Crystallization (Comment) | Organism |
---|---|
crystal structures of apo MTAP and MTAP in complex with p-Cl-PhT-DADMe-ImmA are determined at 1.9 and 2.0 A resolution, respectively. Inhibitor binding causes condensation of the enzyme active site, reorganization at the trimer interfaces, the release of water from the active sites and subunit interfaces, and compaction of the trimeric structure. These structural changes cause the entropy-favored binding of transition state analogues | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
p-Cl-PhT-DADMe-ImmA | - |
Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q13126 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenosine + phosphate | - |
Homo sapiens | adenine + D-ribose 1-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MTAP | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |