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Porcine CD38 exhibits prominent secondary NAD(+) cyclase activity.
- Source :
-
Protein science : a publication of the Protein Society [Protein Sci] 2016 Mar; Vol. 25 (3), pp. 650-61. Date of Electronic Publication: 2016 Jan 12. - Publication Year :
- 2016
-
Abstract
- Cyclic ADP-ribose (cADPR) mobilizes intracellular Ca(2+) stores and activates Ca(2+) influx to regulate a wide range of physiological processes. It is one of the products produced from the catalysis of NAD(+) by the multifunctional CD38/ADP-ribosyl cyclase superfamily. After elimination of the nicotinamide ring by the enzyme, the reaction intermediate of NAD(+) can either be hydrolyzed to form linear ADPR or cyclized to form cADPR. We have previously shown that human CD38 exhibits a higher preference towards the hydrolysis of NAD(+) to form linear ADPR while Aplysia ADP-ribosyl cyclase prefers cyclizing NAD(+) to form cADPR. In this study, we characterized the enzymatic properties of porcine CD38 and revealed that it has a prominent secondary NAD(+) cyclase activity producing cADPR. We also determined the X-ray crystallographic structures of porcine CD38 and were able to observe conformational flexibility at the base of the active site of the enzyme which allow the NAD(+) reaction intermediate to adopt conformations resulting in both hydrolysis and cyclization forming linear ADPR and cADPR respectively.<br /> (© 2016 The Protein Society.)
Details
- Language :
- English
- ISSN :
- 1469-896X
- Volume :
- 25
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Protein science : a publication of the Protein Society
- Publication Type :
- Academic Journal
- Accession number :
- 26660500
- Full Text :
- https://doi.org/10.1002/pro.2859