Information on EC 1.14.19.13 - acyl-CoA 15-desaturase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.13
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RECOMMENDED NAME
GeneOntology No.
acyl-CoA 15-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2 = (9Z,12Z,15Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + 2 H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sorgoleone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA,reduced acceptor:oxygen oxidoreductase (15,16 cis-dehydrogenating)
The enzyme, characterized from the the plant Sorghum bicolor, is involved in the biosynthesis of sorgoleone, an allelopathic compound produced in root hair cells. The enzyme inserts a cis double bond at carbon 15. When acting on its natural substrate, (9Z,12Z)-hexadeca-9,12-dienoyl-CoA, it produces a product with a terminal double bond.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
isolated from Chenghai Lake in Yunnan, China
A0A024B710
UniProt
Manually annotated by BRENDA team
isolated from Chenghai Lake in Yunnan, China
A0A024B710
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + H2O
show the reaction diagram
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z,15Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + 2 H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + H2O
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
two Fe2+ ions bound in the His box; two Fe2+ ions bound in the His box; two Fe2+ ions bound in the His box
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
sequence calculation; sequence calculation; sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
expression of CSFAD3A in both leaves and embryos, it is induced during seed development peaking at the FND stage where it is about 14 times higher than levels in young leaves, quantitative RT-PCR expression analysis
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae InvSc1 cells
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expressed in Yarrowia lipolytica
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gene CsFAD3, variant FAD3-1, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview; gene CsFAD3, variant FAD3-2, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview; gene CsFAD3, variant FAD3-3, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview
gene EhDES15, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenic analysis, a codon-optimized EhDES15 gene lacking the 74 amino acid peptide serving as putative bipartite signal and transit peptides at the N-terminus is synthesized and expressed heterologously Synechocystis sp. PCC 6803 cells under control of the trc promoter leading to increased level of n-3 fatty acid species,which are produced at only low levels in wild-type cyanobacterial cells grown at 30C, semi-quantitative PCR expression analysis. Expression of gene EhDES15 in a Synechocystis mutant lacking the desB gene causes accumulation of 18:3n-3 and 18:4n-3 in the transformed cells
gene FAD2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression in Saccharomyces cerevisiae strain BY4741 supplemented with linoleic acid (DELTA9,DELTA12-18:2) and hexadecadienoic acid (DELTA9,DELTA12-16:2) leads to accumulation of DELTA15-PUFAs, i.e., alpha-linolenic acid (DELTA9,DELTA12,DELTA15-18:3) and hexadecatrienoic acid with an unusual terminal double bond (DELTA9,DELTA12,DELTA15-16:3) results in production of a range of DELTA12- and DELTA15-PUFAs. The major products of CpFad2 are linoleic and hexadecadienoic acid (DELTA9,DELTA12-16:2), accompanied by alpha-linolenic acid and hexadecatrienoic acid (DELTA9,DELTA12,DELTA15-16:3). Ricinoleic acid (12-hydroxy-9-octadecenoic acid) is an additional product of CpFad2 identified by GC/MS analysis; gene FAD3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression in Saccharomyces cerevisiae strain BY4741 supplemented with linoleic acid (DELTA9,DELTA12-18:2) and hexadecadienoic acid (DELTA9,DELTA12-16:2) leads to accumulation of DELTA15-PUFAs, i.e., alpha-linolenic acid (DELTA9,DELTA12,DELTA15-18:3) and hexadecatrienoic acid with an unusual terminal double bond (DELTA9,DELTA12,DELTA15-16:3) results in production of DELTA15-polyunsaturated fatty acids, i.e., alpha-linolenic acid (DELTA9,DELTA12,DELTA15-18:3) and hexadecatrienoic acid with an unusual terminal double bond (DELTA9,DELTA12,DELTA15-16:3), identified by GC/MS analysis
gene FAD3A, quantitative RT-PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae, CSFAD3A produces 18:2DELTA9,15 from endogenous 18:1DELTA9 when expressed in Saccharomyces cerevisiae
gene RKD12, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae
A0A024B710
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a culture temperature downshift from 28C to 15C induces the enzyme