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Information on EC 1.14.19.31 - acyl-lipid (7-3)-desaturase and Organism(s) Papio anubis and UniProt Accession B8R1K0

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IUBMB Comments
The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta7 double bond. The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate . The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
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Papio anubis
UNIPROT: B8R1K0
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Word Map
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  • 1.14.19.31
  • desaturation
  • docosahexaenoic
  • polyunsaturated
  • pavlova
  • microalgae
  • eicosapentaenoic
  • delta5
  • front-end
  • desaturases
The taxonomic range for the selected organisms is: Papio anubis
The enzyme appears in selected viruses and cellular organisms
Synonyms
delta4-desaturase, pldes1, delta4-fatty acid desaturase, psd4des, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
DELTA7 acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase (4,5 cis-dehydrogenating)
The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta7 double bond. The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate [5]. The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
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 classical transcript mediates direct DELTA4-desaturation of 22:5n-3 to 22:6n-3 (docosahexaenoic acid) and of 22:4n-6 to 22:5n-6. The evidence supports trifunctionality of FADS2. The classical transcript shows DELTA6, DELTA8, and DELTA4 activities in mammals
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the localization of FADS2 in mitochondria, supports the involvement of this organelle in long-chain polyunsaturated fatty acid synthesis
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in MCF-7 human breast cancer cells. MCF-7 cells stably expressing FADS1 and FADS2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, H.G.; Park, W.J.; Kothapalli, K.S.; Brenna, J.T.
The fatty acid desaturase 2 (FADS2) gene product catalyzes DELTA4 desaturation to yield n-3 docosahexaenoic acid and n-6 docosapentaenoic acid in human cells
FASEB J.
29
3911-3919
2015
Papio anubis (B8R1K0)
Manually annotated by BRENDA team