Expanding Rutinosidase Versatility: Acylated Quercetin Glucopyranosides as Substrates
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00597615" target="_blank" >RIV/61388971:_____/24:00597615 - isvavai.cz</a>
Alternative codes found
RIV/60076658:12310/24:43908842 RIV/60461373:22330/24:43929140
Result on the web
<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cctc.202400028" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cctc.202400028</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/cctc.202400028" target="_blank" >10.1002/cctc.202400028</a>
Alternative languages
Result language
angličtina
Original language name
Expanding Rutinosidase Versatility: Acylated Quercetin Glucopyranosides as Substrates
Original language description
Rutinosidase is a diglycosidase that catalyzes the cleavage of rutinose (alpha-l-Rhap-(1> 6)-beta-d-Glcp) from rutin or other rutinosides. It is also able to cleave beta-glucopyranosides, e. g., isoquercitrin. This enzyme has a strong transglycosylation activity and a remarkable substrate specificity. We have shown that rutinosidase from Aspergillus niger (AnRut) is able to cleave beta-glucopyranosides acylated at C-6 of glucose (6 '-O-acylisoquercitrin) with acetyl, benzoyl, phenylacetyl, phenylpropanoyl, cinnamoyl, vanillyl, galloyl, 4-hydroxybenzoyl and 3-(4-hydroxy-3-methoxyphenyl)propanoyl. The release of the respective 6-acylglucopyranoses was confirmed by HPLC/MS and NMR methods. Selected compounds, i. e., 6 '-O-acetyl, 6 '-O-benzoyl, and 6 '-O-cinnamyl derivatives of isoquercitrin, were also tested as transglycosylation substrates. Only 6 '-acetylisoquercitrin and 6 '-O-benzoylisoquercitrin underwent transglycosylations by AnRut to produce n-butyl 6-acetyl-beta-d-glucopyranoside and n-butyl 6-benzoyl-beta-d-glucopyranoside. Isoquercitrin 6 '-O-cinnamate yielded on hydrolytic product. Molecular modeling based on the crystal structure of AnRut showed that large aromatic moieties at C-6 ' of isoquercitrin block the side tunnel of AnRut leading into its active site and thus hinder the entry of the acceptor substrate for transglycosylation. This study demonstrates the great substrate flexibility of rutinosidase at the glycone site.
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
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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
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ChemCatChem
ISSN
1867-3880
e-ISSN
1867-3899
Volume of the periodical
16
Issue of the periodical within the volume
11
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
e202400028
UT code for WoS article
001179319300001
EID of the result in the Scopus database
2-s2.0-85186410017