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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/EE2.3.20.0165" target="_blank" >EE2.3.20.0165: Podpora zapojení výzkumného týmu Centra regionu Haná do mezinárodní spolupráce</a><br>

Návaznosti

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

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

290

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

23

Strana od-do

11144-11166

Kód UT WoS článku

000353404500048

EID výsledku v databázi Scopus

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