Cloned (Comment) | Organism |
---|---|
the small regulatory subunit is cloned, expressed and purified | Thermoplasma acidophilum |
Crystallization (Comment) | Organism |
---|---|
structure solved and refined at a resolution of 2.35 A. The enzyme shares a similar fold and a highly conserved C-D-K-catalytic triad, Cys123, Asp9, and Lys90 with the structures of three cysteine hydrolases (PDB codes: 1NBA, 1IM5, and 2HOR). Molecular dynamics simulations of Ta0454/N-carbamoylsarcosine and Ta0454/pyrazinamide complexes are performed to determine the structural basis of the substrate binding pattern for each ligand. The predicted binding free energies suggest that Ta0454 is selective for N-carbamoylsarcosine over pyrazinamide, and zinc ions play an important role in the favorable substrate bound states | Thermoplasma acidophilum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zinc | zinc ions play an important role in the favorable substrate bound staes | Thermoplasma acidophilum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoplasma acidophilum | Q9HKY9 | - |
- |
Purification (Comment) | Organism |
---|---|
the small regulatory subunit is cloned, expressed and purified | Thermoplasma acidophilum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-carbamoylsarcosine + H2O | - |
Thermoplasma acidophilum | sarcosine + CO2 + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CSHase | - |
Thermoplasma acidophilum |
N-carbamoylsarcosine amidase Ta0454 | - |
Thermoplasma acidophilum |
General Information | Comment | Organism |
---|---|---|
physiological function | involved in the degradation of creatinine | Thermoplasma acidophilum |