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Science 3 September 1993:
Vol. 261. no. 5126, pp. 1330 - 1333
DOI: 10.1126/science.8395705
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Articles

Science, Vol 261, Issue 5126, 1330-1333
Copyright © 1993 by American Association for the Advancement of Science

articles

Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases

H Kim, EL Jacobson, and MK Jacobson

Department of Biochemistry and Molecular Biology, University of North Texas Health Science Center at Fort Worth 76107.

Cyclic adenosine diphosphoribose (cADPR), a recently discovered metabolite of nicotinamide adenine dinucleotide (NAD), is a potent calcium-releasing agent postulated to be a new second messenger. An enzyme that catalyzes the synthesis of cADPR from NAD and the hydrolysis of cADPR to ADP-ribose (ADPR) was purified to homogeneity from canine spleen microsomes. The net conversion of NAD to ADPR categorizes this enzyme as an NAD glycohydrolase. NAD glycohydrolases are ubiquitous membrane-bound enzymes that have been known for many years but whose function has not been identified. The results presented here suggest that these enzymes may function in the regulation of calcium homeostasis by the ability to synthesize and degrade cADPR.


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