Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00073772" target="_blank" >RIV/00216224:14740/14:00073772 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/14:00435519

Výsledek na webu

<a href="http://glycob.oxfordjournals.org/content/24/12/1301.long" target="_blank" >http://glycob.oxfordjournals.org/content/24/12/1301.long</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/glycob/cwu074" target="_blank" >10.1093/glycob/cwu074</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst

Popis výsledku v původním jazyce

This study is focused on the analysis and mutagenesis of beta-mannosidase from Bacteroides thetaiotaomicron with the aim of broadening its substrate specificity to 2-acetamido-2-deoxy-beta-d-mannopyranosyl (beta-ManNAc) derivatives. Various conformations(4C1, 4H5, and 1S5) of native and modified ligands were docked to the binding site of the protein to determine the most suitable conformation of sugars for further hydrolysis. Key amino acid residues were mutated in silico focusing on stabilizing the acetamido group of beta-ManNAc as well as forming the oxazoline intermediate needed for hydrolysis. The results of large set of 5 ns molecular dynamic simulations showed that the majority of the active site residues are involved in substrate interaction and do not exhibit a higher flexibility except for Asn178. Mutations of Asn178 to alanine and Asp199 to serine could lead to a stabilisation of the acetamido group in the binding site.

Název v anglickém jazyce

Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst

Popis výsledku anglicky

This study is focused on the analysis and mutagenesis of beta-mannosidase from Bacteroides thetaiotaomicron with the aim of broadening its substrate specificity to 2-acetamido-2-deoxy-beta-d-mannopyranosyl (beta-ManNAc) derivatives. Various conformations(4C1, 4H5, and 1S5) of native and modified ligands were docked to the binding site of the protein to determine the most suitable conformation of sugars for further hydrolysis. Key amino acid residues were mutated in silico focusing on stabilizing the acetamido group of beta-ManNAc as well as forming the oxazoline intermediate needed for hydrolysis. The results of large set of 5 ns molecular dynamic simulations showed that the majority of the active site residues are involved in substrate interaction and do not exhibit a higher flexibility except for Asn178. Mutations of Asn178 to alanine and Asp199 to serine could lead to a stabilisation of the acetamido group in the binding site.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Glycobiology

ISSN

0959-6658

e-ISSN

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Svazek periodika

24

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

1301-1311

Kód UT WoS článku

000347410300011

EID výsledku v databázi Scopus

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