Native Microorganism Creatine Amidohydrolase
| Cat# | DIA-185 |
| Abbr | Creatinase, Native (Microorganism) |
| Alias | Creatinase |
| Source | Microorganism |
| Description | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ↔sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism. |
| Applications | This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. |
| Appearance | White amorphous powder, lyophilized |
| Form | Freeze dried powder |
| Enzyme Commission Number | EC 3.5.3.3 |
| Activity | 4.0 U/mg-solid or more |
| CAS No. | 37340-58-2 |
| Contaminants | NADH oxidase < 5.0×10⁻²%; Catalase < 2.0% |
| Molecular Weight | approx. 67 kDa (by gel filtration) |
| Isoelectric point | 4.5±0.1 |
| pH Stability | pH 4.0-10.0 (25°C, 20hr) |
| Michaelis Constant | 4.5×10－3 M (Creatine) |
| Structure | 2 subunits per mol of enzyme |
| Optimum pH | 6.5-7.5 |
| Optimum temperature | 40－50°C |
| Thermal stability | below 70°C (pH 7.5, 30min) |
| Stability | Stable at -20°C for at least one year |
| Stabilizers | Sugars, EDTA |
| Inhibitors | Hg⁺⁺, Cu⁺⁺, Ag⁺, SH reagent (NEM), PCMB |
| Synonyms | Creatine amidohydrolase; Creatinase; EC 3.5.3.3 |
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