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MetaCyc Enzyme: fatty acyl Δ12 desaturase, endoplasmic reticulum

Gene: FAD2 Accession Number: AT3G12120 (MetaCyc)

Synonyms: At3g12120, oleate desaturase, oleate Δ12 desaturase, ω-6 oleate desaturase

Species: Arabidopsis thaliana col

Subunit composition of fatty acyl Δ12 desaturase, endoplasmic reticulum = [FAD2]
         ω-6 fatty acid desaturase, endoplasmic reticulum = FAD2

Summary:
This ER enzyme introduces a second double (Δ12) bond in oleate which is incorporated into phosphatidylcholine, an important extra-plastidial membrane lipid.

Citations: [Covello96]

Locations: endoplasmic reticulum

Molecular Weight of Polypeptide: 44.048 kD (from nucleotide sequence)

Unification Links: ArrayExpress:P46313 , PhylomeDB:P46313 , Pride:P46313 , String:3702.AT3G12120.2-P , TAIR:AT3G12120 , UniProt:P46313

Relationship Links: Entrez-Nucleotide:PART-OF:L26296 , InterPro:IN-FAMILY:IPR005804 , InterPro:IN-FAMILY:IPR021863 , Pfam:IN-FAMILY:PF00487 , Pfam:IN-FAMILY:PF11960

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005783 - endoplasmic reticulum


Enzymatic reaction of: lipid oleoyl,hydrogen donor:oxygen Δ12-oxidoreductase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

a lipid oleoyl-group + a reduced electron acceptor + oxygen <=> a lipid linoleoyl group + an oxidized electron acceptor + 2 H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: linoleate biosynthesis I (plants)


Enzymatic reaction of: 1-16:0-2-18:1-phosphatidylcholine desaturase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-16:0-2-18:1-phosphatidylcholine + a reduced electron acceptor + oxygen <=> 1-palmitoyl-2-linoleoyl-phosphatidylcholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


Enzymatic reaction of: 1-18:1-2-18:2-phosphatidylcholine desaturase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-18:1-2-18:2-phosphatidylcholine + a reduced electron acceptor + oxygen <=> 1-18:2-2-18:2-sn-glycerol-3-phosphocholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


Enzymatic reaction of: 1-18:2-2-18:1-phosphatidylcholine desaturase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-18:2-2-18:1-phosphatidylcholine + a reduced electron acceptor + oxygen <=> 1-18:2-2-18:2-sn-glycerol-3-phosphocholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


Enzymatic reaction of: 1-18:1-2-18:3-phosphatidylcholinedesaturase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-18:1-2-18:3-phosphatidylcholine + a reduced electron acceptor + oxygen <=> 1-18:2-2-18:3-phosphatidylcholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


Enzymatic reaction of: 1-18:3-2-18:1-phosphatidylcholine desaturase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-18:3-2-18:1-phosphatidylcholine + a reduced electron acceptor + oxygen <=> 1-18:3-2-18:2-phosphatidylcholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


Enzymatic reaction of: 1-18:1-2-18:2-phosphatidylcholine synthase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-18:1-2-18:1-sn-glycerol-3-phosphocholine + a reduced electron acceptor + oxygen <=> 1-18:1-2-18:2-phosphatidylcholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


Enzymatic reaction of: 1-18:1-2-18:1-sn-glycerol-3-phosphocholine desaturase (fatty acyl Δ12 desaturase, endoplasmic reticulum)

EC Number: 1.14.19.-

1-18:1-2-18:1-sn-glycerol-3-phosphocholine + a reduced electron acceptor + oxygen <=> 1-18:2-2-18:1-phosphatidylcholine + an oxidized electron acceptor + 2 H2O

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: phospholipid desaturation


References

Covello96: Covello PS, Reed DW (1996). "Functional expression of the extraplastidial Arabidopsis thaliana oleate desaturase gene (FAD2) in Saccharomyces cerevisiae." Plant Physiol 1996;111(1);223-6. PMID: 8685264

Okuley94: Okuley J, Lightner J, Feldmann K, Yadav N, Lark E, Browse J (1994). "Arabidopsis FAD2 gene encodes the enzyme that is essential for polyunsaturated lipid synthesis." Plant Cell 6(1);147-58. PMID: 7907506


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc14.