Fatty acid desaturase

Fatty acid desaturase, type 1
Identifiers
Symbol Fatty_acid_desaturase-1
Pfam PF00487
InterPro IPR005804
Fatty acid desaturase, type 2
Identifiers
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.

Role in human metabolism

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.

DEGS1; DEGS2; FADS1; FADS2; FADS3; FADS6; SCD4; SCD5

Classification

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 1.14.19.1).[1]

Family 2 is composed of:

References

  1. 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.
  2. 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 51262. PMID 2006187.
  3. 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.

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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