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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F12%3A33141139%21RIV13-MSM-15310___
rdf:type
n13:Vysledek skos:Concept
dcterms: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.
dcterms: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?
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?
skos:notation
RIV/61989592:15310/12:33141139!RIV13-MSM-15310___
n13:predkladatel
n19:orjk%3A15310
n3:aktivita
n5:P n5:Z
n3:aktivity
P(ED0030/01/01), P(ED2.1.00/03.0058), P(EE2.3.20.0017), P(GA303/09/1001), P(LC512), Z(MSM6198959216)
n3:cisloPeriodika
2
n3:dodaniDat
n7:2013
n3:domaciTvurceVysledku
n4:3151948 n4:4936094
n3:druhVysledku
n21:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n17:predkladatel
n3:idSjednocenehoVysledku
143096
n3:idVysledku
RIV/61989592:15310/12:33141139
n3:jazykVysledku
n20:eng
n3:klicovaSlova
Substrate Selectivity; Protein Dynamics; Molecular Dynamics; Flexibility; Cytochrome P450
n3:klicoveSlovo
n9:Substrate%20Selectivity n9:Protein%20Dynamics n9:Cytochrome%20P450 n9:Molecular%20Dynamics n9:Flexibility
n3:kodStatuVydavatele
NL - Nizozemsko
n3:kontrolniKodProRIV
[2E612A198701]
n3:nazevZdroje
Current Drug Metabolism
n3:obor
n18:FR
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
3
n3:projekt
n10:ED2.1.00%2F03.0058 n10:ED0030%2F01%2F01 n10:EE2.3.20.0017 n10:GA303%2F09%2F1001 n10:LC512
n3:rokUplatneniVysledku
n7:2012
n3:svazekPeriodika
13
n3:tvurceVysledku
Berka, Karel Anzenbacher, Pavel Otyepka, Michal
n3:wos
000300417500002
n3:zamer
n12:MSM6198959216
s:issn
1389-2002
s:numberOfPages
13
n6:doi
10.2174/138920012798918372
n15:organizacniJednotka
15310