Aktivní místa cytochromů P450: Jak vypadají?

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F08%3A00007586" target="_blank" >RIV/61989592:15110/08:00007586 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/08:00005286

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Active Sites of cytochromes P450: What are They like?

Popis výsledku v původním jazyce

Although the x-ray crystallography is giving a relatively precise picture of spatial arrangement of the majority of protein structure, it is not able to give detailed information on the flexibility of the protein active site. The properties of active sites of cytochromes P450 (CYP) were supposed earlier to be relatively similar, reflecting the substrate specificities of the individual enzymes mainly by the amino acid residues present in the respective active site. On the other hand, the most recent experimental as well as theoretical results document that it is the flexibility of this part of protein which gives the active site the property to bind substrates correctly and to accommodate them. It is also the flexibility or plasticity of the structure which determines or limits the property of the protein to keep the conformation which guarantees the function of the enzyme.

Název v anglickém jazyce

Active Sites of cytochromes P450: What are They like?

Popis výsledku anglicky

Although the x-ray crystallography is giving a relatively precise picture of spatial arrangement of the majority of protein structure, it is not able to give detailed information on the flexibility of the protein active site. The properties of active sites of cytochromes P450 (CYP) were supposed earlier to be relatively similar, reflecting the substrate specificities of the individual enzymes mainly by the amino acid residues present in the respective active site. On the other hand, the most recent experimental as well as theoretical results document that it is the flexibility of this part of protein which gives the active site the property to bind substrates correctly and to accommodate them. It is also the flexibility or plasticity of the structure which determines or limits the property of the protein to keep the conformation which guarantees the function of the enzyme.

Druh

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

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

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

Název periodika

Acta Chimica Slovenica

ISSN

1318-0207

e-ISSN

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Svazek periodika

55

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

SI - Slovinská republika

Počet stran výsledku

4

Strana od-do

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Kód UT WoS článku

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EID výsledku v databázi Scopus

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