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Information on EC 1.14.19.3 - acyl-CoA 6-desaturase

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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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UNIPROT: Q54795
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Word Map
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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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain C1, gene desD
UniProt
Manually annotated by BRENDA team
strain C1, gene desD
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q54795_ARTPT
368
0
42084
TrEMBL
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene desD, functional analysis of the Spirulina promoter in Escherichia coli, the -10 sequence, TATAAT, located at -33 bp relative to the translation start site, is essential for D6D promoter function, an ‘AT-rich inverted repeat’ -192 to -164 serves as a target-binding site for a transcriptional regulator
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Subudhi, S.; Kurdrid, P.; Hongsthong, A.; Sirijuntarut, M.; Cheevadhanarak, S.; Tanticharoen, M.
Isolation and functional characterization of Spirulina D6D gene promoter: role of a putative GntR transcription factor in transcriptional regulation of D6D gene expression
Biochem. Biophys. Res. Commun.
365
643-649
2008
Arthrospira platensis (Q54795), Arthrospira platensis C1 (Q54795)
Manually annotated by BRENDA team