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1.14.19.5: acyl-CoA 11-(Z)-desaturase

This is an abbreviated version!
For detailed information about acyl-CoA 11-(Z)-desaturase, go to the full flat file.

Word Map on EC 1.14.19.5

Reaction

long-chain acyl-CoA
+
reduced acceptor
+
O2
=
DELTA11-acyl-CoA
+
acceptor
+ 2 H2O

Synonyms

(Z)-11 myristoyl CoA desaturase, acyl-CoA DELTA11-desaturase, acyl-CoA desaturase, acyl-CoA Z/E11 desaturase, APTQ desaturase, bifunctional DELTA11-desaturase, bifunctional Z-DELTA11-desaturase, Cro-Z/E11, CroDELTA11 desaturase, DELTA11 desaturase, DELTA11-(Z)-desaturase, DELTA11-desaturase, DELTA11-fatty-acid desaturase, DELTA11-myristoyl-CoA desaturase, DELTA11-palmitoyl-CoA-desaturase, DELTA11-palmitoyl-coenzyme A desaturase, desat1, desaturase, myristoly coenzyme A (E)-11, Dpu-DELTA11-APSQ, Dpu-DELTA11-LPAE, EC 1.14.99.32, fatty acid DELTA11-desaturase, fatty acyl DELTA11-desaturase, LATPG1, Lca-KPVQ, MambrD11-desaturase, More, myristoyl-CoA 11-(Z) desaturase, OfuZ/E11 protein, OscZ/E11 protein, PDesat-TnDELTA11 Z protein, Sls//E11, sphingolipid long chain base delta 8 desaturase, TpDESN, Z/E11-desaturase, Z/EDELTA11

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
                1.14.19.5 acyl-CoA 11-(Z)-desaturase

General Information

General Information on EC 1.14.19.5 - acyl-CoA 11-(Z)-desaturase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the fatty acid desaturase type 1 family
metabolism
physiological function
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