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Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus

Succinyl-CoA synthetase (SCS) from Thermus aquaticus was characterized biochemically via measurements of the activity of the enzyme and determination of its quaternary structure as well as its stability and refolding properties. The enzyme is most active between pH 8.0 and 8.4 and its activity incre...

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Detaylı Bibliyografya
Asıl Yazarlar: Joyce, Michael A., Hayakawa, Koto, Wolodko, William T., Fraser, Marie E.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: International Union of Crystallography 2012
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC3388811/
https://ncbi.nlm.nih.gov/pubmed/22751660
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0907444912010852
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