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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F12%3A33141136%21RIV13-MSM-15310___
rdf:type
skos:Concept n15:Vysledek
rdfs:seeAlso
http://www.sciencedirect.com/science/article/pii/S0162013412000542
dcterms:description
Human cytochrome P450 2D6 (CYP2D6) is an enzyme of the CYP superfamily responsible for biotransformation of about 20% of drugs of known metabolism containing a basic nitrogen and a planar aromatic ring. Here, we present a combined experimental and computational study on the compressibility and ?exibility of unliganded and quinidine-bound CYP2D6. Experimentally, high-pressure induced Soret band shifts of the enzyme were measured by UV/VIS spectroscopy, while 100 ns all atomic molecular dynamics (MD) simulations in explicit water were used in the computational analysis. We identi?ed sharp differences between ligand-free and quinidine-bound CYP2D6 forms in compressibility, ?exibility parameters and active site solvation. While the unliganded CYP2D6 is compressible, quinidine binding signi?cantly rigidi?es the CYP2D6 active site. In addition, MD simulations show that quinidine binding results in pronounced reductions in active site ?exibility and solvation. Human cytochrome P450 2D6 (CYP2D6) is an enzyme of the CYP superfamily responsible for biotransformation of about 20% of drugs of known metabolism containing a basic nitrogen and a planar aromatic ring. Here, we present a combined experimental and computational study on the compressibility and ?exibility of unliganded and quinidine-bound CYP2D6. Experimentally, high-pressure induced Soret band shifts of the enzyme were measured by UV/VIS spectroscopy, while 100 ns all atomic molecular dynamics (MD) simulations in explicit water were used in the computational analysis. We identi?ed sharp differences between ligand-free and quinidine-bound CYP2D6 forms in compressibility, ?exibility parameters and active site solvation. While the unliganded CYP2D6 is compressible, quinidine binding signi?cantly rigidi?es the CYP2D6 active site. In addition, MD simulations show that quinidine binding results in pronounced reductions in active site ?exibility and solvation.
dcterms:title
Binding of Quinidine Radically Increases the Stability and Decreases the Flexibility of the Cytochrome P450 2D6 Active Site Binding of Quinidine Radically Increases the Stability and Decreases the Flexibility of the Cytochrome P450 2D6 Active Site
skos:prefLabel
Binding of Quinidine Radically Increases the Stability and Decreases the Flexibility of the Cytochrome P450 2D6 Active Site Binding of Quinidine Radically Increases the Stability and Decreases the Flexibility of the Cytochrome P450 2D6 Active Site
skos:notation
RIV/61989592:15310/12:33141136!RIV13-MSM-15310___
n15:predkladatel
n16:orjk%3A15310
n4:aktivita
n20:S n20:P
n4:aktivity
P(ED0030/01/01), P(ED2.1.00/03.0058), P(EE2.3.20.0017), P(GA303/09/1001), P(GD203/09/H046), S
n4:cisloPeriodika
MAY
n4:dodaniDat
n12:2013
n4:domaciTvurceVysledku
n8:3151948 n8:4936094 n8:4203259
n4:druhVysledku
n18:J
n4:duvernostUdaju
n7:S
n4:entitaPredkladatele
n5:predkladatel
n4:idSjednocenehoVysledku
124964
n4:idVysledku
RIV/61989592:15310/12:33141136
n4:jazykVysledku
n19:eng
n4:klicovaSlova
High pressure; Cytochrome P450; Flexibility; Molecular Dynamics; Quinidine; CYP2D6
n4:klicoveSlovo
n11:High%20pressure n11:Quinidine n11:Cytochrome%20P450 n11:Molecular%20Dynamics n11:Flexibility n11:CYP2D6
n4:kodStatuVydavatele
US - Spojené státy americké
n4:kontrolniKodProRIV
[CED8A8787E7A]
n4:nazevZdroje
Journal of Inorganic Biochemistry
n4:obor
n13:FR
n4:pocetDomacichTvurcuVysledku
3
n4:pocetTvurcuVysledku
7
n4:projekt
n14:GD203%2F09%2FH046 n14:ED0030%2F01%2F01 n14:ED2.1.00%2F03.0058 n14:EE2.3.20.0017 n14:GA303%2F09%2F1001
n4:rokUplatneniVysledku
n12:2012
n4:svazekPeriodika
110
n4:tvurceVysledku
Anzenbacher, Pavel Mašek, Vlastimil Berka, Karel Anzenbacherová, Eva Hendrychová, Tereza Otyepka, Michal Lange, Reinhard
n4:wos
000304335700008
s:issn
0162-0134
s:numberOfPages
5
n9:doi
10.1016/j.jinorgbio.2012.02.010
n17:organizacniJednotka
15310