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
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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
<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
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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
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