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Literature summary for 3.5.4.1 extracted from
- An insight into the environmental effects of the pocket of the active site of the enzyme. Ab initio ONIOM-molecular dynamics (MD) study on cytosine deaminase (2008), J. Comput. Chem., 29, 458-465.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the crystal structure of cytosine deaminase combined with the substrate uracil, PDB ID code: 1P6O, optimization in the water solvent at the ONIOM molecular dynamics study, overview | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cytosine + H2O | Saccharomyces cerevisiae | - |
uracil + NH3 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | Q12178 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cytosine + H2O | - |
Saccharomyces cerevisiae | uracil + NH3 | - |
? | |
| cytosine + H2O | - |
Saccharomyces cerevisiae | uracil + NH3 | uracil binding structure at the active site, analysis by ab initio ONIOM-MD simulations showing that uracil is strongly perturbed by Ile33, which sandwiches uracil with His62, through the steric contact due to the thermal motion, detailed overview | ? | |
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