EC Number   |
Reference |
|---|
   2.3.1.85 | high-resolution crystal structure of a large part of human fatty acid synthase that encompasses the tandem domain of beta-oxoacyl synthase KS connected by a linker domain to the malonyltransferase domain MAT, to 2.15 A resolution. Hinge regions that allow for substantial flexibility of the subdomains are defined. The KS domain forms the canonical dimer, and its substrate-binding site geometry differs markedly from that of bacterial homologues but is similar to that of the porcine orthologue. The didomain structure reveals a possible way to generate a small and compact KS domain by omitting a large part of the linker and MAT domains, which could greatly aid in rapid screening of KS inhibitors. In the crystal, the MAT domain exhibits two closed conformations that differ significantly by rigid-body plasticity |
720236 |
| 2.3.1.85 | 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 |
735720 |
| 2.3.1.85 | of thioesterase domain, which comprises two dissimilar subdomains A and B |
663217 |
| 2.3.1.85 | pharmacophore modeling based on crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase domain, PDB entry 3HHD |
719057 |
| 2.3.1.85 | structure at 4.5 A resolution. The dimeric synthase adopts an asymmetric X-shaped conformation with two reaction chambers on each side formed by a full set of enzymatic domains required for fatty acid elongation, which are separated by considerable distances |
677121 |
| 2.3.1.85 | structure-based homology modeling based on PDB entry 2uv8 |
756432 |
| 2.3.1.85 | three-dimensional map of yeast fatty acid synthase at 5.9 A resolution, obtained by electron cryomicroscopy of single particles. Distinct density regions in the reaction chambers next to each of the catalytic domains fitted the substrate-binding acyl carrier protein domain. In each case, this results in the expected distance of about 18 A from the acyl carrier protein substrate-binding site to the active site of the catalytic domains. The multiple, partially occupied positions of the acyl carrier protein within the reaction chamber provide direct structural insight into the substrate-shuttling mechanism. The acyl carrier protein domain is mobile within the fatty acid synthase barrel, enabling it to visit successive catalytic sites |
720912 |
