alpha-L-Fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F15%3A43899756" target="_blank" >RIV/60461373:22330/15:43899756 - isvavai.cz</a>
Výsledek na webu
<a href="http://bmcbiotechnol.biomedcentral.com/articles/10.1186/s12896-015-0160-x" target="_blank" >http://bmcbiotechnol.biomedcentral.com/articles/10.1186/s12896-015-0160-x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1186/s12896-015-0160-x" target="_blank" >10.1186/s12896-015-0160-x</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
alpha-L-Fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus
Popis výsledku v původním jazyce
Background: alpha-L-Fucosidases are enzymes involved in metabolism of alpha-L-fucosylated molecules, compounds with a fundamental role in different life essential processes including immune response, fertilization and development, but also in some serious pathological events. According to the CAZy database, these enzymes belong to families 29 and 95. Some of them are also reported to be able to catalyze transglycosylation reactions, during which alpha-L-fucosylated molecules, representing compounds of interest especially for pharmaceutical industry, are formed. Methods: Activity-based screening of a genomic library was used to isolate the gene encoding a novel alpha-L-fucosidase. The enzyme was expressed in E.coli and affinity chromatography was used for purification of His-tagged alpha-L-fucosidase. Standard activity assay was used for enzyme characterization. Thin layer chromatography and mass spectrometry were used for transglycosylation reactions evaluation. Results: Using a genomi
Název v anglickém jazyce
alpha-L-Fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus
Popis výsledku anglicky
Background: alpha-L-Fucosidases are enzymes involved in metabolism of alpha-L-fucosylated molecules, compounds with a fundamental role in different life essential processes including immune response, fertilization and development, but also in some serious pathological events. According to the CAZy database, these enzymes belong to families 29 and 95. Some of them are also reported to be able to catalyze transglycosylation reactions, during which alpha-L-fucosylated molecules, representing compounds of interest especially for pharmaceutical industry, are formed. Methods: Activity-based screening of a genomic library was used to isolate the gene encoding a novel alpha-L-fucosidase. The enzyme was expressed in E.coli and affinity chromatography was used for purification of His-tagged alpha-L-fucosidase. Standard activity assay was used for enzyme characterization. Thin layer chromatography and mass spectrometry were used for transglycosylation reactions evaluation. Results: Using a genomi
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/LD13024" target="_blank" >LD13024: Chemoinformatika pro glykosynthesu</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
BMC Biotechnology
ISSN
1472-6750
e-ISSN
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Svazek periodika
15
Číslo periodika v rámci svazku
27.5.2015
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
7
Strana od-do
36
Kód UT WoS článku
000355089500003
EID výsledku v databázi Scopus
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