Any feedback?
Literature summary for 3.2.1.18 extracted from
- Modulation of catalytic function by differential plasticity of an active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase (2009), Biochemistry, 48, 3398-3406.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| comparison of the catalytic cleft plasticity of free and ligand-bound forms of Trypanosoma rangeli sialidase and Trypanosoma cruzi trans-sialidase using molecular dynamics simulations. The Trypanosoma cruzi enzyme has a very flexible, widely open catalytic cleft, mostly due to resiude W312 loop motion, in apo form. In ligan-bound form, the flexibility and solvent exposure is significantly reduced. The Trypanosoma rangeli sialidase maintains a more open catalytic cleft in both apo and holo forms | Trypanosoma cruzi |
| comparison of the catalytic cleft plasticity of free and ligand-bound forms of Trypanosoma rangeli sialidase and Trypanosoma cruzi trans-sialidase using molecular dynamics simulations. The Trypanosoma cruzi enzyme has a very flexible, widely open catalytic cleft, mostly due to resiude W312 loop motion, in apo form. In ligan-bound form, the flexibility and solvent exposure is significantly reduced. The Trypanosoma rangeli sialidase maintains a more open catalytic cleft in both apo and holo forms | Trypanosoma rangeli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma cruzi | - |
- |
- |
| Trypanosoma rangeli | O44049 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
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
