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The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether Bonds

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F15%3A33153648" target="_blank" >RIV/61989592:15310/15:33153648 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.jbc.org/content/early/2015/03/16/jbc.M115.638320.full.pdf+html" target="_blank" >http://www.jbc.org/content/early/2015/03/16/jbc.M115.638320.full.pdf+html</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M115.638320" target="_blank" >10.1074/jbc.M115.638320</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether Bonds

  • Original language description

    The bacterial enzyme designated QhpD belongs to the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes and participates in the posttranslational processing of quinohemoprotein amine dehydrogenase (QHNDH). QhpD is essential for the formation ofintra-protein thioether bonds within the small subunit (maturated QhpC) of QHNDH. We overproduced QhpD from Paracoccus denitrificans as a stable complex with its substrate QhpC, carrying the 28-residue leader peptide that is essential for the complex formation. Absorption and electron paramagnetic resonance spectra together with the analyses of iron and sulfur contents suggested the presence of multiple (likely three) [4Fe-4S] clusters in the purified and reconstituted QhpD. In the presence of a reducing agent (sodium dithionite), QhpD catalyzed the multiple-turnover reaction of reductive cleavage of SAM into methionine and 5'-deoxyadenosine and also the single-turnover reaction of intra-protein sulfur-to-methylene carbon thioether bond

  • 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

    <a href="/en/project/EE2.3.20.0165" target="_blank" >EE2.3.20.0165: Integration of Research Team of the Centre of the Region Haná into International Collaboration</a><br>

  • Continuities

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

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    290

  • Issue of the periodical within the volume

    17

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    23

  • Pages from-to

    11144-11166

  • UT code for WoS article

    000353404500048

  • EID of the result in the Scopus database