CD38 in Bovine Lung: A Multicatalytic NADase

CD38 in Bovine Lung: A Multicatalytic NADase We report the kinetics and molecular properties of CD38 purified from bovine lung microsomal membranes after its solubilization with Triton X-100. The enzyme was found to be a novel member of a multicatalytic NAD+-glycohydrolase (NADase, EC It was able to utilize NAD + in different ways, producing nicotinamide (Nam) and either adenosine diphosphoribose (ADPR, NADase activity) or cyclic ADPR (cADPR, cyclase activity); it also catalyzed the hydrolysis of cADPR to ADPR (cADPR, hydrolase activity). In addition, the enzyme catalyzed the pyridine base exchange reaction with conversion of NAD + into NAD analogues. These data are evidence that CD38 is involved in the regulation of both NAD+ and calcium-mobilizing agents, the concentration resulting in an essential enzyme that plays a key role in cellular energy and signal-transduction systems. The Journal of Membrane Biology Springer Journals

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Copyright © 2009 by Springer Science+Business Media, LLC
Life Sciences; Human Physiology ; Biochemistry, general
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