Abstract
CD38 is a novel multifunctional protein that serves not only as an antigen but also as an enzyme. It catalyzes the metabolism of cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate, two structurally and functionally distinct Ca2+ messengers targeting, respectively, the endoplasmic reticulum and lysosomal Ca2+ stores. The protein has recently been crystallized and its three-dimensional structure solved to a resolution of 1.9 Å. The crystal structure of a binary complex reveals critical interactions between residues at the active site and a bound substrate, providing mechanistic insights to its novel multi-functional catalysis. This article reviews the current advances in the understanding of the structural determinants that control the multiple enzymatic reactions catalyzed by CD38.
Highlights
CD38 is a membrane-bound protein first identified by monoclonal antibody typing of lymphocytes and thought of as a lymphocyte-specific antigen [1]
It has been established that CD38 is a multi-functional enzyme catalyzing the metabolism of two distinct Ca2+ messengers, cyclic ADPribose [13,14] and nicotinic acid adenine dinucleotide phosphate (NAADP) [15]
Despite differences in some enzyme characteristics, one consistent feature that is common for all the members of the cyclase family is that they all efficiently catalyze the cyclization of NGD, an analog of NAD, to cyclic GDP-ribose, a fluorescent analog of cyclic ADPribose (cADPR) that is much more stable to hydrolysis [50]
Summary
CD38 is a membrane-bound protein first identified by monoclonal antibody typing of lymphocytes and thought of as a lymphocyte-specific antigen [1]. The Aplysia cyclase is the first enzyme that was found to cyclize NAD, a linear molecule, to cADPR, a cyclic product [20].
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