About: Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Spektroskopické metody ukazují rozdíly ve flexibilitě a stabilitě P450. Nejflexibilnější místo bylo nalezeno u enzymu CYP3A4. Aktivní místo tohoto enzymu se snadno denaturuje při hydrostatickém tlaku. Nejpevnější aktivní místo je schopné odolat účinku vysokého tlaku a má jej CYP1A2. Bakteriální flavocytochrom CYP102 (BM3) má také spíše stabilní , ale flexibilní aktivní místo. (cs) Spectroscopic methods reveal differences in flexibility and stability of P450 forms. Among microsomal P450s, the most flexible active site has been found in the CYP3A4 enzyme as it is compressible and the heme vinyl side chains may adopt two different conformations. On the other hand, active site of this enzyme denatures quite easily upon hydrostatic pressure. The most rigid active site able to withstand the effect of high pressure has CYP1A2. The bacterial CYP102 (BM3) flavocytochrome has also a rather stable, but flexible active site. The differences between CYP3A4 and CYP1A2 active sites apparently reflect their ability to bind various substrates: whereas the CYP3A4 binds a vast variety of structures, the CYP1A2 preferentially binds planar, aromatic structures and its substrate specificity is relatively narrow. Spectroscopic methods reveal differences in flexibility and stability of P450 forms. Among microsomal P450s, the most flexible active site has been found in the CYP3A4 enzyme as it is compressible and the heme vinyl side chains may adopt two different conformations. On the other hand, active site of this enzyme denatures quite easily upon hydrostatic pressure. The most rigid active site able to withstand the effect of high pressure has CYP1A2. The bacterial CYP102 (BM3) flavocytochrome has also a rather stable, but flexible active site. The differences between CYP3A4 and CYP1A2 active sites apparently reflect their ability to bind various substrates: whereas the CYP3A4 binds a vast variety of structures, the CYP1A2 preferentially binds planar, aromatic structures and its substrate specificity is relatively narrow. (en)
Title	Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy (en) Rozdíly flexibility aktivních míst cytochromu P450 testované rezonancí Raman a UV-Vis absorpční spektroskopií (cs)
skos:prefLabel	Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy (en) Rozdíly flexibility aktivních míst cytochromu P450 testované rezonancí Raman a UV-Vis absorpční spektroskopií (cs)
skos:notation	RIV/61989592:15110/01:00006967!RIV09-MSM-15110___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA203/99/0277), Z(MSM 151100001)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2009
http://linked.open...aciTvurceVysledku	ANZENBACHER, Pavel
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 / Lékařská fakulta
http://linked.open...dnocenehoVysledku	677735
http://linked.open...ai/riv/idVysledku	RIV/61989592:15110/01:00006967
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	P450; CYP1A2; Resonance Raman spectroscopy; Active site (en)
http://linked.open.../riv/klicoveSlovo	CYP1A2 P450 Active site Resonance Raman spectroscopy
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[800F1C443393]
http://linked.open...i/riv/nazevZdroje	Journal of Inorganic Biochemistry
http://linked.open...in/vavai/riv/obor	FR
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	2 (xsd:int)
http://linked.open...vavai/riv/projekt	Cytochrome P450 3A - key enzyme of drug metabolism. Comparison of the human enzyme and of the model system
http://linked.open...UplatneniVysledku	2001
http://linked.open...v/svazekPeriodika	87
http://linked.open...iv/tvurceVysledku	Hudeček, Jiří Anzenbacher, Pavel
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20151100001
issn	0162-0134
number of pages	5 (xsd:int)
http://localhost/t...ganizacniJednotka	15110

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 58 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software