, 98, no. 14 (2014):6317-6328,
https://doi.org/10.1007/s00253-014-5587-9 .
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