Inhibitors | Comment | Organism | Structure |
---|---|---|---|
C75 | binds the thioesterase domain in a similar orientation to that of palmitate, with its hydrophobic group buried inside the distal pocket and hydrophilic group interacting with the catalytic triad | Homo sapiens | |
orlistat | in the lowest-energy conformation, its central formylamino group is very close to the catalytic triad of the thioesterase domain. Its shorter chain is placed into the distal pocket where palmitate acyl chain binds and its longer chain extends into pocket 2 | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity | Homo sapiens | ? | - |
? | |
palmitoyl-CoA + H2O | ligand-binding pocket of the thioesterase domain encompasses the catalytic triad of Ser2308, His2481, Asp2338. The hydrophobic interactions are the major decisive factor for the optimal binding of the alphatic chain of palmitate | Homo sapiens | CoA + palmitate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FAS | - |
Homo sapiens |
fatty acid synthase thioesterase | - |
Homo sapiens |