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

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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 cytochromes P450 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) and a 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 flexible distal side; the location, flexibility, and function of these channels are discussed. 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 cytochromes P450 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) and a 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 flexible distal side; the location, flexibility, and function of these channels are discussed. (en)
Title	Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450? Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450? (en)
skos:prefLabel	Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450? Is There a Relationship Between the Substrate Preferences and Structural Flexibility of Cytochromes P450? (en)
skos:notation	RIV/61989592:15310/12:33141139!RIV13-MSM-15310___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(ED0030/01/01), P(ED2.1.00/03.0058), P(EE2.3.20.0017), P(GA303/09/1001), P(LC512), Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika	2
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Otyepka, Michal Berka, Karel
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	143096
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/12:33141139
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Substrate Selectivity; Protein Dynamics; Molecular Dynamics; Flexibility; Cytochrome P450 (en)
http://linked.open.../riv/klicoveSlovo	Molecular Dynamics Protein Dynamics Substrate Selectivity Cytochrome P450 Flexibility
http://linked.open...odStatuVydavatele	NL - Nizozemsko
http://linked.open...ontrolniKodProRIV	[2E612A198701]
http://linked.open...i/riv/nazevZdroje	Current Drug Metabolism
http://linked.open...in/vavai/riv/obor	FR
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	3 (xsd:int)
http://linked.open...vavai/riv/projekt	Structural Determinants of Substrate Specificity of Human Cytochromes P450 Biomedicine for regional development and human resources Regional Centre of Advanced Technologies and Materials Center for biomolecules and complex molecular systems Research team development of the Regional Centre of Advanced Technologies and Materials
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	13
http://linked.open...iv/tvurceVysledku	Otyepka, Michal Anzenbacher, Pavel Berka, Karel
http://linked.open...ain/vavai/riv/wos	000300417500002
http://linked.open...n/vavai/riv/zamer	Modulation of signalling and regulatory pathways in normal and cancer cells
issn	1389-2002
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.2174/138920012798918372
http://localhost/t...ganizacniJednotka	15310

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