Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F10%3A10212789" target="_blank" >RIV/61989592:15310/10:10212789 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15110/10:10212789

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines

Popis výsledku v původním jazyce

Ornithine-delta-aminotransferase (OAT, EC 2.6.1.13) catalyzes the transamination of L-ornithine to L-glutamate-gamma-semialdehyde. We investigated the enzyme from pea (PsOAT). First, a cDNA coding for PsOAT was cloned and expressed in Escherichia coli. Recombinant PsOAT was purified under native conditions and its molecular and kinetic properties were characterized. The purified PsOAT existed asa monomer of 50 kDa and showed typical spectral properties of enzymes containing pyridoxal-5?-phosphate as a prosthetic group. L-Ornithine was the best substrate but PsOAT also slowly converted N(alpha)-acetyl-L-ornithine. In these reactions, 2-oxoglutarate was the exclusive amino group acceptor. The enzyme had a basic optimal pH of 8.8 anddisplayed relatively high temperature optimum. Diamines and polyamines were not accepted assubstrates. On the other hand, putrescine, spermidine and others represented weak non-competitive inhibitors.

Název v anglickém jazyce

Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines

Popis výsledku anglicky

Ornithine-delta-aminotransferase (OAT, EC 2.6.1.13) catalyzes the transamination of L-ornithine to L-glutamate-gamma-semialdehyde. We investigated the enzyme from pea (PsOAT). First, a cDNA coding for PsOAT was cloned and expressed in Escherichia coli. Recombinant PsOAT was purified under native conditions and its molecular and kinetic properties were characterized. The purified PsOAT existed asa monomer of 50 kDa and showed typical spectral properties of enzymes containing pyridoxal-5?-phosphate as a prosthetic group. L-Ornithine was the best substrate but PsOAT also slowly converted N(alpha)-acetyl-L-ornithine. In these reactions, 2-oxoglutarate was the exclusive amino group acceptor. The enzyme had a basic optimal pH of 8.8 anddisplayed relatively high temperature optimum. Diamines and polyamines were not accepted assubstrates. On the other hand, putrescine, spermidine and others represented weak non-competitive inhibitors.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Biochimie

ISSN

0300-9084

e-ISSN

—

Svazek periodika

92

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

9

Strana od-do

—

Kód UT WoS článku

000280570800004

EID výsledku v databázi Scopus

—