CD38 in Bovine Lung: A Multicatalytic NADase |
| |
Authors: | Valeria Polzonetti Stefania Pucciarelli Alberto Vita Silvia Vincenzetti Paolo Natalini |
| |
Institution: | (1) Dipartimento di Scienze Morfologiche e Biochimiche Comparate, Università di Camerino, Via Gentile III da Varano, Camerino (MC), 62032, Italy |
| |
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. |
| |
Keywords: | CD38 NAD+-glycohydrolase Multicatalytic enzyme cADPR NAD homeostasis |
本文献已被 SpringerLink 等数据库收录! |
|