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Information on EC 1.14.19.6 - acyl-CoA (9+3)-desaturase and Organism(s) Caenorhabditis elegans and UniProt Accession G5EGA5

for references in articles please use BRENDA:EC1.14.19.6
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IUBMB Comments
This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9. When acting on 19:1Delta10 fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, towards the methyl-end of the fatty acid. Requires cytochrome b5 as the electron donor .
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Caenorhabditis elegans
UNIPROT: G5EGA5
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
delta 12 desaturase, fad-2, delta-12 fatty acid desaturase, le-fad2, delta 12 fatty acid desaturases, ptfad2, csfad2a, delta12 fad, delta12 acyl-lipid desaturase, microsomal delta-12 fatty acid desaturase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA12-desaturase
-
FAT-2
a bifunctional DELTA12/DELTA15-desaturase
acyl-CoA (9+3)-desaturase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (12,13 cis-dehydrogenating)
This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9. When acting on 19:1Delta10 fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, towards the methyl-end of the fatty acid. Requires cytochrome b5 as the electron donor [4].
CAS REGISTRY NUMBER
COMMENTARY hide
84628-81-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
heptadecyloleic acid + reduced acceptor + O2
C17:2DELTA9,12 + acceptor + H2O
show the reaction diagram
-
-
-
?
myristoleic acid + reduced acceptor + O2
C14:2DELTA9,12 + acceptor + H2O
show the reaction diagram
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
show the reaction diagram
-
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
show the reaction diagram
-
-
-
?
pentadecyloleic acid + reduced acceptor + O2
C15:2DELTA9,12 + acceptor + H2O + acceptor
show the reaction diagram
-
-
-
?
additional information
?
-
the enzyme can also catalyze DELTA15 desaturation
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FAT2_CAEEL
376
4
43463
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peyou-Ndi, M.M.; Watts, J.L.; Browse, J.
Identification and characterization of an animal DELTA12 fatty acid desaturase gene by heterologous expression in Saccharomyces cerevisiae
Arch. Biochem. Biophys.
376
399-408
2000
Caenorhabditis elegans
Manually annotated by BRENDA team
Zhou, X.; Green, A.; Singh, S.
Caenorhabditis elegans ?12-desaturase FAT-2 is a bifunctional desaturase able to desaturate a diverse range of fatty acid substrates at the DELTA12 and DELTA15 positions
J. Biol. Chem.
286
43644-43650
2011
Caenorhabditis elegans (G5EGA5)
Manually annotated by BRENDA team