Structural highlights
Function
[FAS2_YEAST] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101]
Publication Abstract from PubMed
Acyl carrier proteins participate in the synthesis of fatty acids. Here we report the NMR resonances assignment of the acyl carrier protein domain of the Saccharomyces cerevisiae fatty acid synthase which corresponds to the fragment 138A-302L in the primary structure. The assignment will allow performing NMR studies with the aim to investigate the intrinsic dynamics of this protein, and to study the structural changes upon apo-holo transformation in order to unveil the mechanism of binding of the growing acyl chain.
1H, 15N, 13C resonance assignment of the acyl carrier protein subunit of the Saccharomyces cerevisiae fatty acid synthase.,Perez DR, Wider G Biomol NMR Assign. 2009 Jun;3(1):133-6. doi: 10.1007/s12104-009-9158-4. Epub 2009, Apr 7. PMID:19636964[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Perez DR, Wider G. 1H, 15N, 13C resonance assignment of the acyl carrier protein subunit of the Saccharomyces cerevisiae fatty acid synthase. Biomol NMR Assign. 2009 Jun;3(1):133-6. doi: 10.1007/s12104-009-9158-4. Epub 2009, Apr 7. PMID:19636964 doi:http://dx.doi.org/10.1007/s12104-009-9158-4
