Yüklüyor......
The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes
Bifunctional FAD synthetases (FADSs) fold in two independent modules; The C-terminal riboflavin kinase (RFK) catalyzes the RFK activity, while the N-terminal FMN-adenylyltransferase (FMNAT) exhibits the FMNAT activity. The search for macromolecular interfaces in the Corynebacterium ammoniagenes FADS...
Kaydedildi:
| Yayımlandı: | Sci Rep |
|---|---|
| Asıl Yazarlar: | , , , , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
Nature Publishing Group UK
2017
|
| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5428420/ https://ncbi.nlm.nih.gov/pubmed/28341845 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-017-00402-6 |
| Etiketler: |
Etiketle
Etiket eklenmemiş, İlk siz ekleyin!
|