IMR Press / FBL / Volume 19 / Issue 6 / DOI: 10.2741/4262

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Review

The ADP-ribosyl cyclases - the current evolutionary state of the ARCs

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1 Immunogenetics Lab, Department of Medical Sciences,University of Torino, Via Santena 19, 10126 Torino, Italy
Academic Editor:Maria Rosaria Faraone-Mennella
Front. Biosci. (Landmark Ed) 2014, 19(6), 986–1002; https://doi.org/10.2741/4262
Published: 1 June 2014
(This article belongs to the Special Issue The ADP-ribosyl cyclases - the current evolutionary state of the ARCs)
Abstract

The major ADP-ribosylating enzyme families are the focus of this special issue of Frontiers in Bioscience. However, there is room for another family of enzymes with the capacity to utilize nicotinamide adenine dinucleotide (NAD): the ADP-ribosyl cyclases (ARCs). These unique enzymes catalyse the cyclization of NAD to cyclic ADP ribose (cADPR), a widely distributed second messenger. However, the ARCs are versatile enzymes that can manipulate NAD, NAD phosphate (NADP) and other substrates to generate various bioactive molecules including nicotinic acid adenine dinucleotide diphosphate (NAADP) and ADP ribose (ADPR). This review will focus on the group of well-characterized invertebrate and vertebrate ARCs whose common gene structure allows us to trace their origin to the ancestor of bilaterian animals. Behind a façade of gene and protein homology lies a family with a disparate functional repertoire dictated by the animal model and the physical trait under investigation. Here we present a phylogenetic view of the ARCs to better understand the evolution of function in this family.

Keywords
Protein family
evolution
NAD-consuming enzymes
ADP-ribosyl cyclases
cADPR and NAADP
Review
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