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Literature summary for 2.3.1.85 extracted from
- Regulating effect of beta-ketoacyl synthase domain of fatty acid synthase on fatty acyl chain length in de novo fatty acid synthesis (2016), Biochim. Biophys. Acta, 1861, 149-155.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| molecular dynamic simulation based binding free energy calculation and access tunnels analysis. The C16 acyl tail fatty acid, the major product of FAS, fits to the active site on beta-ketoacyl synthase domain better than any other substrates. The geometric shape of active site on beta-ketoacyl synthase domain might explain the product ratio of FAS | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
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Release 2023.1 (January 2023)
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