General Stability | Organism |
---|---|
EDTA stabilizes the purified enzyme during storage | Oryctolagus cuniculus |
enzyme is associated to the histidine-proline-rich-glycoprotein HPRG via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability | Oryctolagus cuniculus |
additional information | Oryctolagus cuniculus |
phosphate stabilizes the tetrameric structure of the enzyme | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phosphate | competitive inhibitor, stabilizing the tetrameric enzyme structure | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.4 | - |
AMP | crude enzyme extract, pH 6.5, 20°C | Oryctolagus cuniculus | |
0.6 | - |
AMP | imidazole-eluted purified enzyme, pH 6.5, 20°C | Oryctolagus cuniculus | |
1 | - |
AMP | EDTA-eluted purified enzyme, pH 6.5, 20°C | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | stabilizing the enzyme structure | Oryctolagus cuniculus | |
Zn2+ | enzyme HPRG component binds to Zn2+ | Oryctolagus cuniculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
80000 | - |
4 * 80000, stabilized by phosphate | Oryctolagus cuniculus |
309000 | - |
- |
Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | enzyme contains a histidine-proline-rich-glycoprotein HPRG component | Oryctolagus cuniculus |
Purification (Comment) | Organism |
---|---|
both native enzyme and its histidine-proline-rich-glycoprotein HPRG component, the latter being completely separated from the enzyme and its catalytic subunit by Zn2+-affinity chromatography including presence of 1 M KCl | Oryctolagus cuniculus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
AMP + H2O = IMP + NH3 | enzyme is associated to the histidine-proline-rich-glycoprotein HPRG via its catalytic subunit in a protein-protein complex | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1100 | - |
purified enzyme | Oryctolagus cuniculus |
Storage Stability | Organism |
---|---|
4°C, purified enzyme, loss of 50% activity within 1 week in absence of EDTA, in presence of EDTA it is stable for 10 days, fragmentation occurs at 4°C | Oryctolagus cuniculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
AMP + H2O | - |
Oryctolagus cuniculus | IMP + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 70000-95000, histidine-proline-rich-glycoprotein HPRG component, partially proteolyzed or deglycosylated, SDS-PAGE | Oryctolagus cuniculus |
More | enzyme contains a histidine-proline-rich-glycoprotein HPRG component, bound via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability, disulfide bridges are involved in formation of enzyme conformation | Oryctolagus cuniculus |
tetramer | 4 * 80000, stabilized by phosphate | Oryctolagus cuniculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Oryctolagus cuniculus |