CD38 in bovine lung: A multicatalytic NADase.

J Membr Biol

Dipartimento di Scienze Morfologiche e Biochimiche Comparate, Università di Camerino, Italy.

Published: February 2009

AI Article Synopsis

  • CD38 is identified as a new type of NAD(+)-glycohydrolase enzyme, indicating its role in multiple biochemical reactions involving NAD(+)
  • It can break down NAD(+) into nicotinamide and either adenosine diphosphoribose (ADPR) or cyclic ADPR (cADPR), showcasing its diverse functionality
  • The enzyme is significant for regulating NAD(+) levels and calcium signaling in cells, impacting energy and communication processes within the cell.

Article 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.

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http://dx.doi.org/10.1007/s00232-008-9149-xDOI Listing

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