Any feedback?
Literature summary for 3.5.1.5 extracted from
- A combined temperature-pH study of urease kinetics. Assigning pKa values to ionizable groups of the active site involved in the catalytic reaction (2016), J. Mol. Catal. B, 124, 70-76 .
No PubMed abstract available
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
Urea | a combined temperature-pH study of urease kinetics is performed at eight pHs between 5.0 and 8.3 in noninteracting biological buffers (MES and HEPES), at each pH at five temperatures between 15°C and 35°C. The analysis of the determined kinetic parameters KM and vmax shows that even though both the thermodynamic and activation parameters of the urease reaction are little pH-dependent | Canavalia ensiformis |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ni2+ | nickel-dependent metallo-enzyme | Canavalia ensiformis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| urea + H2O | Canavalia ensiformis | - |
CO2 + 2 NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Canavalia ensiformis | P07374 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| urea + H2O | - |
Canavalia ensiformis | CO2 + 2 NH3 | - |
? | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
