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Information on EC 1.14.19.3 - acyl-CoA 6-desaturase and Organism(s) Siganus canaliculatus and UniProt Accession B2KKL4

for references in articles please use BRENDA:EC1.14.19.3
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EC Tree
IUBMB Comments
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA , and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate . The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
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Siganus canaliculatus
UNIPROT: B2KKL4
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Word Map
The taxonomic range for the selected organisms is: Siganus canaliculatus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fads2, delta-6 desaturase, delta6-desaturase, delta 6-desaturase, delta 6 desaturase, fatty acid desaturase 2, delta-6-desaturase, delta6 desaturase, delta6-fatty acid desaturase, fads6, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA6-desaturase
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DELTA6-acyl CoA desaturase
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DELTA6-desaturase
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DELTA6-fatty acyl-CoA desaturase
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desaturase, fatty acid DA6-
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desaturase, linoleate
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fatty acid 6-desaturase
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fatty acid DA6-desaturase
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linoleate desaturase
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linoleic acid desaturase
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linoleic desaturase
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linoleoyl CoA desaturase
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linoleoyl-coenzyme A desaturase
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long-chain fatty acid DELTA6-desaturase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA [4], and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate [3]. The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-34-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + AH2 + O2
?
show the reaction diagram
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?
linoleic acid + AH2 + O2
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show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression
Manually annotated by BRENDA team
weak expression
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FAD1_SIGCA
443
3
51872
Swiss-Prot
other Location (Reliability: 3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, Y.Y.; Hu, C.B.; Zheng, Y.J.; Xia, X.A.; Xu, W.J.; Wang, S.Q.; Chen, W.Z.; Sun, Z.W.; Huang, J.H.
The effects of dietary fatty acids on liver fatty acid composition and Delta6-desaturase expression differ with ambient salinities in Siganus canaliculatus
Comp. Biochem. Physiol. B
151
183-190
2008
Siganus canaliculatus (B2KKL4), Siganus canaliculatus
Manually annotated by BRENDA team