|Gene:||desC2||Accession Number: G-14791 (MetaCyc)|
Synonyms: sn-2 acyl-lipid Δ9 desaturase
Species: Nostoc sp. 36
Acyl-lipid desaturases desaturate carbon single bonds in fatty acids that are esterified to membrane-bound glycerolipids [Chintalapati06]. Four types of front-loading acyl-lipid desaturases, DesA, DesB, DesC and DesD, have been described in cyanobacteria, that act at the 12, 15, 9 and 6 positions, respectively.
While all of the enzymes initially described are specific for fatty acids bound to the sn-1 position of glycerolipids, this enzyme, characterized from the cyanobacterium Nostoc sp. 36, desaturates fatty acids esterified on the sn-2 position of glycerolipids [Chintalapati06].
The desC2 gene was cloned from Nostoc sp. 36 and expressed in the cyanobacterium Synechocystis sp. PCC 6803, which cannot desaturate fatty acids at the sn-2 position. Analysis of lipids from the recombinant host identifed a prominent increase in the level of palmitoleate at the sn-2 position, indicating that the enzyme indeed acts on fatty acids at that position [Chintalapati06].
Molecular Weight of Polypeptide: 33.24 kD (from nucleotide sequence)
Enzymatic reaction of: sn-2 palmitoyl-lipid Δ9 desaturase (sn-2 acyl-lipid 9-desaturase)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: palmitoleate biosynthesis III (cyanobacteria)
Chintalapati06: Chintalapati S, Prakash JS, Gupta P, Ohtani S, Suzuki I, Sakamoto T, Murata N, Shivaji S (2006). "A novel Delta9 acyl-lipid desaturase, DesC2, from cyanobacteria acts on fatty acids esterified to the sn-2 position of glycerolipids." Biochem J 398(2);207-14. PMID: 16689682
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