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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/61989592:15110/12:33141139

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    FR - Pharmacology and apothecary chemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Current Drug Metabolism

  • ISSN

    1389-2002

  • e-ISSN

  • Volume of the periodical

    13

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    13

  • Pages from-to

    130-142

  • UT code for WoS article

    000300417500002

  • EID of the result in the Scopus database