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
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Czech description
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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
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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
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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
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