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Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase (and not to be confused with Long Chain fatty acyl-CoA synthetase), is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.〔 ==Reaction== The enzyme catalyzes the reaction: Acetyl-CoA + n malonyl-CoA + 4n NADPH + 4n H+ long-chain-acyl-CoA + n CoA + n CO2 + 4n NADP+ The 4 substrates of this enzyme are acetyl-CoA, malonyl-CoA, NADPH, and H+, whereas its 4 products are Acyl-CoA, CoA, CO2, and NADP+. More specifically, the FAS catalysis mechanism consumes an acetyl-coenzyme A (acetyl-CoA) and seven malonyl-CoA molecules to produce a Palmitoyl-CoA. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Fatty-acyl-CoA synthase」の詳細全文を読む スポンサード リンク
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