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Literature summary for 3.2.2.5 extracted from
- Critical role for NAD glycohydrolase in regulation of erythropoiesis by hematopoietic stem cells through control of intracellular NAD content (2014), J. Biol. Chem., 289, 16362-16373.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, genomic structure, recombinant expression of FLAG-tagged wild-type and mutant enzymes in HEK293 cells | Oryctolagus cuniculus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | sh-RNA-mediated enzyme knockdown in HEK293 cells using shRNA-expressing lentivirus | Oryctolagus cuniculus |
| Q218A | site-directed mutagenesis | Oryctolagus cuniculus |
| Q218D | site-directed mutagenesis, loss of NADase activity without increase in ADP-ribosyltransferase activity | Oryctolagus cuniculus |
| Q218E | site-directed mutagenesis, loss of NADase activity and increase in ADP-ribosyltransferase activity | Oryctolagus cuniculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell surface | NADase is a glycosylated, glycosylphosphatidylinositol-anchored cell surface protein | Oryctolagus cuniculus | 9986 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 32769 | - |
x * 40000, SDS-PAGE, x * 32769, sequence calculation | Oryctolagus cuniculus |
| 40000 | - |
x * 40000, SDS-PAGE, x * 32769, sequence calculation | Oryctolagus cuniculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NAD+ + H2O | Oryctolagus cuniculus | - |
ADP-D-ribose + nicotinamide | - |
? |  |
| NAD+ + H2O | Oryctolagus cuniculus New Zealand White | - |
ADP-D-ribose + nicotinamide | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
| Oryctolagus cuniculus New Zealand White | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the NADase is glycosylated | Oryctolagus cuniculus |
| side-chain modification | the enzyme is a glycosylphosphatidylinositol-anchored cell surface protein | Oryctolagus cuniculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 81fold from reticulocytes, by lipid extracction, affinity and hydrophobic interaction chromatography, and gel filtration | Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| bone marrow cell | - |
Oryctolagus cuniculus | - |
| hematopoietic stem cell | - |
Oryctolagus cuniculus | - |
| intestine | - |
Oryctolagus cuniculus | - |
| additional information | not in muscle, heart, brain, kidney, spleen, liver, lung, and testis | Oryctolagus cuniculus | - |
| reticulocyte | - |
Oryctolagus cuniculus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 74.5 | - |
purified native enzyme from reticulocytes, pH 7.5, 37°C | Oryctolagus cuniculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NAD+ + H2O | - |
Oryctolagus cuniculus | ADP-D-ribose + nicotinamide | - |
? | |
| NAD+ + H2O | - |
Oryctolagus cuniculus New Zealand White | ADP-D-ribose + nicotinamide | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, SDS-PAGE, x * 32769, sequence calculation | Oryctolagus cuniculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NAD glycohydrolase | - |
Oryctolagus cuniculus |
| NADase | - |
Oryctolagus cuniculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Oryctolagus cuniculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | shRNA-mediated knockdown of the NADase in bone marrow cells results in a reduction of erythroid colony formation and an increase in NAD level, and treatment of the bone marrow cells with NAD, nicotinamide, or nicotinamide riboside, which induce an increase in NAD content, results in a significant decrease in erythroid progenitors | Oryctolagus cuniculus |
| additional information | the catalytic glutamine 218 of NADase is a crucial residue for NADase activity | Oryctolagus cuniculus |
| physiological function | the enzyme may play a critical role in regulating erythropoiesis of hematopoietic stem cells by modulating intracellular NAD+ | Oryctolagus cuniculus |
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Release 2023.1 (January 2023)
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