Access to both anomers of rutinosyl azide using wild-type rutinosidase and its catalytic nucleophile mutant
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00541617" target="_blank" >RIV/61388971:_____/21:00541617 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14740/21:00124509
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S1566736720302697" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1566736720302697</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.catcom.2020.106193" target="_blank" >10.1016/j.catcom.2020.106193</a>
Alternative languages
Result language
angličtina
Original language name
Access to both anomers of rutinosyl azide using wild-type rutinosidase and its catalytic nucleophile mutant
Original language description
Rutinosidases hydrolyze beta-rutinosylated flavonoids. As retaining glycosidases they also have a transglycosylation activity. Here we show that two newly identified wild-type rutinosidases, which are members of the glycoside hydrolase family 5-23, are capable of glycosylation of an inorganic azide with rutin as a glycosyl donor, yielding rutinosyl alpha-azide. On the other hand, rutinosyl beta-azide was synthesized by the catalytic nucleophile mutant of the rutinosidase from Aspergillus niger, which also belongs to GH5-23. Thus, we were able to synthesize at a preparatory scale both anomers of rutinosyl azide from rutin using either wild-type or mutant rutinosidases of GH5-23.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Catalysis Communication
ISSN
1566-7367
e-ISSN
1873-3905
Volume of the periodical
149
Issue of the periodical within the volume
JAN 15
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
5
Pages from-to
106193
UT code for WoS article
000600589400006
EID of the result in the Scopus database
2-s2.0-85092636727