1.14.19.24: acyl-CoA 11-(E)-desaturase
This is an abbreviated version!
For detailed information about acyl-CoA 11-(E)-desaturase, go to the full flat file.
Word Map on EC 1.14.19.24
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1.14.19.24
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pheromone
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moth
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desaturases
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desaturation
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delta9
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littoralis
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ostrinia
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borer
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z-11-hexadecenoic
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tetradecanoic
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helicoverpa
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deuterium-labeled
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furnacalis
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nubilalis
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hexadecanoic
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gland-specific
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trichoplusia
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assulta
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adzuki
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pseudonana
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front-end
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thalassiosira
- 1.14.19.24
- pheromone
- moth
-
desaturases
-
desaturation
-
delta9
- littoralis
- ostrinia
- borer
-
z-11-hexadecenoic
-
tetradecanoic
- helicoverpa
-
deuterium-labeled
- furnacalis
- nubilalis
-
hexadecanoic
-
gland-specific
-
trichoplusia
- assulta
-
adzuki
- pseudonana
-
front-end
-
thalassiosira
Reaction
+ 2 ferrocytochrome b5 + + 2 H+ = + 2 ferricytochrome b5 + 2 H2O
Synonyms
(E)-11 myristoyl CoA desaturase, acyl-CoA Z/E11 desaturase, CroDELTA11 desaturase, DELTA11 desaturase, DELTA11-desaturase, desaturase, myristoly coenzyme A (E)-11, EC 1.14.99.31, EDELTA11, LATPG1, More, myristoyl-CoA 11-(E) desaturase, Z/E11 desaturase, Z/EDELTA11
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General Information
General Information on EC 1.14.19.24 - acyl-CoA 11-(E)-desaturase
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evolution
additional information
the enzyme belongs to the fatty acid desaturase type 1 family
evolution
the enzyme belongs to the fatty acid desaturase type 1 family
at least three DELTA11-desaturase genes are present in the genome of Ostrinia latipennis, and gene latpg1 is selectively transcribed in the pheromone gland of this moth
additional information
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at least three DELTA11-desaturase genes are present in the genome of Ostrinia latipennis, and gene latpg1 is selectively transcribed in the pheromone gland of this moth
additional information
the 258E/D residue contributes to the formation of the secondary coordination sphere of the dimetal unit, along with 129D, 133D and 228N, molecular docking study, overview. This residue might be influencing the shape of the reactive cavity and may play an important role in the catalytic property of this desaturase. Residue D258 in the cytosolic carboxyl terminus of the protein is critical for the steroechmistry of activity
additional information
the 258E/D residue contributes to the formation of the secondary coordination sphere of the dimetal unit, along with 129D, 133D and 228N, molecular docking study, overview. This residue might be influencing the shape of the reactive cavity and may play an important role in the catalytic property of this desaturase. Residue E258 in the cytosolic carboxyl terminus of the protein is critical for the steroechmistry of activity