Active Site Complementation and Hexameric Arrangement in the GH Family 29: A Structure-Function Study of α-L-Fucosidase Isoenzyme 1 from Paenibacillus thiaminolyticus.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F19%3A43918196" target="_blank" >RIV/60461373:22330/19:43918196 - isvavai.cz</a>

Result on the web

<a href="https://academic.oup.com/glycob/article/29/1/59/5078562" target="_blank" >https://academic.oup.com/glycob/article/29/1/59/5078562</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/glycob/cwy078" target="_blank" >10.1093/glycob/cwy078</a>

Result language

angličtina

Original language name

Active Site Complementation and Hexameric Arrangement in the GH Family 29: A Structure-Function Study of α-L-Fucosidase Isoenzyme 1 from Paenibacillus thiaminolyticus.

Original language description

alpha-L-Fucosidase isoenzyme 1 from bacterium Paenibacillus thiaminolyticus is a member of the glycoside hydrolase family GH29 capable of cleaving l-fucose from nonreducing termini of oligosaccharides and glycoconjugates. Here we present the first crystal structure of this protein revealing a novel quaternary state within this family. The protein is in a unique hexameric assembly revealing the first observed case of active site complementation by a residue from an adjacent monomer in this family. Mutation of the complementing tryptophan residue caused changes in the catalytic properties including a shift of the pH optimum, a change of affinity to an artificial chromogenic substrate and a decreased reaction rate for a natural substrate. The wild-type enzyme was active on most of the tested naturally occurring oligosaccharides and capable of transglycosylation on a variety of acceptor molecules, including saccharides, alcohols or chromogenic substrates. Mutation of the complementing residue changed neither substrate specificity nor the preference for the type of transglycosylation acceptor molecule; however, the yields of the reactions were lower in both cases. Maltose molecules bound to the enzyme in the crystal structure identified surface carbohydrate-binding sites, possibly participating in binding of larger oligosaccharides.

Czech name

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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

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

—

Continuities

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

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

Name of the periodical

Glycobiology

ISSN

0959-6658

e-ISSN

—

Volume of the periodical

29

Issue of the periodical within the volume

1

Country of publishing house

US - UNITED STATES

Number of pages

15

Pages from-to

59-73

UT code for WoS article

000462551800005

EID of the result in the Scopus database

2-s2.0-85058766539