Inhibitors | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | inhibits both NADase and ADPase activities through the reduction of Cu(II) to Cu(I) and the cleavage of disulfide-bonds in AA-NADase | Deinagkistrodon acutus | |
DTT | - |
Deinagkistrodon acutus | |
glutathione | inhibits both NADase and ADPase activities through the reduction of Cu(II) to Cu(I) and the cleavage of disulfide-bonds in AA-NADase | Deinagkistrodon acutus | |
L-ascorbate | inhibits AA-NADase on both NADase and ADPase activities through the reduction of Cu(II) in AA-NADase to Cu(I) | Deinagkistrodon acutus | |
tris(2-carboxyethyl)phosphine | TCEP, inhibits both NADase and ADPase activities through the reduction of Cu(II) to Cu(I) and the cleavage of disulfide-bonds in AA-NADase | Deinagkistrodon acutus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | venom | Deinagkistrodon acutus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | among all identified NADases, only AA-NADase contains Cu2+ and has six disulfide-bond linkages between two peptide chains | Deinagkistrodon acutus | |
Zn2+ | apo-AA-NADase can recover its NADase and ADPase activities in the presence of 1 mM Zn2+, which is inhibited by tris(2-carboxyethyl)phosphine | Deinagkistrodon acutus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
NAD+ + H2O | Deinagkistrodon acutus | - |
ADP-ribose + nicotinamide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Deinagkistrodon acutus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme | Deinagkistrodon acutus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
venom | - |
Deinagkistrodon acutus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the multifunctional AA-NADase also shows ADPase activity | Deinagkistrodon acutus | ? | - |
? | |
NAD+ + H2O | - |
Deinagkistrodon acutus | ADP-ribose + nicotinamide | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | among all identified NADases, only AA-NADase contains Cu2+ and has six disulfide-bond linkages between two peptide chains, and it has 15 free cysteine residues | Deinagkistrodon acutus |
Synonyms | Comment | Organism |
---|---|---|
AA-NADase | - |
Deinagkistrodon acutus |
NAD-glycohydrolase | - |
Deinagkistrodon acutus |
NADase | - |
Deinagkistrodon acutus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Deinagkistrodon acutus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Deinagkistrodon acutus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics, overview | Deinagkistrodon acutus |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.42 | - |
pH 7.4, 37°C, inhibition of the NADase activity | Deinagkistrodon acutus | tris(2-carboxyethyl)phosphine | |
1.79 | - |
pH 7.4, 37°C, inhibition of the NADase activity | Deinagkistrodon acutus | L-ascorbate | |
2.48 | - |
pH 7.4, 37°C, inhibition of the NADase activity | Deinagkistrodon acutus | DTT | |
6.11 | - |
pH 7.4, 37°C, inhibition of the NADase activity | Deinagkistrodon acutus | glutathione |