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1,N6-etheno NAD+ + H2O
epsilon-ADP-ribose + nicotinamide + H+
-
-
-
-
?
2-fluoro-NAD+ + H2O
2-fluoro-ADP-ribose + nicotinamide
-
in presence of methanol, formation of methanolysis product beta-1''-O-methyl 2-fluoro-ADP-ribose, with a preference for methanolysis over hydrolysis of 100:1
-
-
?
3-acetylpyridine + H2O
?
-
-
-
-
?
3-acetylpyridine adenine dinucleotide + H2O
?
3-acetylpyridine hypoxanthine dinucleotide + H2O
?
3-aminopyridine + H2O
?
-
-
-
-
?
3-carboxyhydrazide adenine dinucleotide + H2O
?
-
-
-
-
?
3-formylpyridine adenine dinucleotide + H2O
?
-
-
-
-
?
3-methylpyridine + H2O
?
-
-
-
-
?
3-pyridylacetonitrile + H2O
?
-
-
-
-
?
3-pyridylcarbinol + H2O
?
-
-
-
-
?
alpha-NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
beta-NAD+ + H2O
ADP-ribose + nicotinamide
beta-NAD+ + H2O
ADP-ribose + nicotinamide + H+
-
-
-
-
?
beta-nicotine guanine dinucleotide + H2O
?
-
-
-
-
?
epsilon-NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
-
?
methylnicotinate adenine dinucleotide + H2O
?
-
-
-
-
?
NAD+ + H2O
adenosine + nicotinamide + ?
-
solubilized enzyme form sNADase, unusual cleavage reaction, no hydrolysis of the labile quarternary nicotinamide-ribose pyridinium linkage
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
NAD+ + H2O
ADP-ribose + nicotinamide
NAD+ + H2O
ADP-ribose + nicotinamide + H+
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
NAD+ + H2O
cADPribose + nicotinamide
NADP+ + H2O
phospho-ADP-ribose + nicotinamide
NADP+ + H2O
phospho-ADPribose + nicotinamide
nicotinamide ethenoadenine dinucleotide + H2O
?
-
-
-
-
?
nicotinamide guanine dinucleotide + H2O
3',5'-cyclic GDP-ribose + GDP-ribose
-
-
-
-
?
nicotinamide guanine dinucleotide + H2O
?
-
-
-
-
?
nicotinamide hypoxanthine dinucleotide + H2O
?
nicotinic acid adenine dinucleotide + H2O
?
-
-
-
-
?
NMN + H2O
phosphoribose + nicotinamide
pyridine + H2O
?
-
-
-
-
?
pyridine-3-aldehyde adenine dinucleotide + H2O
?
-
-
-
-
?
pyridine-3-aldehyde hypoxanthine dinucleotide + H2O
?
-
-
-
-
?
thioNADP+ + H2O
?
-
-
-
-
?
additional information
?
-
1,N6-etheno-NAD+ + H2O

?
-
-
-
?
1,N6-etheno-NAD+ + H2O
?
-
-
-
-
?
3-acetylpyridine adenine dinucleotide + H2O

?
-
-
-
-
?
3-acetylpyridine adenine dinucleotide + H2O
?
-
-
-
-
?
3-acetylpyridine adenine dinucleotide + H2O
?
-
-
-
-
?
3-acetylpyridine hypoxanthine dinucleotide + H2O

?
-
-
-
-
?
3-acetylpyridine hypoxanthine dinucleotide + H2O
?
-
-
-
-
?
3-acetylpyridine hypoxanthine dinucleotide + H2O
?
-
-
-
-
?
beta-NAD+ + H2O

ADP-ribose + nicotinamide
-
-
-
-
?
beta-NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O

ADP-D-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
-
-
-
?
NAD+ + H2O

ADP-ribose + nicotinamide
-
ADP-ribose reacts further with polyarginine, polyhistidine, or polylysine
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
ADP-ribose reacts spontaneously with polyarginine, polyhistidine, or polylysine
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
CD38 is a multifunctional enzyme involved in the degradation of beta-nicotinamide adenine dinucleotide. the beta-nicotinamide adenine dinucleotide/CD38 system may provide new mechanisms in autonomic neurovascular control
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
purified bifunctional enzyme has a ADP-ribosyl cyclase/NAD glycohydrolase ratio of 1/120. In situ cyclase/NAD glycohydrolase ratio measured in seminal plasma is 1/1. Physiological concentrations of zinc present in the seminal fluid, in the range of 0.6 to 4 mM, are responsible for the modulation of the cyclase/NAD glycohydrolase ratio
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
substrate binding structure, overview. Catalytically important CD38 residue Thr221 disfavors the cyclizing folding of the substrate, resulting in NADase being the dominant activity
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
low activity in CD38-deficient cell membranes at all developmental stages
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
enzyme contributes to the pathogenicity of group A streptococci, after it is transported into the cytoplasm and membranes of host endothelial cells, by modulation of host cell signalling pathways to inhibit group A streptococci internalization, leading to apoptosis of keratinocytes
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
enzyme contributes to the pathogenicity of group A streptococci, after it is transported into the cytoplasm and membranes of host endothelial cells, by modulation of host cell signalling pathways to inhibit group A streptococci internalization, leading to apoptosis of keratinocytes
-
-
?
NAD+ + H2O

ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O
ADPribose + nicotinamide
-
-
137055, 137060, 137063, 137065, 137067, 137068, 137070, 137076, 137077, 137079, 137088, 137089, 137091, 137093, 137095, 137096 -
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
ADPribose + nicotinamide
-
-
-
-
ir
NAD+ + H2O

cADPribose + nicotinamide
-
-
-
-
?
NAD+ + H2O
cADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O

phospho-ADP-ribose + nicotinamide
-
-
-
?
NADP+ + H2O
phospho-ADP-ribose + nicotinamide
-
-
-
?
NADP+ + H2O
phospho-ADP-ribose + nicotinamide
-
-
-
?
NADP+ + H2O
phospho-ADP-ribose + nicotinamide
-
-
-
?
NADP+ + H2O

phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
ir
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
phospho-ADPribose + nicotinamide
-
-
-
-
?
nicotinamide hypoxanthine dinucleotide + H2O

?
-
-
-
-
?
nicotinamide hypoxanthine dinucleotide + H2O
?
-
-
-
-
?
NMN + H2O

phosphoribose + nicotinamide
-
-
-
-
?
NMN + H2O
phosphoribose + nicotinamide
-
-
-
-
?
thioNAD+ + H2O

?
-
-
-
-
?
thioNAD+ + H2O
?
-
-
-
-
?
thioNAD+ + H2O
?
-
-
-
-
?
additional information

?
-
-
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
-
-
?
additional information
?
-
-
substrate binding structure of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
NADP is not cleaved by chromatin NADase
-
-
?
additional information
?
-
-
alcoholysis of NAD to form O-alkyl-ADP-ribosides, ADP-ribosylation of imidazole derivates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
ATP and ADP are also hydrolyzed by AA-NADase to form ADP and AMP, respectively, theAA-NADase-catalyzed cleavage reaction of NAD is markedly inhibited in the presence of ATP and ADP, overview
-
-
?
additional information
?
-
-
the multifunctional AA-NADase also shows ADPase activity
-
-
?
additional information
?
-
-
the multifunctional AA-NADase also shows ADPase activity
-
-
?
additional information
?
-
-
bifunctional enzyme ADP-ribose cyclase/NAD glycohydrolase, enzyme activities are regulated by zinc, enzyme is capable of both synthesis and hydrolysis of cADP-ribose
-
-
?
additional information
?
-
-
bifunctional enzyme ADP-ribose cyclase/NAD glycohydrolase, enzyme is capable of both synthesis and hydrolysis of cADP-ribose
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the ADP-ribosyl cyclase activity shows identical properties and is inseparable, thus the enzyme is bifunctional one
-
-
?
additional information
?
-
-
CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme-mediated inhibition of osteoclastogenesis is related to its NADase activity, not its ADPribosyl cyclase activity
-
-
?
additional information
?
-
-
no substrate: cyclic ADP-ribose
-
-
?
additional information
?
-
nicotinamide and ADP-ribose are the only detectable products, no cyclization is found, i.e. no reaction of EC 3.2.2.6
-
-
?
additional information
?
-
nicotinamide and ADP-ribose are the only detectable products, no cyclization is found, i.e. no reaction of EC 3.2.2.6
-
-
?
additional information
?
-
-
enzyme is involved in regulation of mitogen-stimulated T-cell proliferation by inhibition via NAD+ and ADP-ribose, not nicotinamide
-
-
?
additional information
?
-
-
NADP is not cleaved by chromatin NADase
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
SPN is specific for beta-NAD+ glycohydrolase activity, and does not show ADP-ribosyl cyclase and ADP-ribosyltransferase activities, overview. SPN is unable to catalyze cyclic ADPR hydrolysis, and cannot catalyze methanolysis or transglycosidation
-
-
?
additional information
?
-
lack of ADP-ribosyltransferase activity of the enzyme
-
-
?
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