Attributes | Values |
---|
rdf:type
| |
Description
| - 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.
- 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. (en)
|
Title
| - Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines
- Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines (en)
|
skos:prefLabel
| - Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines
- Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines (en)
|
skos:notation
| - RIV/61989592:15110/10:10212789!RIV11-GA0-15110___
|
http://linked.open...avai/riv/aktivita
| |
http://linked.open...avai/riv/aktivity
| - P(GA522/08/0555), P(GD522/08/H003)
|
http://linked.open...iv/cisloPeriodika
| |
http://linked.open...vai/riv/dodaniDat
| |
http://linked.open...aciTvurceVysledku
| |
http://linked.open.../riv/druhVysledku
| |
http://linked.open...iv/duvernostUdaju
| |
http://linked.open...titaPredkladatele
| |
http://linked.open...dnocenehoVysledku
| |
http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15110/10:10212789
|
http://linked.open...riv/jazykVysledku
| |
http://linked.open.../riv/klicovaSlova
| - pyridoxal-5'-phosphate; proline; polyamine; ornithine-delta-aminotransferase; ornithine (en)
|
http://linked.open.../riv/klicoveSlovo
| |
http://linked.open...odStatuVydavatele
| - FR - Francouzská republika
|
http://linked.open...ontrolniKodProRIV
| |
http://linked.open...i/riv/nazevZdroje
| |
http://linked.open...in/vavai/riv/obor
| |
http://linked.open...ichTvurcuVysledku
| |
http://linked.open...cetTvurcuVysledku
| |
http://linked.open...vavai/riv/projekt
| |
http://linked.open...UplatneniVysledku
| |
http://linked.open...v/svazekPeriodika
| |
http://linked.open...iv/tvurceVysledku
| - STRÁNSKÁ, Jana
- KOPEČNÝ, David
- TYLICHOVÁ, Martina
- ŠEBELA, Marek
- SNÉGAROFF, Jacques
|
http://linked.open...ain/vavai/riv/wos
| |
issn
| |
number of pages
| |
http://localhost/t...ganizacniJednotka
| |
is http://linked.open...avai/riv/vysledek
of | |