Transglycosylation abilities of beta-D-galactosidases from GH family 2

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F21%3A43923199" target="_blank" >RIV/60461373:22330/21:43923199 - isvavai.cz</a>

Result on the web

<a href="http://doi.org/10.1007/s13205-021-02715-w" target="_blank" >http://doi.org/10.1007/s13205-021-02715-w</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s13205-021-02715-w" target="_blank" >10.1007/s13205-021-02715-w</a>

Result language

angličtina

Original language name

Transglycosylation abilities of beta-D-galactosidases from GH family 2

Original language description

The ability to predict the transglycosylation activity of glycosidases by in silico analysis was investigated. The transglycosylation abilities of 7 different beta-D-galactosidases from GH family 2 were tested experimentally using 7 different acceptors and p-nitrophenyl-beta-D-galactopyranoside as a donor of galactosyl moiety. Similar transglycosylation abilities were confirmed for all enzymes originating from bacteria belonging to Enterobacteriaceae, which were able to use all tested acceptor molecules. Higher acceptor selectivity was observed for all others used bacterial strains. Structure models of all enzymes were constructed using homology modeling. Ligand-docking method was used for enzymes-transglycosylation products models construction and evaluation. Results obtained by in silico analysis were compared with results arisen out of experimental testing. The experiments confirmed that significant differences in transglycosylation abilities are caused by small differences in active sites composition of analyzed enzymes. According to obtained result, it is possible to conclude that homology modeling may serve as a quick starting point for detection or exclusion of enzymes with defined transglycosylation abilities, which can be used for subsequent synthesis of e.g., pharmaceutically interesting glycosides.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2021

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

3 Biotech

ISSN

2190-572X

e-ISSN

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Volume of the periodical

11

Issue of the periodical within the volume

4

Country of publishing house

DE - GERMANY

Number of pages

9

Pages from-to

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UT code for WoS article

000629633500003

EID of the result in the Scopus database

2-s2.0-85102572400