The surprising diversity of Δ6-desaturase substrates. (1st February 2004)
- Record Type:
- Journal Article
- Title:
- The surprising diversity of Δ6-desaturase substrates. (1st February 2004)
- Main Title:
- The surprising diversity of Δ6-desaturase substrates
- Authors:
- Guillou, H.
D'Andrea, S.
Rioux, V.
Jan, S.
Legrand, P. - Abstract:
- Abstract : A single gene encoding a δ6-desaturase (FADS2) has been isolated and characterized in mammalian species. This δ6-desaturase plays a major role in the biosynthesis of PUFAs (polyunsaturated fatty acids). It catalyses the rate-limiting desaturation of linoleic acid (C18:2 n −6) and α-linolenic acid (C18:3 n −3) required for the biosynthesis of long-chain PUFAs. Moreover, recent studies have provided strong evidence that this δ6-desaturase also acts on 24-carbon PUFAs of both the n −6 and n −3 series. Another substrate of this δ6-desaturase has been identified through complementary works from different investigators. This δ6-desaturase acts on a saturated fatty acid, palmitic acid (C16:0 ), leading to the newly characterized biosynthesis of hexadecenoic acid (C16:1 n −10) or sapienate.
- Is Part Of:
- Biochemical Society transactions. Volume 32:Number 1(2004)
- Journal:
- Biochemical Society transactions
- Issue:
- Volume 32:Number 1(2004)
- Issue Display:
- Volume 32, Issue 1 (2004)
- Year:
- 2004
- Volume:
- 32
- Issue:
- 1
- Issue Sort Value:
- 2004-0032-0001-0000
- Page Start:
- 86
- Page End:
- 87
- Publication Date:
- 2004-02-01
- Subjects:
- Δ6-desaturase -- FADS2 -- palmitic acid -- polyunsaturated fatty acid (PUFA)
Biochemistry -- Congresses
572 - Journal URLs:
- https://portlandpress.com/biochemsoctrans ↗
- DOI:
- 10.1042/bst0320086 ↗
- Languages:
- English
- ISSNs:
- 0300-5127
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 15899.xml