Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence.

@article{Mohamed1988PrimarySO,
  title={Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence.},
  author={Ayman Helmy Mohamed and Subrahmanyam S. Chirala and Nat Mody and William Y. Huang and Salih J. Wakil},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 25},
  pages={12315-25}
}
The yeast fatty acid synthase consists of two multifunctional proteins, alpha and beta, arranged in an alpha 6 beta 6 complex with a molecular weight of 2.4 x 10(6). Five of the seven enzymatic activities reside in the beta subunit, while the remaining two activities, beta-ketoacyl synthase and beta-ketoacyl reductase, and the domain of the acyl carrier protein, with its prosthetic group, 4'-phosphopantetheine, are in the alpha subunit. The genes FAS1 and FAS2 coding for beta and alpha subunits… CONTINUE READING