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Literature summary for 3.2.2.5 extracted from
- Identification of an unusual AT(D)Pase-like activity in multifunctional NAD glycohydrolase from the venom of Agkistrodon acutus (2009), Biochimie, 91, 240-251.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP | competitive | Deinagkistrodon acutus |  |
| ATP | competitive | Deinagkistrodon acutus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, overview | Deinagkistrodon acutus | |
| 0.26 | - |
NAD+ | pH 7.4, 37°C | Deinagkistrodon acutus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | venom | Deinagkistrodon acutus | - |
- |
Metals/Ions
| 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. The binding of Cu2þ ions to AA-NADase is reversible, overview | Deinagkistrodon acutus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
2 x * 50000, SDS-PAGE | Deinagkistrodon acutus |
| 100000 | - |
about | Deinagkistrodon acutus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Deinagkistrodon acutus | 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 | ? | - |
? | |
| NAD+ + H2O | Deinagkistrodon acutus | - |
ADP-ribose + nicotinamide | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Deinagkistrodon acutus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from venom | Deinagkistrodon acutus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| venom | - |
Deinagkistrodon acutus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
activities of hydrolysis of NAD, ATP, ADP, and and AMP-PNP, overview | Deinagkistrodon acutus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | Deinagkistrodon acutus | ? | - |
? | |
| 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 | Deinagkistrodon acutus | ? | - |
? | |
| NAD+ + H2O | - |
Deinagkistrodon acutus | ADP-ribose + nicotinamide | - |
? | |
| nicotinamide guanine dinucleotide + H2O | - |
Deinagkistrodon acutus | 3',5'-cyclic GDP-ribose + GDP-ribose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 x * 50000, SDS-PAGE | Deinagkistrodon acutus |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| AA-NADase | - |
Deinagkistrodon acutus |
| NAD glycohydrolase | - |
Deinagkistrodon acutus |
| NADase | - |
Deinagkistrodon acutus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Deinagkistrodon acutus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 22.3 | - |
NAD+ | pH 7.4, 37°C | Deinagkistrodon acutus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Deinagkistrodon acutus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.86 | - |
NAD+ | pH 7.4, 37°C | Deinagkistrodon acutus | |
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