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1.14.19.33: DELTA12 acyl-lipid conjugase (11E,13E-forming)

This is an abbreviated version!
For detailed information about DELTA12 acyl-lipid conjugase (11E,13E-forming), go to the full flat file.

Reaction

a gamma-linolenoyl-[glycerolipid]
+ 2 ferrocytochrome b5 +
O2
+ 2 H+ =
an alpha-parinaroyl-[glycerolipid]
+ 2 ferricytochrome b5 + 2 H2O

Synonyms

DELTA12 desaturase, DELTA12 oleate desaturase, FADX, FADX-1A, FADX-1B, FADX-2, fatty acid DELTA12-conjugase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
                1.14.19.33 DELTA12 acyl-lipid conjugase (11E,13E-forming)

Engineering

Engineering on EC 1.14.19.33 - DELTA12 acyl-lipid conjugase (11E,13E-forming)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D115E
site-directed mutagenesis, the mutant shows reaction product like the wild-type enzyme, predominantly alpha-eleostearic acid and little punicic acid
G111V
site-directed mutagenesis, the mutant shows reaction product like the wild-type enzyme, predominantly alpha-eleostearic acid and little punicic acid
G111V/D115E
site-directed mutagenesis, the mutant shows reaction product unlike the wild-type enzyme, approximately equal amounts of alpha-eleostearic acidandits isomer, punicic acid
additional information
construction of a series of Momordica charantia FADX-Arabidopsis thaliana FAD2 chimeras: chimera 1 contains Momordica FADX amino acids 1-157 and Arabidopsis FAD2 amino acids 149-383, chimera 2 contains FADX aa 1–210 with FAD2 aa 202-383, chimera 3 contains FADX aa 1-252 with FAD2 aa 244-383, chimera 4 contains FADX aa 1-326 with FAD2 aa 317-383, chimera 5 contains FAD2 aa 1-52 with FADX aa 61-399, chimera 6 contains FAD2 aa 1-83 with FADX aa 93-399, chimera 7 contains FAD2 aa 1-116 with FADX aa 126-399, and chimera 8 containsFAD2 aa 1-148 with FADX aa 158-399, mutant product formations, overview. Analysis of a FADX mutant containing six substitutions in which the sequence of helix 2 and first histidine box is converted to that of FAD2