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Dual Substrate Specificity of the Rutinosidase from Aspergillus nigerand the Role of Its Substrate Tunnel

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901219" target="_blank" >RIV/60076658:12310/20:43901219 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/20:00532691 RIV/61388963:_____/20:00532691

  • Result on the web

    <a href="https://www.mdpi.com/1422-0067/21/16/5671" target="_blank" >https://www.mdpi.com/1422-0067/21/16/5671</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms21165671" target="_blank" >10.3390/ijms21165671</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Dual Substrate Specificity of the Rutinosidase from Aspergillus nigerand the Role of Its Substrate Tunnel

  • Original language description

    Rutinosidases (alpha-l-rhamnopyranosyl-(1-6)-beta-d-glucopyranosidases, EC 3.2.1.168, CAZy GH5) are diglycosidases that cleave the glycosidic bond between the disaccharide rutinose and the respective aglycone. Similar to many retaining glycosidases, rutinosidases can also transfer the rutinosyl moiety onto acceptors with a free -OH group (so-called transglycosylation). The recombinant rutinosidase fromAspergillus niger(AnRut) is selectively produced inPichia pastoris.It can catalyze transglycosylation reactions as an unpurified preparation directly from cultivation. This enzyme exhibits catalytic activity towards two substrates; in addition to rutinosidase activity, it also exhibits beta-d-glucopyranosidase activity. As a result, new compounds are formed by beta-glucosylation or rutinosylation of acceptors such as alcohols or strong inorganic nucleophiles (NaN3). Transglycosylation products with aliphatic aglycones are resistant towards cleavage by rutinosidase, therefore, their side hydrolysis does not occur, allowing higher transglycosylation yields. Fourteen compounds were synthesized by glucosylation or rutinosylation of selected acceptors. The products were isolated and structurally characterized. Interactions between the transglycosylation products and the recombinantAnRut were analyzed by molecular modeling. We revealed the role of a substrate tunnel in the structure ofAnRut, which explained the unusual catalytic properties of this glycosidase and its specific transglycosylation potential.AnRut is attractive for biosynthetic applications, especially for the use of inexpensive substrates (rutin and isoquercitrin).

  • Czech name

  • Czech description

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

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    International Journal of Molecular Sciences

  • ISSN

    1422-0067

  • e-ISSN

  • Volume of the periodical

    21

  • Issue of the periodical within the volume

    16

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    21

  • Pages from-to

  • UT code for WoS article

    000565060500001

  • EID of the result in the Scopus database