Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F08%3A00005308" target="_blank" >RIV/61989592:15310/08:00005308 - isvavai.cz</a>

Result on the web

—

DOI - Digital Object Identifier

—

Result language

angličtina

Original language name

Ornithine delta-aminotransferase: an enzyme implicated in salt tolerance in higher plants

Original language description

This review deals with biochemical and physiological aspects of plant ornithine delta-aminotransferase (OAT, EC 2.6.1.13). OAT is a mitochondrial enzyme containing pyridoxal-5'-phosphate as a cofactor, which catalyzes the conversion of L-ornithine to L-glutamate ?-semialdehyde using 2-oxoglutarate as a terminal amino group acceptor. It has been described in humans, animals, insects, plants and microorganisms. Based on the crystal structure of human OAT, both substrate binding and reaction mechanism of the enzyme are well understood. OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases, which transfer an amino group from a carbon atom that does not carry a carboxyl function. In plants, the enzyme has been implicated in proline biosynthesis and accumulation (via pyrroline-5-carboxylate), which represents a way to regulate cellular osmolarity in response to osmotic stress. However, the exact metabolic pathway involving OAT rem

Czech name

Ornithin-delta-aminotransferasa: enzym zapojený do mechanismů salinitní tolerance u vyšších rostlin

Czech description

Ornithin-delta-aminotransferasa (OAT) je mitochondriální enzym obsahující pyridoxal-5´-fosfát, který katalyzuje přeměnu L-ornithinu na L-glutamát-?-semialdehyd s použitím 2-oxoglutarátu jako koncového akceptoru aminoskupiny. Byl popsán v řadě organismů.Na základě krystalové struktury lidské OAT je velmi dobře prouzkoumán princip vazby substrátu a reakční mechanismus enzymu. OAT má vlastnosti velmi podobné ostatním enzymům z podskupiny 3 aminotransferas. V rostlinách se enzym účastní biosyntézy a akumulace prolinu, což je jedna z cest regulace osmolarity v odpovědi na osmotický stres.

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2008

Confidentiality

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

Name of the periodical

Plant Signalling & Behavior

ISSN

1559-2316

e-ISSN

—

Volume of the periodical

3

Issue of the periodical within the volume

11

Country of publishing house

US - UNITED STATES

Number of pages

7

Pages from-to

—

UT code for WoS article

—

EID of the result in the Scopus database

—