EC Number   |
Natural Substrates |
|---|
    3.2.2.5 | more |
bifunctional enzyme ADP-ribose cyclase/NAD glycohydrolase, enzyme activities are regulated by zinc, enzyme is capable of both synthesis and hydrolysis of cADP-ribose |
| 3.2.2.5 | more |
enzyme is involved in regulation of mitogen-stimulated T-cell proliferation by inhibition via NAD+ and ADP-ribose, not nicotinamide |
| 3.2.2.5 | more |
CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins |
| 3.2.2.5 | more |
streptolysin and NAD+ -glycohydrolase interact functionally as a compound signaling toxin. When Streptococcus pyogenes is bound to the surface of epithelial cells in vitro, streptolysin forms pores in the cell membrane and delivers NADase to the epithelial cell cytoplasm. In vitro, intoxication of keratinocytes with NADase is associated with cytotoxic effects and induction of apoptosis. NADase and streptolysin together enhance Streptococcus pyogenes virulence in vivo |
| 3.2.2.5 | more |
the capacity of NADase to enhance streptolysin O-mediated cytotoxicity is not due to a direct effect on pore formation but rather due to depletion of cellular NAD+ and ATP |
| 3.2.2.5 | more |
CD38 rather than poly-ADP-ribose polymerase PARP-1, is an important source of ADP-ribose in mouse neutrophils and dendritic cells that use ADP-ribose as a secong messenger. ADP-ribose controls calcium influx and chemotaxis when cells are activated through chemokine receptors that rely on CD38 and cyclic ADP-ribose for activity |
| 3.2.2.5 | more |
enzyme plays a crucial role in neutrophil diapedesis. Its ligation with specific monoclonal antibodies both on neutrophils or endothelial cells results in altered neutrophil movement on the apical surface of endothelium and, ultimately, in loss of diapedesis. Following CD157 ligation, neutrophils appear disoriented, meandering toward junctions where they eventually stop without transmigrating |
| 3.2.2.5 | more |
enzyme-mediated inhibition of osteoclastogenesis is related to its NADase activity, not its ADPribosyl cyclase activity |
| 3.2.2.5 | more |
multifunctional AA-NADase is not only able to cleave the CeN glycosyl bond of NAD to produce ADPR and nicotinamide, but also able to cleave the phosphoanhydride linkages of ATP, ADP and AMP-PNP to yield AMP, overview |
| 3.2.2.5 | more |
Phe174 in ADP-ribosyl cyclase, ADPRC, is a critical residue in directing the folding of the substrate during the cyclization reaction. Thus, a point mutation of Phe174 to glycine can turn ADPRC from a cyclase toward an NADase, overview |
