Active site complementation and hexameric arrangement in the GH family 29, a structure-function study of alpha-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F19%3A00510112" target="_blank" >RIV/86652036:_____/19:00510112 - 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 alpha-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

—

Czech description

—

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

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)

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

24

Pages from-to

59-73

UT code for WoS article

000462551800005

EID of the result in the Scopus database

—