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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

3 Biotech

ISSN

2190-572X

e-ISSN

—

Svazek periodika

11

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

9

Strana od-do

—

Kód UT WoS článku

000629633500003

EID výsledku v databázi Scopus

2-s2.0-85102572400