Dual substrate specificity of the rutinosidase from aspergillus niger and the role of its substrate tunnel

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F20%3A43926400" target="_blank" >RIV/60461373:22330/20:43926400 - isvavai.cz</a>

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>

Result language

angličtina

Original language name

Dual substrate specificity of the rutinosidase from aspergillus niger and the role of its substrate tunnel

Original language description

Rutinosidases (α-L-rhamnopyranosyl-(1-6)-β-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 from Aspergillus niger (AnRut) is selectively produced in Pichia 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 β-D-glucopyranosidase activity. As a result, new compounds are formed by β-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 recombinant AnRut were analyzed by molecular modeling. We revealed the role of a substrate tunnel in the structure of AnRut, 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). © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

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

Name of the periodical

International Journal of Molecular Sciences

ISSN

1661-6596

e-ISSN

1422-0067

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

1-21

UT code for WoS article

000565060500001

EID of the result in the Scopus database

2-s2.0-85089407984