CD38 in bovine lung: A multicatalytic NADase.
The Journal of membrane biology
confidence
Key findings
CD38 purified from bovine lung is a multicatalytic NADase with NADase, cyclase, hydrolase, and pyridine base exchange activities; no clinical/biological endpoints.
View source on PubMed (PMID 19169615) ↗
- Sample size
- Not reported
- Population
- Bovine lung (in vitro enzyme study)
- Dosing
- Not reported
- Duration
- Not reported
- Route
- Not reported
- Blinding
- not_reported
- Controls
- none
- Drug class
- coenzyme
Full abstract
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 3.2.2.6). 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.