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Structural and functional characterization of a plant S-nitrosoglutathione reductase from Solanum lycopersicum

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33147734" target="_blank" >RIV/61989592:15310/13:33147734 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.sciencedirect.com/science/article/pii/S0300908412004877" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0300908412004877</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.biochi.2012.12.009" target="_blank" >10.1016/j.biochi.2012.12.009</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural and functional characterization of a plant S-nitrosoglutathione reductase from Solanum lycopersicum

  • Original language description

    S-nitrosoglutathione reductase (GSNOR), also known as S-(hydroxymethyl)glutathione (HMGSH) dehydrogenase, belongs to the alcohol dehydrogenase superfamily, namely to the class III ADHs. GSNOR catalyses the oxidation of HMGSH to S-formylglutathione usinga catalytic zinc and NAD(+) as a coenzyme. The enzyme also catalyses the NADH-dependent reduction of S-nitrosoglutathione (GSNO). In plants, GSNO has been suggested to serve as a nitric oxide (NO) reservoir locally or possibly as NO donor in distant cells and tissues. NO and NO-related molecules such as S-nitrosothiols (S-NOs) play a central role in the regulation of normal plant physiological processes and host defence. The enzyme thus participates in the cellular homeostasis of S-NOs and in the metabolism of reactive nitrogen species. Although GSNOR has recently been characterized from several organisms, this study represents the first detailed biochemical and structural characterization of a plant GSNOR, that from tomato (Solanum lyc

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

    2013

  • 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

  • Volume of the periodical

    95

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    FR - FRANCE

  • Number of pages

    14

  • Pages from-to

    889-902

  • UT code for WoS article

    000316513100030

  • EID of the result in the Scopus database