Biochemical properties of human dehydrogenase/reductase (SDR family) member 7
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F14%3A10281978" target="_blank" >RIV/00216208:11160/14:10281978 - isvavai.cz</a>
Výsledek na webu
<a href="http://www.sciencedirect.com/science/article/pii/S0009279713002792" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0009279713002792</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.cbi.2013.11.003" target="_blank" >10.1016/j.cbi.2013.11.003</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Biochemical properties of human dehydrogenase/reductase (SDR family) member 7
Popis výsledku v původním jazyce
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDRmember 11 p-hydroxysteroid dehydrogenase 1 (11 beta-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein
Název v anglickém jazyce
Biochemical properties of human dehydrogenase/reductase (SDR family) member 7
Popis výsledku anglicky
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDRmember 11 p-hydroxysteroid dehydrogenase 1 (11 beta-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein
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/EE2.3.20.0235" target="_blank" >EE2.3.20.0235: Vybudování výzkumného týmu experimentální a aplikované biofarmacie</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2014
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Chemico-Biological Interactions
ISSN
0009-2797
e-ISSN
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Svazek periodika
207
Číslo periodika v rámci svazku
January
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
6
Strana od-do
52-57
Kód UT WoS článku
000330260700009
EID výsledku v databázi Scopus
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