Structural properties of CYP2D6: requirements for substrates and inhibitors

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F14%3A33150428" target="_blank" >RIV/61989592:15310/14:33150428 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15110/14:33150428

Výsledek na webu

<a href="http://www.futuremedicine.com/doi/pdf/10.2217/fmeb2013.13.91" target="_blank" >http://www.futuremedicine.com/doi/pdf/10.2217/fmeb2013.13.91</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2217/9781780844626" target="_blank" >10.2217/9781780844626</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural properties of CYP2D6: requirements for substrates and inhibitors

Popis výsledku v původním jazyce

CYP450 2D6 is a relatively flexible protein with plastic active site structure, allowing binding with high specificity of many different substrates of various sizes. Presence of a basic nitrogen atom at a distance of 5-7 ? from the site of metabolism isoften found in the structure of typical substrates. After substrate binding, the active site structure is changed, embracing the substrate and fixing it in the optimal position for enzyme reaction. The alleles found in the human population that correspond to CYP450 2D6 variants with decreased enzymatic activity possess changed amino acids which, interestingly, do not directly participate in forming the active site. Instead, they probably take part in maintaining other properties of the enzyme, for example in the formation of solvent or substrate access channels.

Název v anglickém jazyce

Structural properties of CYP2D6: requirements for substrates and inhibitors

Popis výsledku anglicky

CYP450 2D6 is a relatively flexible protein with plastic active site structure, allowing binding with high specificity of many different substrates of various sizes. Presence of a basic nitrogen atom at a distance of 5-7 ? from the site of metabolism isoften found in the structure of typical substrates. After substrate binding, the active site structure is changed, embracing the substrate and fixing it in the optimal position for enzyme reaction. The alleles found in the human population that correspond to CYP450 2D6 variants with decreased enzymatic activity possess changed amino acids which, interestingly, do not directly participate in forming the active site. Instead, they probably take part in maintaining other properties of the enzyme, for example in the formation of solvent or substrate access channels.

Druh

C - Kapitola v odborné knize

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/GPP303%2F12%2FP019" target="_blank" >GPP303/12/P019: Mechanismus vstupu a výstupu látek do/z aktivního místa mikrosomálních cytochromů P450 při metabolizmu léčiv</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název knihy nebo sborníku

CYP2D6: Genetics, Pharmacology and Clinical Relevance

ISBN

978-1-78084-462-6

Počet stran výsledku

10

Strana od-do

69-78

Počet stran knihy

153

Název nakladatele

Future Medicine Ltd.

Místo vydání

London

Kód UT WoS kapitoly

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