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ADP-Ribosyl Cyclases - A Family of cADPR and NAADP Metabolizing Enzymes

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Cyclic ADP-Ribose and NAADP

Abstract

ADP-ribosyl cyclase cyclizes NAD to produce cyclic ADP-ribose (cADPR) and releases nicotinamide in the process [1]. It is a ubiquitous enzyme widely present in animal cells [1, 2] and has even been identified in Euglena, a protozoan [4]. The first cyclase purified was from Aplysia ovotestis [1, 5]. It is a soluble protein of approximately 30 kDa. Sequence comparison reveals that CD38, a lymphocyte antigen, is a mammalian homolog [6]. CD38 is a transmembrane glycoprotein of approximately 45 kDa [7]. It catalyzes not only the synthesis of cADPR but also its hydrolysis to ADP-ribose [8, 11]. Additionally, both CD38 and the Aplysia cyclase use NADP as a substrate and catalyze the exchange of the nicotinamide group with nicotinic acid, producing nicotinic acid adenine dinucleotide phosphate (NAADP) [12]. The Aplysia cyclase has been crystallized and its structure solved [13, 14]. Current knowledge of the structures of these enzymes and the novel multiplicity of their catalytic activities are described in this chapter. Since both of their products are Ca2+ messengers, this class of enzymes is crucial in mediating Ca2+ signaling functions in cells. Some of their physiological functions have now been revealed by gene ablation and are summarised here.

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  1. Department of Pharmacology, University of Minnesota, Minneapolis, MN, 55455, USA

    Hon Cheung Lee, Cyrus B. Munshi & Richard Graeff

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    Hon Cheung Lee

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Lee, H.C., Munshi, C.B., Graeff, R. (2002). ADP-Ribosyl Cyclases - A Family of cADPR and NAADP Metabolizing Enzymes. In: Lee, H.C. (eds) Cyclic ADP-Ribose and NAADP. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0269-2_2

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