FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F00%3A00001109" target="_blank" >RIV/61989592:15310/00:00001109 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/01:00001262

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants

Popis výsledku v původním jazyce

Recent investigations on plant polyamine oxidase (PAO) are reviewed. The enzyme belongs to a new class of flavoenzymes with similar structural features including, among others, monoamine oxidase. Plant PAOs catalyse the oxidation of the polyamine substrates spermidine and spermine. The reaction products are propane-1,3-diamine and 1-pyrroline or 1-(3-aminopropyl)pyrroline, respectively, along with hydrogen peroxide. Plant PAOs are predominantly localised in the cell wall. Purification procedures and molecular properties of several plant PAOs are compared. A special attention is being paid to the recently solved crystal structure of the maize enzyme and its implications for the substrate binding and catalytic mechanism. Substrate specificity and inhibitors of plant PAOs are also described. The potential roles for PAO-generated H2O2 in lignin biosynthesis and cell wall cross-linking reactions, which may regulate growth and contribute to cell defence, are discussed.

Název v anglickém jazyce

FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants

Popis výsledku anglicky

Recent investigations on plant polyamine oxidase (PAO) are reviewed. The enzyme belongs to a new class of flavoenzymes with similar structural features including, among others, monoamine oxidase. Plant PAOs catalyse the oxidation of the polyamine substrates spermidine and spermine. The reaction products are propane-1,3-diamine and 1-pyrroline or 1-(3-aminopropyl)pyrroline, respectively, along with hydrogen peroxide. Plant PAOs are predominantly localised in the cell wall. Purification procedures and molecular properties of several plant PAOs are compared. A special attention is being paid to the recently solved crystal structure of the maize enzyme and its implications for the substrate binding and catalytic mechanism. Substrate specificity and inhibitors of plant PAOs are also described. The potential roles for PAO-generated H2O2 in lignin biosynthesis and cell wall cross-linking reactions, which may regulate growth and contribute to cell defence, are discussed.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F97%2F0097" target="_blank" >GA203/97/0097: Molekulární, strukturní a fyziologické vlastnosti rostlinných aminoxidas a cytokininoxidas</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2001

Kód důvěrnosti údajů

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

Název periodika

Plant Science

ISSN

0168-9452

e-ISSN

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Svazek periodika

160

Číslo periodika v rámci svazku

NA

Stát vydavatele periodika

XX - osoby bez státní příslušnosti

Počet stran výsledku

1

Strana od-do

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Kód UT WoS článku

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EID výsledku v databázi Scopus

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