Any feedback?
Information on EC 1.14.19.13 - acyl-CoA 15-desaturase
for references in articles please use BRENDA:EC1.14.19.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.19.13 acyl-CoA 15-desaturaseIUBMB Comments
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.
Specify your search results
Word Map
- 1.14.19.13
-
linolenic
-
polyunsaturated
-
desaturases
- flax
- usitatissimum
-
linum
-
desaturation
-
omega-6
-
trienoic
-
linseed
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
fad3a, omega-3 desaturase, fad3-2, rkd12, cpfad2, csfad3, csfad3a, cpfad3, ehdes15, fad3-1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional DELTA12/DELTA15-fatty acid desaturase
CpFAD2
CpFAD3
DELTA12-desaturase
DELTA12-fatty acid desaturase
DELTA15 desaturase
DELTA15 fatty acid desaturase
DELTA15-fatty acid desaturase
DES3
EhDES15
RKD12
additional information
DES3
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z,15Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + 2 H2O
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + H2O
-
-
-
-
?
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + H2O
-
the double bond introduced by the enzyme occurs between carbons 15 and 16 resulting in a terminal double bond aliphatic chain
-
-
?
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z,15Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + 2 H2O
-
-
-
?
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z,15Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + 2 H2O
Rhodotorula kratochvilovae YM25235
-
-
-
?
additional information
?
-
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
-
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
recombinant CpFad3 produces 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
-
-
?
additional information
?
-
recombinant CpFad3 produces 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
-
-
?
additional information
?
-
-
recombinant CpFad3 produces 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
-
-
?
additional information
?
-
unambiguous identification of the triunsaturated product of CpFad2 as DELTA9,DELTA12,DELTA15-16:3 with terminal (n-1) double bond by comparing its spectrum to that of DELTA9,DELTA12,DELTA15-16:3 methylester. The major products of recombinant 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
-
-
?
additional information
?
-
unambiguous identification of the triunsaturated product of CpFad2 as DELTA9,DELTA12,DELTA15-16:3 with terminal (n-1) double bond by comparing its spectrum to that of DELTA9,DELTA12,DELTA15-16:3 methylester. The major products of recombinant 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
-
-
?
additional information
?
-
-
unambiguous identification of the triunsaturated product of CpFad2 as DELTA9,DELTA12,DELTA15-16:3 with terminal (n-1) double bond by comparing its spectrum to that of DELTA9,DELTA12,DELTA15-16:3 methylester. The major products of recombinant 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
-
-
?
additional information
?
-
Candida parapsilosis CP-69
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
Candida parapsilosis CP-69
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
Candida parapsilosis CP-69
unambiguous identification of the triunsaturated product of CpFad2 as DELTA9,DELTA12,DELTA15-16:3 with terminal (n-1) double bond by comparing its spectrum to that of DELTA9,DELTA12,DELTA15-16:3 methylester. The major products of recombinant 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
-
-
?
additional information
?
-
Candida parapsilosis CP-69
unambiguous identification of the triunsaturated product of CpFad2 as DELTA9,DELTA12,DELTA15-16:3 with terminal (n-1) double bond by comparing its spectrum to that of DELTA9,DELTA12,DELTA15-16:3 methylester. The major products of recombinant 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
-
-
?
additional information
?
-
Candida parapsilosis CP-69
recombinant CpFad3 produces 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
-
-
?
additional information
?
-
Candida parapsilosis CP-69
recombinant CpFad3 produces 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
-
-
?
additional information
?
-
the FAD3 enzyme is responsible for the DELTA15 desaturation of linoleic acid (18:2DELTA9,12) to alpha-linolenoic acid (18:3DELTA9,12,15) and of gamma-linolenic acid (18:3DELTA6,9,12) to stearidonic acid (18:4DELTA6,9,12,15). CSFAD3A acts as a DELTA15 desaturase in vivo as well as in a heterologous host
-
-
?
additional information
?
-
the enzyme produces linoleic acid and alpha-linolenic acid, overview
-
-
?
additional information
?
-
-
the enzyme produces linoleic acid and alpha-linolenic acid, overview
-
-
?
additional information
?
-
absence of desaturation activity of RKD12 for C16 substrates
-
-
?
additional information
?
-
-
absence of desaturation activity of RKD12 for C16 substrates
-
-
?
additional information
?
-
Rhodotorula kratochvilovae YM25235
the enzyme produces linoleic acid and alpha-linolenic acid, overview
-
-
?
additional information
?
-
Rhodotorula kratochvilovae YM25235
absence of desaturation activity of RKD12 for C16 substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + H2O
-
-
-
-
?
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12,15-trienoyl-CoA + acceptor + H2O
-
the double bond introduced by the enzyme occurs between carbons 15 and 16 resulting in a terminal double bond aliphatic chain
-
-
?
additional information
?
-
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
-
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
Candida parapsilosis CP-69
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
Candida parapsilosis CP-69
analysis of content in polyunsaturated and hydroxylated fatty acids in the cells, mass spectrometric analysis, overview
-
-
?
additional information
?
-
the FAD3 enzyme is responsible for the DELTA15 desaturation of linoleic acid (18:2DELTA9,12) to alpha-linolenoic acid (18:3DELTA9,12,15) and of gamma-linolenic acid (18:3DELTA6,9,12) to stearidonic acid (18:4DELTA6,9,12,15). CSFAD3A acts as a DELTA15 desaturase in vivo as well as in a heterologous host
-
-
?
additional information
?
-
the enzyme produces linoleic acid and alpha-linolenic acid, overview
-
-
?
additional information
?
-
-
the enzyme produces linoleic acid and alpha-linolenic acid, overview
-
-
?
additional information
?
-
Rhodotorula kratochvilovae YM25235
the enzyme produces linoleic acid and alpha-linolenic acid, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Non-mammalian fat-1 gene prevents neoplasia when introduced to a mouse hepatocarcinogenesis model Omega-3 fatty acids prevent liver neoplasia.
Prostatic Neoplasms
Effect of dietary polyunsaturated fatty acids on castration-resistant Pten-null prostate cancer.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from Chenghai Lake in Yunnan, China
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
brenda
developing, high expression level, particularly from 6 to 12 days after flowering and from 18 to 24 days after flowering, corresponding with the phases of seed expansion and oil accumulation respectively
brenda
developing, high expression level, particularly from 6 to 12 days of flowering and from 18 to 24 days of flowering, corresponding with the phases of seed expansion and oil accumulation respectively
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
integral membrane enzyme
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
all members of the CSFAD3 subclass contain eight exons and seven introns within the gene. Evolutionary relationship of Cannabis sativa putative desaturases, overview
evolution
bifunctional DELTA12/DELTA15-desaturases are widely found in fungi species belonging to Ascomycota and Basidiomycota. Enzyme RKD12 shares higher homology to the Cop-odeA, it only exhibits DELTA12 and DELTA15 desaturation activity on C18 substrates without preference
evolution
three different copies of the genes FAD2 and FAD3 are identified, which contain three histidine rich motifs (HXCGHX, HRXHH andHVXHH) and six highly conserved transmembrane domains. Comparing their sequences, the CsFAD2copies accommodate four conservative changes (E36D, R48H, V97A, and A177P) and two semi-conservative ones (V63I and L249M), whereas only one semi-conservative change (A327S) is detected in CsFAD3 but with two extra amino acids (H147 and G148)
evolution
Rhodotorula kratochvilovae YM25235
-
bifunctional DELTA12/DELTA15-desaturases are widely found in fungi species belonging to Ascomycota and Basidiomycota. Enzyme RKD12 shares higher homology to the Cop-odeA, it only exhibits DELTA12 and DELTA15 desaturation activity on C18 substrates without preference
-
metabolism
the enzyme is is thought to be involved in 18:5n-3 biosynthesis
metabolism
-
the enzyme is is thought to be involved in 18:5n-3 biosynthesis
-
physiological function
DELTA12-fatty acid desaturase CpFAD2 from Candida parapsilosis is a multifunctional desaturase producing a range of DELTA12- and DELTA15-polyunsaturated and hydroxylated fatty acids
physiological function
DELTA12-fatty acid desaturase CpFAD3 from Candida parapsilosis is a DELTA15-desaturase producing 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), overview
physiological function
for better adaptation to low temperatures, Rhodosporidium kratochvilovae YM25235 may have evolved some adaptative mechanisms that might include the alteration of unsaturation levels of fatty acids in membrane lipids involving the enzyme
physiological function
the FAD3 enzyme is responsible for the DELTA15 desaturation of linoleic acid (18:2DELTA9,12) to alpha-linolenoic acid (18:3DELTA9,12,15)
physiological function
Candida parapsilosis CP-69
-
DELTA12-fatty acid desaturase CpFAD2 from Candida parapsilosis is a multifunctional desaturase producing a range of DELTA12- and DELTA15-polyunsaturated and hydroxylated fatty acids
-
physiological function
Candida parapsilosis CP-69
-
DELTA12-fatty acid desaturase CpFAD3 from Candida parapsilosis is a DELTA15-desaturase producing 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), overview
-
physiological function
Rhodotorula kratochvilovae YM25235
-
for better adaptation to low temperatures, Rhodosporidium kratochvilovae YM25235 may have evolved some adaptative mechanisms that might include the alteration of unsaturation levels of fatty acids in membrane lipids involving the enzyme
-
additional information
hemp seeds contain three DELTA15 desaturases, FAD3A is the major DELAT15 desaturase in hemp seed
additional information
the enzyme contains a putative transit sequence for localization in chloroplasts and a DELTA6 desaturase-like domain, but it does not contain a cytochrome b5 domain nor typical His-boxes found in DELTA15 desaturases
additional information
-
the enzyme contains a putative transit sequence for localization in chloroplasts and a DELTA6 desaturase-like domain, but it does not contain a cytochrome b5 domain nor typical His-boxes found in DELTA15 desaturases
additional information
-
the enzyme contains a putative transit sequence for localization in chloroplasts and a DELTA6 desaturase-like domain, but it does not contain a cytochrome b5 domain nor typical His-boxes found in DELTA15 desaturases
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DES3_SORBI
389
4
44775
Swiss-Prot
other Location (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 22°C compared to 30°C, 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 22°C compared to 30°C, 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 22°C compared to 30°C, 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 30°C, 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a culture temperature downshift from 28C to 15C induces the enzyme
a culture temperature downshift from 28C to 15C induces the enzyme
a culture temperature downshift from 28C to 15C induces the enzyme
Rhodotorula kratochvilovae YM25235
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xue, Z.; He, H.; Hollerbach, D.; Macool, D.J.; Yadav, N.S.; Zhang, H.; Szostek, B.; Zhu, Q.
Identification and characterization of new DELTA-17 fatty acid desaturases
Appl. Microbiol. Biotechnol.
97
1973-1985
2013
Fusarium verticillioides
brenda
Pan, Z.; Rimando, A.; Baerson, S.; Fishbein, M.; Duke, S.
Functional characterization of desaturases involved in the formation of the terminal double bond of an unusual 16:3DELTA9,12,15 fatty acid isolated from Sorghum bicolor root hairs
J. Biol. Chem.
282
4326-4335
2007
Sorghum bicolor
brenda
Kotajima, T.; Shiraiwa, Y.; Suzuki, I.
Functional screening of a novel DELTA15 fatty acid desaturase from the coccolithophorid Emiliania huxleyi
Biochim. Biophys. Acta
1842
1451-1458
2014
Emiliania huxleyi (R1FY33), Emiliania huxleyi, Emiliania huxleyi CCMP1516 (R1FY33)
brenda
Cui, J.; He, S.; Ji, X.; Lin, L.; Wei, Y.; Zhang, Q.
Identification and characterization of a novel bifunctional DELTA12/DELTA15-fatty acid desaturase gene from Rhodosporidium kratochvilovae
Biotechnol. Lett.
38
1155-1164
2016
Rhodotorula kratochvilovae (A0A024B710), Rhodotorula kratochvilovae, Rhodotorula kratochvilovae YM25235 (A0A024B710)
brenda
Rodriguez-Rodriguez, M.; Salas, J.; Venegas-Caleron, M.; Garces, R.; Martinez-Force, E.
Molecular cloning and characterization of the genes encoding a microsomal oleate DELTA12 desaturase (CsFAD2) and linoleate DELTA15 desaturase (CsFAD3) from Camelina sativa
Ind. Crops Prod.
89
405-415
2016
Camelina sativa (A0A059V6T7), Camelina sativa (A0A059V8B3), Camelina sativa (A0A059V8R1)
-
brenda
Bielecka, M.; Kaminski, F.; Adams, I.; Poulson, H.; Sloan, R.; Li, Y.; Larson, T.R.; Winzer, T.; Graham, I.A.
Targeted mutation of DELTA12 and DELTA15 desaturase genes in hemp produce major alterations in seed fatty acid composition including a high oleic hemp oil
Plant Biotechnol. J.
12
613-623
2014
Cannabis sativa (A0A088MER7)
brenda
Bucek, A.; Matouskova, P.; Sychrova, H.; Pichova, I.; Hruskova-Heidingsfeldova, O.
DELTA12-Fatty acid desaturase from Candida parapsilosis is a multifunctional desaturase producing a range of polyunsaturated and hydroxylated fatty acids
PLoS ONE
9
e93322
2014
Candida parapsilosis (C3W956), Candida parapsilosis (C3W957), Candida parapsilosis, Candida parapsilosis CP-69 (C3W956), Candida parapsilosis CP-69 (C3W957)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.19.13)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
