Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450?

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F12%3A33141139" target="_blank" >RIV/61989592:15310/12:33141139 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15110/12:33141139

Výsledek na webu

<a href="http://dx.doi.org/10.2174/138920012798918372" target="_blank" >http://dx.doi.org/10.2174/138920012798918372</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2174/138920012798918372" target="_blank" >10.2174/138920012798918372</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450?

Popis výsledku v původním jazyce

In the last decades, the structural flexibility of cytochromes P450 has been extensively studied by spectroscopic and in silico methods. Here, both approaches are reviewed and compared. Comparison of both methods indicates that the individual cytochromesP450 differ significantly in the flexibilities of their substrate-binding active sites. This finding probably accounts for the large number of isoforms of these enzymes (there are fifty-seven known cytochrome P450 genes in the human genome) and their functional versatility. On the other hand, most of the known cytochrome P450s have a set of common structural features, with an overall structure consisting of a relatively flexible domain (the distal side), a more rigid domain (the heme-binding core) anda domain on the proximal side of the hemoprotein with intermediate flexibility. Substrate access and product egress channels of CYP enzymes are also important structural elements as the majority of these channels are located in the flexib

Název v anglickém jazyce

Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450?

Popis výsledku anglicky

In the last decades, the structural flexibility of cytochromes P450 has been extensively studied by spectroscopic and in silico methods. Here, both approaches are reviewed and compared. Comparison of both methods indicates that the individual cytochromesP450 differ significantly in the flexibilities of their substrate-binding active sites. This finding probably accounts for the large number of isoforms of these enzymes (there are fifty-seven known cytochrome P450 genes in the human genome) and their functional versatility. On the other hand, most of the known cytochrome P450s have a set of common structural features, with an overall structure consisting of a relatively flexible domain (the distal side), a more rigid domain (the heme-binding core) anda domain on the proximal side of the hemoprotein with intermediate flexibility. Substrate access and product egress channels of CYP enzymes are also important structural elements as the majority of these channels are located in the flexib

Druh

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

CEP obor

FR - Farmakologie a lékárnická chemie

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>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Current Drug Metabolism

ISSN

1389-2002

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

13

Strana od-do

130-142

Kód UT WoS článku

000300417500002

EID výsledku v databázi Scopus

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