EC Number   |
General Information |
Reference |
|---|
   2.3.1.86 | malfunction |
construction of Fas2 disruptants influences virulence, unability to form normal biofilms |
706450 |
| 2.3.1.86 | metabolism |
cotranslational assembly of yeast FAS. The N-terminus of subunit alpha (FAS2) intertwines with the C-terminus of subunt beta (FAS1) by getting sandwiched between a structured malonyl-palmitoyl-transferase core fold and a alpha67/alpha68 element. The cotranslationally formed interaction is sensitive to perturbations. The assembly of yeast FAS can also proceed when subunit borders are shifted. Linking subunits of FAS at the cotranslationally formed interface and introducing splitting sites at two other sites, within the alpha-helical bundle structure 4-helical bundle of subunit alpha and within the antiparallel 6-stranded beta-sheet of beta, leads to intact protein. The cotranslational assembly may not be strictly sequence- or site-specific |
-, 758355 |
| 2.3.1.86 | physiological function |
essential for growth in absence of exogenous fatty acids, involved in unsatured fatty acid production |
706450 |
| 2.3.1.86 | physiological function |
translation machinery-associated protein Tma17 copurifies with FAS complex. 6 copies of Tma17p can simultaneously bind to one FAS molecule, binding follows a positive cooperativity. Tma17 acts as FAS gamma subunit regulating the activity in response to the abundance of cosubstrate NADPH |
-, 756369 |
