Computational study of beta-N-acetylhexosaminidase from Talaromyces flavus, a glycosidase with high substrate flexibility

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F15%3A43888814" target="_blank" >RIV/60076658:12310/15:43888814 - isvavai.cz</a>

Výsledek na webu

<a href="http://bmcbioinformatics.biomedcentral.com/articles/10.1186/s12859-015-0465-8" target="_blank" >http://bmcbioinformatics.biomedcentral.com/articles/10.1186/s12859-015-0465-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1186/s12859-015-0465-8" target="_blank" >10.1186/s12859-015-0465-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Computational study of beta-N-acetylhexosaminidase from Talaromyces flavus, a glycosidase with high substrate flexibility

Popis výsledku v původním jazyce

Background: beta- N- Acetylhexosaminidase (GH20) from the filamentous fungus Talaromyces flavus, previously identified as a prominent enzyme in the biosynthesis of modified glycosides, lacks a high resolution three-dimensional structure so far. Despite of high sequence identity to previously reported Aspergillus oryzae and Penicilluim oxalicum beta-N-acetylhexosaminidases, this enzyme tolerates significantly better substrate modification. Understanding of key structural features, prediction of effectivemutants and potential substrate characteristics prior to their synthesis are of general interest. Results: Computational methods including homology modeling and molecular dynamics simulations were applied to shad light on the structure-activity relationship in the enzyme. Primary sequence analysis revealed some variable regions able to influence difference in substrate affinity of hexosaminidases. Moreover, docking in combination with consequent molecular dynamics simulations of C-6 mod

Název v anglickém jazyce

Computational study of beta-N-acetylhexosaminidase from Talaromyces flavus, a glycosidase with high substrate flexibility

Popis výsledku anglicky

Background: beta- N- Acetylhexosaminidase (GH20) from the filamentous fungus Talaromyces flavus, previously identified as a prominent enzyme in the biosynthesis of modified glycosides, lacks a high resolution three-dimensional structure so far. Despite of high sequence identity to previously reported Aspergillus oryzae and Penicilluim oxalicum beta-N-acetylhexosaminidases, this enzyme tolerates significantly better substrate modification. Understanding of key structural features, prediction of effectivemutants and potential substrate characteristics prior to their synthesis are of general interest. Results: Computational methods including homology modeling and molecular dynamics simulations were applied to shad light on the structure-activity relationship in the enzyme. Primary sequence analysis revealed some variable regions able to influence difference in substrate affinity of hexosaminidases. Moreover, docking in combination with consequent molecular dynamics simulations of C-6 mod

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

BMC Bioinformatics

ISSN

1471-2105

e-ISSN

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Svazek periodika

16

Číslo periodika v rámci svazku

JAN 28 2015

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

15

Strana od-do

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Kód UT WoS článku

000354554900001

EID výsledku v databázi Scopus

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