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Information on EC 1.14.19.3 - acyl-CoA 6-desaturase and Organism(s) Danio rerio and UniProt Accession Q9DEX7

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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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Danio rerio
UNIPROT: Q9DEX7
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The taxonomic range for the selected organisms is: Danio rerio
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
DELTA-6 desaturase
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DELTA6-acyl CoA desaturase
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-
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DELTA6-desaturase
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-
-
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DELTA6-fatty acyl-CoA desaturase
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desaturase, fatty acid DA6-
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-
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desaturase, linoleate
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-
-
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fatty acid 6-desaturase
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-
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fatty acid DA6-desaturase
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-
-
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linoleate desaturase
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-
-
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linoleic acid desaturase
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-
-
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linoleic desaturase
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-
-
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linoleoyl CoA desaturase
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-
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linoleoyl-coenzyme A desaturase
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long-chain fatty acid DELTA6-desaturase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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-
-
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the zebrafish enzyme is a bifunctional DELTA5/DELTA6 desaturase
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the zebrafish enzyme is a bifunctional DELTA5/DELTA6 desaturase
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FADS2_DANRE
444
3
52032
Swiss-Prot
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vagner, M.; Santigosa, E.
Characterization and modulation of gene expression and enzymatic activity of DELTA-6 desaturase in teleosts: A review
Aquaculture
315
131-143
2011
Dicentrarchus labrax (B2ZE91), Rachycentron canadum (B7U6V1), Gadus morhua (Q4TVM9), Scophthalmus maximus (Q6QDP0), Salmo salar (Q6SES0), Sparus aurata (Q8AY64), Oncorhynchus mykiss (Q98SW7), Cyprinus carpio (Q9DEX6), Danio rerio (Q9DEX7)
Manually annotated by BRENDA team