1.14.19.34: acyl-lipid (9+3)-(E)-desaturase
This is an abbreviated version!
For detailed information about acyl-lipid (9+3)-(E)-desaturase, go to the full flat file.
Reaction
+ 2 ferrocytochrome b5 + + 2 H+ = + 2 ferricytochrome b5 + 2 H2O
Synonyms
acyl-lipid 12-(E)-desaturase, DELTA12 oleate desaturase, DELTA12 oleic acid desaturase, DELTA12-oleic acid desaturase, DsFAD2-1, DsFAD2-2, FAD2, FADX
ECTree
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Reaction
Reaction on EC 1.14.19.34 - acyl-lipid (9+3)-(E)-desaturase
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a palmitoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-hexadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2)
-
-
-
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(1)
-
-
-
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
proposed mechanism of DsFAD2-2: removal of a C-11 hydrogen atom from trans-DELTA12-linoleic acid by the diiron-oxo center of DsFAD2-2 results in the shift of the cis-DELTA9 double bond to the trans-DELTA10 position. The radical remaining at the C-9 position is then able to remove an oxygen atom from the diiron-oxo center because of close proximity to the catalytic core of DsFAD2-2 as dictated by the substrate binding properties of this enzyme