Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F12%3A00007377" target="_blank" >RIV/00023884:_____/12:00007377 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/1873-3468.12798" target="_blank" >http://dx.doi.org/10.1002/1873-3468.12798</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/1873-3468.12798" target="_blank" >10.1002/1873-3468.12798</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH

Popis výsledku v původním jazyce

Mouse acidic mammalian chitinase (AMCase) degrades chitin with highest efficiency at pH 2.0 and is active up to pH 8.0. Here, we report that mouse AMCase also exhibits transglycosylation activity under neutral conditions. We incubated natural and artificial chitin substrates with mouse AMCase at pH 2.0 or 7.0 and analyzed the resulting oligomers using an improved method of fluorescence assisted carbohydrate electrophoresis. Mouse AMCase produces primarily dimers of N-acetyl-D-glucosamine [(GlcNAc)2 ] under both pH conditions while generating transglycosylated (GlcNAc)3 primarily at pH 7.0 and at lower levels at pH 2.0. These results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs. This article is protected by copyright. All rights reserved.

Název v anglickém jazyce

Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH

Popis výsledku anglicky

Mouse acidic mammalian chitinase (AMCase) degrades chitin with highest efficiency at pH 2.0 and is active up to pH 8.0. Here, we report that mouse AMCase also exhibits transglycosylation activity under neutral conditions. We incubated natural and artificial chitin substrates with mouse AMCase at pH 2.0 or 7.0 and analyzed the resulting oligomers using an improved method of fluorescence assisted carbohydrate electrophoresis. Mouse AMCase produces primarily dimers of N-acetyl-D-glucosamine [(GlcNAc)2 ] under both pH conditions while generating transglycosylated (GlcNAc)3 primarily at pH 7.0 and at lower levels at pH 2.0. These results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs. This article is protected by copyright. All rights reserved.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30101 - Human genetics

Projekt

—

Návaznosti

N - Vyzkumna aktivita podporovana z neverejnych zdroju

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Febs Letters

ISSN

0014-5793

e-ISSN

—

Svazek periodika

591

Číslo periodika v rámci svazku

20

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

3310-3318

Kód UT WoS článku

000413767100014

EID výsledku v databázi Scopus

2-s2.0-85031090027