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Activation is catalyzed by fatty acyl-CoA synthetases (also called acyl-CoA ligases or thiokinases). The net result of this activation process is the consumption of two molar equivalents of ATP. Humans express at least 26 acyl-CoA synthetases with several of these enzymes also being involved in fatty acid transport into cells (FATP1–FATP6) as indicated in the Table above in the Cellular Uptake of Fatty Acids section. The various acyl-CoA synthetases exhibit different substrate specificities, subcellular localization, and tissue distribution. Additional members of the family are the long-chain acyl-CoA synthetases.
Long chain fatty acyl-CoA synthetase, LC-FACS, plays a role in the physiological regulation of various cellular functions via the production of long chain fatty acyl-CoA esters, which reportedly have affected protein transport, enzyme activation, protein acylation, cell signaling, and transcriptional regulation.  The formation of fatty acyl-CoA is catalyzed in two steps: a stable intermediate of fatty acyl-AMP molecule and then the product is formed—fatty acid acyl-CoA molecule.
SLC27A1 (FATP1), SLC27A2 (FATP2), SLC27A3 (FATP3), SLC27A4 (FATP4), SLC27A5 (FATP5), SLC27A6 (FATP6) FATP1 is also known as acyl-CoA synthetase very long-chain family, member 5 (ACSVL5) FATP2 is also known as acyl-CoA synthetase very long-chain family, member 1 (ACSVL1) and very long-chain acyl-CoA synthetase.
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.