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beta-N-Acetylhexosaminidases-the wizards of glycosylation
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SYSNO ASEP 0509795 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title beta-N-Acetylhexosaminidases-the wizards of glycosylation Author(s) Bojarová, Pavla (MBU-M) ORCID
Bruthans, J. (CZ)
Křen, Vladimír (MBU-M) RID, ORCIDSource Title Applied Microbiology and Biotechnology. - : Springer - ISSN 0175-7598
Roč. 103, č. 19 (2019), s. 7869-7881Number of pages 13 s. Language eng - English Country DE - Germany Keywords beta-N-acetylhexosaminidase ; Carbohydrate ; Enzymatic synthesis Subject RIV CE - Biochemistry OECD category Biochemistry and molecular biology R&D Projects LTC17005 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LTC18041 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support MBU-M - RVO:61388971 UT WOS 000485936100004 EID SCOPUS 85070332450 DOI 10.1007/s00253-019-10065-0 Annotation beta-N-Acetylhexosaminidases (EC 3.2.1.52) are a unique family of glycoside hydrolases with dual substrate specificity and a particular reaction mechanism. Though hydrolytic enzymes per se, their good stability, easy recombinant production, absolute stereoselectivity, and a broad substrate specificity predestine these enzymes for challenging applications in carbohydrate synthesis. This mini-review aims to demonstrate the catalytic potential of beta-N-acetylhexosaminidases in a range of unusual reactions, processing of unnatural substrates, formation of unexpected products, and demanding reaction designs. The use of unconventional media can considerably alter the progress of transglycosylation reactions. By means of site-directed mutagenesis, novel catalytic machineries can be constructed. Glycosylation of difficult substrates such as sugar nucleotides was accomplished, and the range of afforded glycosidic bonds comprises unique non-reducing sugars. Specific functional groups may be tolerated in the substrate molecule, which makes beta-N-acetylhexosaminidases invaluable allies in difficult synthetic problems. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2020 Electronic address https://link.springer.com/article/10.1007%2Fs00253-019-10065-0
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