Fatty acid desaturase

Fatty acid desaturase, type 1
Symbol Fatty_acid_desaturase-1
Pfam PF00487
InterPro IPR005804
Fatty acid desaturase, type 2
Symbol Fatty_acid_desaturase-2
Pfam PF03405
InterPro IPR005067

A fatty acid desaturase is an enzyme that removes two hydrogen atoms from a fatty acid, creating a carbon/carbon double bond. These desaturases are classified as

In the biosynthesis of essential fatty acids, an elongase alternates with different desaturases (for example, Δ6desaturase) repeatedly inserting an ethyl group, then forming a double bond.


Maintain structure and function of membranes within cells of the organisms above. This is important when temperatures changes and the membrane is under distress. The enzyme creates the double bond C-Cs which allow the membrane to become more fluid and the temperature is decreased.[1] When temperatures change, a phase transition occurs. In the case of a temperature decrease, the membrane gels and becomes solid which can result in cracks and the imbedded proteins cannot partake in conformational changes, therefore it is important to maintain membrane fluidity.[2]

Role in human metabolism

Fatty acid desaturase appear in all organisms: for example, bacteria fungus plants animals and humans.[1] Four desaturases occur in humans: Δ9 desaturase, Δ6 desaturase, Δ5 desaturase, and Δ4 desaturase.

Δ9 desaturase, also known as stearoyl-CoA desaturase-1, is used to synthesize oleic acid, a monounsaturated, ubiquitous component of all cells in the human body. Δ9 desaturase produces oleic acid by desaturating stearic acid, a saturated fatty acid either synthesized in the body from palmitic acid or ingested directly.

Δ6 and Δ5 desaturases are required for the synthesis of highly unsaturated fatty acids such as eicosopentaenoic and docosahexaenoic acids (synthesized from α-linolenic acid), and arachidonic acid (synthesized from linoleic acid). This is a multi-stage process requiring successive actions by elongase and desaturase enzymes. The genes coding for Δ6 and Δ5 desaturase production have been located on human chromosome 11.


Vertebrates are unable to synthesize polyunsaturated fatty acids because they do not have the necessary fatty acid desaturases to "convert oleic acid (18:1n-9) into linoleic acid (18:2n-6) and α-linolenic acid".[3] These polyunsaturated fatty acids are important for ideal health within humans and are essential for development. By creating desaturations at the Δ6 and Δ5 positions in the carbon backbone with the addition of an elongation allows the process of linoleic acid to achidonic acid and from α-linolenic acid to eicosapentaenoic acid to partake.[3]


Δ-desaturases are represented by two distinct families which do not seem to be evolutionarily related.

Family 1 includes Stearoyl-CoA desaturase-1 (SCD) (EC[4]

Family 2 is composed of:

Related Research

Kodama et al. (1994) found that an increased amount of trienoic fatty acids allow plants to become more tolerant to cold temperatures.[7] These trienoic fatty acids are associated with plant response to cold temperatures and allows the plant to adjust. They determined that transgenic tobacco plants that contained a fatty acid desaturase gene were able to tolerate low temperatures better than wild-type plants.[7]


  1. 1 2 Los, Dmitry A.; Murata, Norio (1998-10-02). "Structure and expression of fatty acid desaturases". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1394 (1): 3–15. doi:10.1016/S0005-2760(98)00091-5.
  2. Alberts, Bruce (2015). Molecular Biology of the Cell. New York: Garland Science. p. 571. ISBN 978-0-8153-4453-7.
  3. 1 2 Hastings, Nicola; Agaba, Morris; Tocher, Douglas R.; Leaver, Michael J.; Dick, James R.; Sargent, John R.; Teale, Alan J. (2001-12-04). "A vertebrate fatty acid desaturase with Δ5 and Δ6 activities". Proceedings of the National Academy of Sciences. 98 (25): 14304–14309. doi:10.1073/pnas.251516598. ISSN 0027-8424. PMC 64677Freely accessible. PMID 11724940.
  4. Lane MD, Ntambi JM, Kaestner KH, Kelly Jr TJ (1989). "Differentiation-induced gene expression in 3T3-L1 preadipocytes. A second differentially expressed gene encoding stearoyl-CoA desaturase". J. Biol. Chem. 264 (25): 14755–14761. PMID 2570068.
  5. Shanklin J, Somerville C (1991). "Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs". Proc. Natl. Acad. Sci. U.S.A. 88 (6): 2510–2514. doi:10.1073/pnas.88.6.2510. PMC 51262Freely accessible. PMID 2006187.
  6. Wada H, Gombos Z, Murata N (1990). "Enhancement of chilling tolerance of a cyanobacterium by genetic manipulation of fatty acid desaturation". Nature. 347 (6289): 200–203. doi:10.1038/347200a0. PMID 2118597.
  7. 1 2 Kodama, H.; Hamada, T.; Horiguchi, G.; Nishimura, M.; Iba, K. (1994-06-01). "Genetic Enhancement of Cold Tolerance by Expression of a Gene for Chloroplast [omega]-3 Fatty Acid Desaturase in Transgenic Tobacco". Plant Physiology. 105 (2): 601–605. doi:10.1104/pp.105.2.601. ISSN 1532-2548. PMID 12232227.

Nakamura MT, Nara TY (2004). "Structure, function and dietary regulation of Δ6, Δ5 and Δ9 desaturases". Annual Review of Nutrition. 24 (24): 345–76. doi:10.1146/annurev.nutr.24.121803.063211. PMID 15189125. 

This article incorporates text from the public domain Pfam and InterPro IPR005067

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