Fatty acid synthase (FAS)[1] is an enzyme that in humans is encoded by the FASN gene.[2][3][4][5]
Fatty acid synthase is a multi-enzyme protein that catalyzes fatty acid synthesis. It is not a single enzyme but a whole enzymatic system composed of two identical 272 kDa multifunctional polypeptides, in which substrates are handed from one functional domain to the next.[1][6][7][8][9]
Its main function is to catalyze the synthesis of palmitate (C16:0, a long-chain saturated fatty acid) from acetyl-CoA and malonyl-CoA, in the presence of NADPH.[5]
The fatty acids are synthesized by a series of decarboxylative Claisen condensation reactions from acetyl-CoA and malonyl-CoA. Following each round of elongation the beta keto group is reduced to the fully saturated carbon chain by the sequential action of a ketoreductase (KR), dehydratase (DH), and enoyl reductase (ER). The growing fatty acid chain is carried between these active sites while attached covalently to the phosphopantetheine prosthetic group of an acyl carrier protein (ACP), and is released by the action of a thioesterase (TE) upon reaching a carbon chain length of 16 (palmitic acid).[1]
^ abcPaiva P, Medina FE, Viegas M, Ferreira P, Neves RP, Sousa JP, Ramos MJ, Fernandes PA (2021-08-11). "Animal Fatty Acid Synthase: A Chemical Nanofactory". Chemical Reviews. 121 (15): 9502–9553. doi:10.1021/acs.chemrev.1c00147. ISSN 0009-2665. PMID 34156235. S2CID 235595027.
^Jayakumar A, Chirala SS, Chinault AC, Baldini A, Abu-Elheiga L, Wakil SJ (February 1995). "Isolation and chromosomal mapping of genomic clones encoding the human fatty acid synthase gene". Genomics. 23 (2): 420–424. doi:10.1006/geno.1994.1518. PMID 7835891.
^Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ (Oct 1995). "Human fatty acid synthase: properties and molecular cloning". Proceedings of the National Academy of Sciences of the United States of America. 92 (19): 8695–8699. Bibcode:1995PNAS...92.8695J. doi:10.1073/pnas.92.19.8695. PMC 41033. PMID 7567999.
^Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Feb 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1–3): 94–98. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
^ ab"Entrez Gene: FASN fatty acid synthase".
^Alberts AW, Strauss AW, Hennessy S, Vagelos PR (October 1975). "Regulation of synthesis of hepatic fatty acid synthetase: binding of fatty acid synthetase antibodies to polysomes". Proceedings of the National Academy of Sciences of the United States of America. 72 (10): 3956–3960. Bibcode:1975PNAS...72.3956A. doi:10.1073/pnas.72.10.3956. PMC 433116. PMID 1060077.
^Stoops JK, Arslanian MJ, Oh YH, Aune KC, Vanaman TC, Wakil SJ (May 1975). "Presence of two polypeptide chains comprising fatty acid synthetase". Proceedings of the National Academy of Sciences of the United States of America. 72 (5): 1940–1944. Bibcode:1975PNAS...72.1940S. doi:10.1073/pnas.72.5.1940. PMC 432664. PMID 1098047.
^Smith S, Agradi E, Libertini L, Dileepan KN (April 1976). "Specific release of the thioesterase component of the fatty acid synthetase multienzyme complex by limited trypsinization". Proceedings of the National Academy of Sciences of the United States of America. 73 (4): 1184–1188. Bibcode:1976PNAS...73.1184S. doi:10.1073/pnas.73.4.1184. PMC 430225. PMID 1063400.
^Smith S, Witkowski A, Joshi AK (July 2003). "Structural and functional organization of the animal fatty acid synthase". Progress in Lipid Research. 42 (4): 289–317. doi:10.1016/S0163-7827(02)00067-X. PMID 12689621.
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