ENZYME entry: EC 1.14.19.5
Accepted Name |
Acyl-CoA 11-(Z)-desaturase.
|
Alternative Name(s) |
Delta(11) desaturase. |
Delta(11)-fatty-acid desaturase. |
Delta(11)-palmitoyl-CoA desaturase. |
Fatty acid Delta(11)-desaturase. |
Z/E11-desaturase. |
Reaction catalysed |
An acyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O |
Comment(s) |
- The enzyme introduces a cis double bond at position C-11 of saturated
fatty acyl-CoAs.
- In moths the enzyme participates in the biosynthesis of their sex
pheromones.
- The enzyme from the marine microalga Thalassiosira pseudonana is
specific for palmitoyl-CoA (16:0), that from the leafroller moth
Choristoneura rosaceana desaturates myristoyl-CoA (14:0), while that
from the moth Spodoptera littoralis accepts both substrates.
- The enzyme contains three histidine boxes that are conserved in all
desaturases.
- It is membrane-bound, and contains a cytochrome b5-like domain at the
N-terminus that serves as the electron donor for the active site of
the desaturase.
- Formerly EC 1.14.19.n2 and EC 1.14.99.32.
|
Cross-references |
BRENDA | 1.14.19.5 |
EC2PDB | 1.14.19.5 |
ExplorEnz | 1.14.19.5 |
PRIAM enzyme-specific profiles | 1.14.19.5 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.19.5 |
IUBMB Enzyme Nomenclature | 1.14.19.5 |
IntEnz | 1.14.19.5 |
MEDLINE | Find literature relating to 1.14.19.5 |
MetaCyc | 1.14.19.5 |
Rhea expert-curated reactions | 1.14.19.5 |
UniProtKB/Swiss-Prot |
|
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