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Information on EC 1.14.19.3 - acyl-CoA 6-desaturase and Organism(s) Papio anubis and UniProt Accession B8R1K0

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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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Papio anubis
UNIPROT: B8R1K0
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Word Map
The taxonomic range for the selected organisms is: Papio anubis
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-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
additional information
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the FADS2 product introduces a double bond at the DELTA6, DELTA4 and DELTA8 positions by acting on at least ten substrates, including fatty acids 16:0, 18:2n-6, and 18:3n-3. MCF7 cells stably transformed with FADS2 biosynthesizes fatty acid 16:1n-10 from exogenous fatty acid 16:0, fatty acid 18:4n-3 from fatty acid 18:3n-3, fatty acid 18:3n-6 from fatty acid 18:2n-6, fatty acid 18:2n-9 from fatty acid 18:1n-9, fatty acid 24:6n-3 from fatty acid 24:5n-3 and fatty acid 24:5n-6 from fatty acid 24:4n-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FADS2_PAPAN
444
4
52301
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in MCF7 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, H.G.; Kothapalli, K.S.D.; Park, W.J.; DeAllie, C.; Liu, L.; Liang, A.; Lawrence, P.; Brenna, J.T.
Palmitic acid (16 0) competes with omega-6 linoleic and omega-3 alpha-linolenic acids for FADS2 mediated DELTA6-desaturation
Biochim. Biophys. Acta
1861
91-97
2016
Papio anubis (B8R1K0)
Manually annotated by BRENDA team