Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines
The result's identifiers
Result code in 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>
Alternative codes found
RIV/61989592:15110/10:10212789
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines
Original language 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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochimie
ISSN
0300-9084
e-ISSN
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Volume of the periodical
92
Issue of the periodical within the volume
8
Country of publishing house
FR - FRANCE
Number of pages
9
Pages from-to
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UT code for WoS article
000280570800004
EID of the result in the Scopus database
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