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Literature summary for 3.5.3.1 extracted from
- Biochemical and biophysical insights into the metal binding spectrum and bioactivity of arginase of Entamoeba histolytica (2018), Metallomics, 10, 623-638 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli Rosetta (DE3) | Entamoeba histolytica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Entamoeba histolytica |  |
| NaCl | the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increased, the activity of the enzyme was reduced to almost half of the maximal activity but the enzyme was still partially active | Entamoeba histolytica | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Cd2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Co2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Cu2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Hg2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Mg2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Mn2+ | two Mn2+ ions are required for the enzyme to be fully functional | Entamoeba histolytica | |
| NaCl | the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increase, the activity of the enzyme is reduced to almost half of the maximal activity but the enzyme is still partially active | Entamoeba histolytica | |
| Ni2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
| Zn2+ | chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity | Entamoeba histolytica | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginine + H2O | Entamoeba histolytica | the enzyme catalyses the catabolism of L-arginine to L-ornithine and urea | L-ornithine + urea | - |
? | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| urea | 8 M urea denatures the enzyme which results in the release of the deeply embedded metal ion too | Entamoeba histolytica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | C4LSS0 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Entamoeba histolytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginine + H2O | - |
Entamoeba histolytica | L-ornithine + urea | - |
? | |
| L-arginine + H2O | the enzyme catalyses the catabolism of L-arginine to L-ornithine and urea | Entamoeba histolytica | L-ornithine + urea | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | exists in monomeric and dimeric form in solution | Entamoeba histolytica |
| monomer | exists in monomeric and dimeric form in solution | Entamoeba histolytica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
- |
Entamoeba histolytica |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 4 | 70 | 4°C: about 80% of maximal activity, 70°C: about 95% of maximal activity | Entamoeba histolytica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | 9 | - |
Entamoeba histolytica |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 11 | pH 5.0: about 55% of maximal activity, pH 11.0: about 50% of maximal activity | Entamoeba histolytica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme catalyses the catabolism of l-arginine to l-ornithine and urea. First committed step in polyamine biosynthesis. In pathogenic organisms, arginase plays a crucial role in depleting host L-arginine, a substrate for nitric oxide synthase that participates in protective immunity, thereby evading host immune response | Entamoeba histolytica |
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