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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Библиографические подробности
Главные авторы: Egea, Pascal F., Muller-Steffner, Hélène, Kuhn, Isabelle, Cakir-Kiefer, Céline, Oppenheimer, Norman J., Stroud, Robert M., Kellenberger, Esther, Schuber, Francis
Формат: Artigo
Язык:Inglês
Опубликовано: Public Library of Science 2012
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Research Article
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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