Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | the enzyme has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity | Deinagkistrodon acutus | |
EDTA | irreversible inhibition | Deinagkistrodon acutus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics and thermodynamics in presence of different metal ions, overview | Deinagkistrodon acutus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | venom | Deinagkistrodon acutus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | AA-NADase has one strong and two weak Co2+ binding sites | Deinagkistrodon acutus | |
Co2+ | the enzyme has one strong and two weak Co2+ binding sites | Deinagkistrodon acutus | |
Cu2+ | although Cu2+ ions are important for catalyzing the hydrolysis of NAD, they are also able to inhibit its NADase activity in a concentration-dependent manner, Cu2+ ions in low-affinity binding sites inhibit its NADase activity. AA-NADase has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity. Cu2+ ions function as a switch for its NADase activity. | Deinagkistrodon acutus | |
Cu2+ | the enzyme contains Cu2+ ions that are essential for its multicatalytic activity. The enzyme has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity. Both NADase and ADPase activities of the enzyme do not have an absolute requirement for Cu2+ and may be replaced by Zn2+ > Mn2+ > Cu2+/Co2+ > Ni2+ | Deinagkistrodon acutus | |
Mn2+ | AA-NADase has one Mn2+ binding site | Deinagkistrodon acutus | |
Mn2+ | the enzyme has one Mn2+ binding site | Deinagkistrodon acutus | |
additional information | no absolute requirement for metal ions, metal ion binding affinities in descending order: Cu2+ , Ni2+, Mn2+, Co2+, and Zn2+. Enzyme-metal ion interaction analysis by equilibrium dialysis, isothermal titration calorimetry, fluorescence, circular dichroism, dynamic light scattering and HPLC, overview | Deinagkistrodon acutus | |
Ni2+ | AA-NADase has two strong and six weak Ni2+ binding sites | Deinagkistrodon acutus | |
Ni2+ | the enzyme has two strong and six weak Ni2+ binding sites | Deinagkistrodon acutus | |
Zn2+ | AA-NADase has one Zn2+ binding site | Deinagkistrodon acutus | |
Zn2+ | the enzyme has one Zn2+ binding site | 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 |
---|---|
- |
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 | - |
? | |
NAD+ + H2O | - |
Deinagkistrodon acutus | ADP-ribose + nicotinamide + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AA-NADase | - |
Deinagkistrodon acutus |
NAD-glycohydrolase | - |
Deinagkistrodon acutus |
NADase | multicatalytic enzyme with both NADase and AT(D)Pase activities | 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 |