Roles of Nicotinamide Adenine Dinucleotide (NAD + ) in Biological Systems

Palmiro Poltronieri and Nataša Čerekovic
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Palmiro Poltronieri: Institute of Sciences of Food Productions, CNR-ISPA, Ecotekne, via prov.le Lecce-Monteroni km 7, 73100 Lecce, Italy
Nataša Čerekovic: Institute of Sciences of Food Productions, CNR-ISPA, Ecotekne, via prov.le Lecce-Monteroni km 7, 73100 Lecce, Italy

Challenges, 2018, vol. 9, issue 1, 1-14

Abstract: NAD + has emerged as a crucial element in both bioenergetic and signaling pathways since it acts as a key regulator of cellular and organism homeostasis. NAD + is a coenzyme in redox reactions, a donor of adenosine diphosphate-ribose (ADPr) moieties in ADP-ribosylation reactions, a substrate for sirtuins, a group of histone deacetylase enzymes that use NAD + to remove acetyl groups from proteins; NAD + is also a precursor of cyclic ADP-ribose, a second messenger in Ca ++ release and signaling, and of diadenosine tetraphosphate (Ap4A) and oligoadenylates (oligo2?-5?A), two immune response activating compounds. In the biological systems considered in this review, NAD + is mostly consumed in ADP-ribose (ADPr) transfer reactions. In this review the roles of these chemical products are discussed in biological systems, such as in animals, plants, fungi and bacteria. In the review, two types of ADP-ribosylating enzymes are introduced as well as the pathways to restore the NAD + pools in these systems.

Keywords: Nicotinamide adenine dinucleotide (NAD + ); ADP ribose (ADPr); ADP Ribosyl Transferase (ADPRT); nicotinamide (Nam); nicotinamide mononucleotide (NMN); nicotinamide riboside (NR); nicotinic acid (NA); nicotinic acid adenine dinucleotide phosphate (NAADP); cyclic ADP ribose (cADPr); post-translational modification (PTM); deacetylation; poly ADP ribose glycohydrolase (PARG); Nicotinamide mononucleotide adenylyl transferease (NMNAT-1); nicotinamide phosphoribosyl transferase (NAMPT) (search for similar items in EconPapers)
JEL-codes: A00 C00 Z00 (search for similar items in EconPapers)
Date: 2018
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (3)

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