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Insights into the Mechanism of Bovine CD38/NAD+Glycohydrolase from the X-Ray Structures of Its Michaelis Complex and Covalently-Trapped Intermediates
Bovine CD38/NAD(+)glycohydrolase (bCD38) catalyses the hydrolysis of NAD(+) into nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose (cADPR). We solved the crystal structures of the mono N-glycosylated forms of the ecto-domain of bCD38 or the catalytic residue mutant Glu218Gln in thei...
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| Главные авторы: | , , , , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Public Library of Science
2012
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3329556/ https://ncbi.nlm.nih.gov/pubmed/22529956 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0034918 |
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