A study on the reactions of plant copper amine oxidase with short-chain aliphatic diamines

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F01%3A00001377" target="_blank" >RIV/61989592:15310/01:00001377 - isvavai.cz</a>

Alternative codes found

RIV/61989592:15310/01:00007753

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

A study on the reactions of plant copper amine oxidase with short-chain aliphatic diamines

Original language description

Biogenic amines are widely distributed in living organisms. They have been proposed to play an important role in processes of growth, cell division and differentiation. Copper amine oxidases (CAOs; EC 1.4.3.6) concerned with their catabolism are ubiquitous enzymes. CAOs catalyse the oxidative deamination of amines to the corresponding aldehydes, ammonia and H2O2. The enzymes are homodimers containing both topaquinone cofactor and a Cu(II) ion at the active site of each subunit. The crystal structures ofseveral CAOs have been reported and the catalytic cycle elucidated.

Czech name

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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

<a href="/en/project/ME%20153" target="_blank" >ME 153: Principles and applications of diverse amine oxidizing enzymes with different prosthetic groups from plants and microorganisms.</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2001

Confidentiality

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

Name of the periodical

Inflammation Research

ISSN

1023-3830

e-ISSN

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Volume of the periodical

50

Issue of the periodical within the volume

2

Country of publishing house

CH - SWITZERLAND

Number of pages

2

Pages from-to

138-139

UT code for WoS article

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EID of the result in the Scopus database

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