Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

čeština

Název v původním jazyce

Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu

Popis výsledku v původním jazyce

Cu-amine oxidases (CAOs) catalyze the oxidative deamination of biogenic amines. An amine, oxygen and water enter into the reaction and the products are corresponding aldehyde, ammonia and hydrogen peroxide. Phenylethylamine oxidase from Arthrobacter globiformis (AGAO) belongs to a group of microbial Cu-amine oxidases. The best substrates are 2-phenylethylamine and tyramine. Three types of AGAO have been studied. "Wild type", i.e. native holoenzyme, and its two mutants K184Q and K354Q, where lysine is replaced with glutamine. These mutants have the same catalytic activity as the "wild type". All three types were provided by prof. Katsuyuki Tanizawa from Institute for Industrial Research, Osaka University, Japan. The main goal of the work was to describethe interaction of AGAO with 2-butyne-1,4-diamine (DABI), an analogue of putrescine and a typical mechanism-based inhibitor of other amine oxidases which is CAO from Pisum sativum (PSAO) 3. The formation of the aminoallenic intermediate i

Název v anglickém jazyce

Mechanism-based inhibition of Cu-amine oxidase from the bacterium Arthrobacter globiformis in the presence of 2-butyne-1,4-diamine

Popis výsledku anglicky

Cu-amine oxidases (CAOs) catalyze the oxidative deamination of biogenic amines. An amine, oxygen and water enter into the reaction and the products are corresponding aldehyde, ammonia and hydrogen peroxide. Phenylethylamine oxidase from Arthrobacter globiformis (AGAO) belongs to a group of microbial Cu-amine oxidases. The best substrates are 2-phenylethylamine and tyramine. Three types of AGAO have been studied. "Wild type", i.e. native holoenzyme, and its two mutants K184Q and K354Q, where lysine is replaced with glutamine. These mutants have the same catalytic activity as the "wild type". All three types were provided by prof. Katsuyuki Tanizawa from Institute for Industrial Research, Osaka University, Japan. The main goal of the work was to describethe interaction of AGAO with 2-butyne-1,4-diamine (DABI), an analogue of putrescine and a typical mechanism-based inhibitor of other amine oxidases which is CAO from Pisum sativum (PSAO) 3. The formation of the aminoallenic intermediate i

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2002

Kód důvěrnosti údajů

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

Název periodika

Chemické listy

ISSN

0009-2770

e-ISSN

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Svazek periodika

96

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

1

Strana od-do

226

Kód UT WoS článku

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EID výsledku v databázi Scopus

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