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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001556" target="_blank" >RIV/61989592:15310/02:00001556 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

čeština

Original language name

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

Original language description

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

Czech name

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

Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2002

Confidentiality

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

Name of the periodical

Chemické listy

ISSN

0009-2770

e-ISSN

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Volume of the periodical

96

Issue of the periodical within the volume

4

Country of publishing house

CZ - CZECH REPUBLIC

Number of pages

1

Pages from-to

226

UT code for WoS article

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EID of the result in the Scopus database

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