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Information on EC 1.14.19.4 - acyl-lipid (11-3)-desaturase and Organism(s) Papio anubis and UniProt Accession B8R1K0

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IUBMB Comments
The enzyme, characterized from the protist Euglena gracilis and the microalga Rebecca salina , introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Delta11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
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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
delta8 desaturase, atsld1, delta8-desaturase, slsld, atsld2, delta8-sphingolipid desaturase, delta8 sphingolipid desaturase, delta8 sphingobase desaturase, boofd8, sphingolipid delta8-desaturase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA6-desaturase
-
DELTA8-desaturase
-
FADS2
the DELTA6-desaturase FADS2 shows DELTA8-desaturase activity
DELTA8-fatty-acid desaturase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
reduction
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase [(11-3),(11-2)-cis-dehydrogenating]
The enzyme, characterized from the protist Euglena gracilis [1] and the microalga Rebecca salina [2], introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Delta11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11,14,17-eicosatrienoic acid + reduced acceptor + O2
?
show the reaction diagram
20:3n-3, yield 20:4n-3
-
-
?
11,14-eicosadienoic acid + reduced acceptor + O2
?
show the reaction diagram
20:2n-6, yield 20:3n-6
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the pGEM-T easy vector for sequencing, into the pYES2 vector for expression in Saccharomyces cerevisiae cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, W.J.; Kothapalli, K.S.; Lawrence, P.; Tyburczy, C.; Brenna, J.T.
An alternate pathway to long-chain polyunsaturates: the FADS2 gene product DELTA8-desaturates 20:2n-6 and 20:3n-3
J. Lipid Res.
50
1195-1202
2009
Papio anubis (B8R1K0)
Manually annotated by BRENDA team