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Information on EC 1.14.19.3 - acyl-CoA 6-desaturase and Organism(s) Borago officinalis and UniProt Accession O04353

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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Borago officinalis
UNIPROT: O04353
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The taxonomic range for the selected organisms is: Borago officinalis
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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-
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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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desaturase, linoleate
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-
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fatty acid 6-desaturase
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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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-
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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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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
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
-
-
-
-
?
linoleoyl phosphatidylcholine + AH2 + O2
gamma-linolenoylphosphatidylcholine + A + H2O
show the reaction diagram
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-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
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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
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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membrane
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DES6_BOROF
448
5
51635
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
transformed into Agrobacterium tumefaciens and expressed in Glycine max
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Griffiths, G.; Stobart, A.K.; Stymne, S.
DELTA 6- and DELTA 12-desaturase activities and phosphatidic acid formation in microsomal preparations from the developing cotyledons of common borage (Borago officinalis)
Biochem. J.
252
641-647
1988
Borago officinalis
Manually annotated by BRENDA team
Eckert, H.; La Vallee, B.; Schweiger, B.J.; Kinney, A.J.; Cahoon, E.B.; Clemente, T.
Co-expression of the borage DELTA6 desaturase and the Arabidopsis DELTA15 desaturase results in high accumulation of stearidonic acid in the seeds of transgenic soybean
Planta
224
1050-1057
2006
Borago officinalis
Manually annotated by BRENDA team
Chen, Q.; Nimal, J.; Li, W.; Liu, X.; Cao, W.
Delta-6 desaturase from borage converts linoleic acid to gamma-linolenic acid in HEK293 cells
Biochem. Biophys. Res. Commun.
410
484-488
2011
Borago officinalis (O04353), Borago officinalis
Manually annotated by BRENDA team