Copper/topa quinone-containing amine oxidases - recent research developments

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001660" target="_blank" >RIV/61989592:15310/02:00001660 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/02:00007750

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Copper/topa quinone-containing amine oxidases - recent research developments

Popis výsledku v původním jazyce

Amine oxidases (EC 1.4.3.6) that contain copper/topa quinone cofactor belong to a new protein group of quinoproteins emerging in recentyears. This review brings together information on the general properties of the enzymes and their physiological functions. In plants, these enzymes are involved in processes of development and senescence, they reduce the concentration of toxic amines produced during exposure to stress conditions, provide hydrogen peroxide for wall stiffening and lignification and precursor compounds for biosynthesis of some alkaloids. Major attention is currently being paid to the structure of the active site of the enzymes that contains copper ions and a posttranslationally modified tyrosyl residue, topa quinone. Three-dimensional structures recently obtained for several amine oxidases by X-ray diffraction analysis of the respective crystals provide important structural information about the unique protein folding of the native enzyme and molecular arrangement of the a

Název v anglickém jazyce

Copper/topa quinone-containing amine oxidases - recent research developments

Popis výsledku anglicky

Amine oxidases (EC 1.4.3.6) that contain copper/topa quinone cofactor belong to a new protein group of quinoproteins emerging in recentyears. This review brings together information on the general properties of the enzymes and their physiological functions. In plants, these enzymes are involved in processes of development and senescence, they reduce the concentration of toxic amines produced during exposure to stress conditions, provide hydrogen peroxide for wall stiffening and lignification and precursor compounds for biosynthesis of some alkaloids. Major attention is currently being paid to the structure of the active site of the enzymes that contains copper ions and a posttranslationally modified tyrosyl residue, topa quinone. Three-dimensional structures recently obtained for several amine oxidases by X-ray diffraction analysis of the respective crystals provide important structural information about the unique protein folding of the native enzyme and molecular arrangement of the a

Druh

C - Kapitola v odborné knize

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/ME%20153" target="_blank" >ME 153: Vlastnosti a využití enzymů oxidujících různé aminy s různými prostetickými skupinami z rostlin a mikroorganismů.</a><br>

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 knihy nebo sborníku

Studies in Natural Products Chemistry, Vol. 26

ISBN

0-444-51004-4

Počet stran výsledku

1347

Strana od-do

1259-1299

Počet stran knihy

—

Název nakladatele

Elsevier

Místo vydání

Amsterdam

Kód UT WoS kapitoly

—