Známé struktury cytochromu P450

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002037" target="_blank" >RIV/61989592:15310/04:00002037 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Lessons from known P450 structures

Popis výsledku v původním jazyce

There is a considerable progress last five years in knowledge of the P450 (CYP) structures which allows to draw out at least some conclusions important for function of the respective enzymes. First, the structure of mammalian (rabbit) liver microsomal CYP2C5 was published in 2000 which allowed for detailed comparisons of all important human liver microsomal P450s. The next milestone was the structure of CYP2C9 presented in full in 2003 showing the first human liver microsomal P450 in the absence as wellas in the presence of substrate. Third success was the resolution of the CYP3A4 structure presented this year. The structures show that although the overall "P450 fold" is preserved, there are considerable differences in the ways the substrates approachthe active site and in the properties of the active site itself. Relative flexibility and openness of the CYP3A4 active site was expected by the modeling as well as by the spectroscopic approaches. The CYP2C9 structure opens a possibilit

Název v anglickém jazyce

Lessons from known P450 structures

Popis výsledku anglicky

There is a considerable progress last five years in knowledge of the P450 (CYP) structures which allows to draw out at least some conclusions important for function of the respective enzymes. First, the structure of mammalian (rabbit) liver microsomal CYP2C5 was published in 2000 which allowed for detailed comparisons of all important human liver microsomal P450s. The next milestone was the structure of CYP2C9 presented in full in 2003 showing the first human liver microsomal P450 in the absence as wellas in the presence of substrate. Third success was the resolution of the CYP3A4 structure presented this year. The structures show that although the overall "P450 fold" is preserved, there are considerable differences in the ways the substrates approachthe active site and in the properties of the active site itself. Relative flexibility and openness of the CYP3A4 active site was expected by the modeling as well as by the spectroscopic approaches. The CYP2C9 structure opens a possibilit

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F99%2F0277" target="_blank" >GA203/99/0277: Cytochrom P-4503A - klíčový enzym matabolismu léčiv. Srovnání lidského enzymu a modelových systémů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

Suppl.

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

198

Kód UT WoS článku

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EID výsledku v databázi Scopus

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