Crystallization (Comment) | Organism |
---|---|
molecular dynamics simulation. In the apo-enzyme, the two catalytic residues are chemically equivalent and are expected to be both unprotonated. Upon substrate binding, the catalytic residues of HTLV-1 protease evolve to a singly protonated state, in which the carboxylic oxygen atom OD1 of Asp32 is protonated and forms a hydrogen bond with the OD1 atom of Asp32' , which is unprotonated | Human T-cell leukemia virus type I |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human T-cell leukemia virus type I | Q82134 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Ace-Pro-Val-Ile-Leu-Pro-Ile-NMe + H2O | - |
Human T-cell leukemia virus type I | Ace-Pro-Val-Ile-Leu + Pro-Ile-NMe | - |
? |