Structure
Yeast fatty acyl synthase, of Type I FAS, is composed of a α6β6 complex in which an αβ unit forms one functional center for fatty acid synthesis. Yeast fatty acyl synthase therefore has six reaction units for its fatty acid synthesis, in which each of these units function independently from one another. Each α and β subunit, in turn, has four functional domains, and together, the eight functional domains catalyze all the reactions of fatty acid synthesis in yeast, which includes: activation, priming, elongation, and termination. Consequently, yeast FAS is incredibly unique due to its structural complexity, which contains 48 functional centers for one α6β6 complex and can efficiently performs 6 fatty acid syntheses separately at one time.
There are seven, total enzymatic reactions in fatty acid synthesis. These reactions include: activation, priming, four reactions in elongation, and termination. Five these reactions are performed in the beta subunit and two reactions are performed in the alpha subunit.
Read more about this topic: Fatty-acyl-Co A Synthase
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