Gs. Prasad et al., CRYSTAL-STRUCTURE OF APLYSIA ADP RIBOSYL CYCLASE, A HOMOLOG OF THE BIFUNCTIONAL ECTOZYME CD38, Nature structural biology, 3(11), 1996, pp. 957-964
ADP ribosyl cyclase synthesizes the novel secondary messenger cyclic A
DP ribose (cADPR) utilizing NAD as a substrate. The enzyme shares exte
nsive sequence similarity with two lymphocyte antigens, CD38 and BST-l
,which hydrolyse as well as synthesize cADPR. The crystal structure pr
ovides a model for these cell surface enzymes. Cyclase contains two sp
atially separated pockets composed of sequence conserved residues, sug
gesting that the cyclization reaction may entail use of distinct sites
. The enzyme dimer encloses a cavity which may entrap the intermediate
, ADP ribose.