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The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether Bonds
T. Nakai, H. Ito, K. Kobayashi, Y. Takahashi, H. Hori, M. Tsubaki, K. Tanizawa, T. Okajima,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2008 do Před 1 rokem
Freely Accessible Science Journals
od 1905 do Před 1 rokem
PubMed Central
od 2005
Europe PubMed Central
od 2005 do Před 1 rokem
Open Access Digital Library
od 1905-10-01
Open Access Digital Library
od 1905-10-01
ROAD: Directory of Open Access Scholarly Resources
od 1905
PubMed
25778402
DOI
10.1074/jbc.m115.638320
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny chemie genetika metabolismus MeSH
- elektronová paramagnetická rezonance MeSH
- oxidoreduktasy chemie genetika metabolismus MeSH
- Paracoccus denitrificans enzymologie genetika MeSH
- proteiny obsahující železo a síru chemie genetika metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The bacterial enzyme designated QhpD belongs to the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes and participates in the post-translational processing of quinohemoprotein amine dehydrogenase. QhpD is essential for the formation of intra-protein thioether bonds within the small subunit (maturated QhpC) of quinohemoprotein amine dehydrogenase. 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 formation in QhpC bound to QhpD, producing a multiknotted structure of the polypeptide chain. Homology modeling and mutagenic analysis revealed several conserved residues indispensable for both in vivo and in vitro activities of QhpD. Our findings uncover another challenging reaction catalyzed by a radical SAM enzyme acting on a ribosomally translated protein substrate.
the Department of Chemistry Graduate School of Science Kobe University Kobe Hyogo 657 8501 Japan and
Citace poskytuje Crossref.org
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- $a Nakai, Tadashi $u From the Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan.
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- $a The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether Bonds / $c T. Nakai, H. Ito, K. Kobayashi, Y. Takahashi, H. Hori, M. Tsubaki, K. Tanizawa, T. Okajima,
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- $a The bacterial enzyme designated QhpD belongs to the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes and participates in the post-translational processing of quinohemoprotein amine dehydrogenase. QhpD is essential for the formation of intra-protein thioether bonds within the small subunit (maturated QhpC) of quinohemoprotein amine dehydrogenase. 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 formation in QhpC bound to QhpD, producing a multiknotted structure of the polypeptide chain. Homology modeling and mutagenic analysis revealed several conserved residues indispensable for both in vivo and in vitro activities of QhpD. Our findings uncover another challenging reaction catalyzed by a radical SAM enzyme acting on a ribosomally translated protein substrate.
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- $a Okajima, Toshihide $u From the Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan, tokajima@sanken.osaka-u.ac.jp.
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