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Enzyme Nomenclature
Information on EC 1.14.19.6 - acyl-CoA (9+3)-desaturase
Word Map on EC 1.14.19.6
- 1.14.19.6
-
linoleic
-
oleic
-
polyunsaturated
-
unsaturated
-
desaturation
-
alpha-linolenic
- cotton
-
omega3
-
di-unsaturated
-
hardening
- synechococcus
- plastidial
-
rapeseed
-
gossypium
- hirsutum
-
pufas
-
histidine-rich
- nutrition
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.14.19.6
-
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RECOMMENDED NAME
GeneOntology No.
acyl-CoA (9+3)-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
(1)
-
-
-
palmitoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = (9Z,12Z)-hexadeca-9,12-dienoyl-CoA + 2 ferricytochrome b5 + 2 H2O
(2)
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (12,13 cis-dehydrogenating)
This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9. When acting on 19:1Delta10 fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, towards the methyl-end of the fatty acid. Requires cytochrome b5 as the electron donor [4].
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CAS REGISTRY NUMBER
COMMENTARY
84628-81-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
functional expression of a DELTA12 fatty acid desaturase gene from Spinacia oleracea in transgenic Sus scrofa
SwissProt
-
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
the docosahexaenoic acid content is increased slightly in DELTA12des-disruption mutants
malfunction
-
the docosahexaenoic acid content is increased slightly in DELTA12des-disruption mutants
-
malfunction
-
the docosahexaenoic acid content is increased slightly in DELTA12des-disruption mutants
-
physiological function
the DELTA12-fatty acid desaturase gene is absolutely essential for the biosynthesis of linoleic acid as the main substrate for lipid peroxidation
physiological function
fatty acid desaturases, FADs, play an essential role in fatty acid metabolism and the maintenance of biological membranes; fatty acid desaturases, FADs, play an essential role in fatty acid metabolism and the maintenance of biological membranes
physiological function
-
inserted heterologous desA gene for DELTA12 acyl-lipid desaturase in potato plants results in improved tolerance of transformants to oxidative stress due to the more efficient maintenance of stable cell membrane structure functioning, and this permits prevention of electron jump to oxygen and, as a result, of accelerated reactive oxygen species generation
physiological function
-
overexpression of the acyl-lipid DELTA12-desaturase in transformed potato plants promotes fatty acid polyunsaturation and presumably averts the accelerated generation of the superoxide anion, thus suppressing lipid peroxidation under low-temperature stress
physiological function
-
the enzyme increases the tolerance to low temperature
physiological function
-
Solanum tuberosum plants expressing Synechocystis DELTA12-acyl-lipid desaturase experience less severe thermal and oxidative stress upon cooling and can cope with the cold without considerable increase in the enzyme activity
physiological function
-
the expression of DELTA12 acyl-lipid desaturase positively influences stabilization of not only structure but also functioning of chloroplast membranes in Solanum tuberosum, thus preventing a transfer of electrons from the electron transport chain to oxygen and subsequent reactive oxygen species generation at hypothermia
physiological function
-
recombinant enzyme expression improves potato plant resistance to Phytophthora infestans infection
physiological function
-
fatty acid desaturases, FADs, play an essential role in fatty acid metabolism and the maintenance of biological membranes; fatty acid desaturases, FADs, play an essential role in fatty acid metabolism and the maintenance of biological membranes
-
additional information
-
expression profile of desA gene from Synechocystis sp. PCC6803 and its effect on cell membrane lipid composition and cold tolerance in prokaryotic, Escherichia coli and eukaryotic, Solanum tuberosum cells, overview
additional information
-
shifting of the Mucor rouxii culture from anaerobic to aerobic conditions results in an increase of biomass and total fatty acid content. In addition, the levels of unsaturated fatty acids are enhanced accompanied by a decrease in the levels of medium- and long-chain saturated fatty acids, levels of expressions of the DELTA9-, DELTA12- and DELTA6-desaturases genes are coordinately upregulated after the shift, overview
additional information
the enzyme contains three histidine-rich domains and four membrane-spanning domains characteristic for DELTA12-fatty acid desaturases
additional information
the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes; the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes
additional information
the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes; the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes
additional information
-
the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes; the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes
-
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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
(10Z)-nonadec-10-enoic acid + reduced acceptor + O2
(10Z,13Z)-nonadeca-10,13-dienoic acid + acceptor + H2O
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
5,8,11,14-eicosatetraenoyl-CoA + reduced acceptor + O2
5,8,11,14,17-eicosadecapentaenoyl-CoA + acceptor + H2O
6,9,12-octadecatrienoyl-CoA + reduced acceptor + O2
6,9,12,15-octadecatetraenoyl-CoA + acceptor + H2O
9,12-octadecadienoyl-CoA + reduced acceptor + O2
9,12,15-octadecatrienoyl-CoA + acceptor + H2O
9-hexadecenoyl-CoA + reduced acceptor + O2
9,12-hexadecadienoyl-CoA + acceptor + H2O
low activity
-
-
?
9-octadecenoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + H2O
-
-
-
?
acyl-CoA + reduced acceptor + O2
DELTA12-acyl-CoA + acceptor + H2O
-
-
-
?
cis-7-hexadecenoic acid + reduced acceptor + O2
cis,cis-7,10-hexadecadienoic acid + acceptor + H2O
-
5.2% desaturation
-
-
?
cis-9-heptadecenoic acid + reduced acceptor + O2
cis,cis-9,12-heptadecadienoic acid + acceptor + H2O
-
22.3% desaturation
-
-
?
cis-9-hexadecenoic acid + reduced acceptor + O2
cis,cis-9,12-hexadecadienoic acid + acceptor + H2O
cis-9-icosenoic acid + reduced acceptor + O2
cis,cis-11,14-icosadienoic acid + acceptor + H2O
-
4.1% desaturation
-
-
?
cis-9-octadecenoic acid + reduced acceptor + O2
cis,cis-9,12-octadecadienoic acid + acceptor + 2 H2O
eicosenoic acid + reduced acceptor + O2
20:2DELTA11,14 + acceptor + H2O
62% conversion
-
-
?
heptadecyloleic acid + reduced acceptor + O2
C17:2DELTA9,12 + acceptor + H2O
-
-
-
?
myristoleic acid + reduced acceptor + O2
C14:2DELTA9,12 + acceptor + H2O
-
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
pentadecyloleic acid + reduced acceptor + O2
C15:2DELTA9,12 + acceptor + H2O + acceptor
-
-
-
?
(10Z)-nonadec-10-enoic acid + reduced acceptor + O2
(10Z,13Z)-nonadeca-10,13-dienoic acid + acceptor + H2O
-
-
-
-
?
(10Z)-nonadec-10-enoic acid + reduced acceptor + O2
(10Z,13Z)-nonadeca-10,13-dienoic acid + acceptor + H2O
-
-
-
-
?
(10Z)-nonadec-10-enoic acid + reduced acceptor + O2
(10Z,13Z)-nonadeca-10,13-dienoic acid + acceptor + H2O
-
-
-
-
?
(Z)-9-tetradecenoic acid + ?
tetradec-9,12-dienoic acid
-
biosynthetic pathway for producing the sex pheromone component (Z,E)-9,12-tetradecadienyl acetate in moths involves a DELTA12 desaturase
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
5,8,11,14-eicosatetraenoyl-CoA + reduced acceptor + O2
5,8,11,14,17-eicosadecapentaenoyl-CoA + acceptor + H2O
-
-
-
?
5,8,11,14-eicosatetraenoyl-CoA + reduced acceptor + O2
5,8,11,14,17-eicosadecapentaenoyl-CoA + acceptor + H2O
-
-
-
?
6,9,12-octadecatrienoyl-CoA + reduced acceptor + O2
6,9,12,15-octadecatetraenoyl-CoA + acceptor + H2O
-
-
-
?
6,9,12-octadecatrienoyl-CoA + reduced acceptor + O2
6,9,12,15-octadecatetraenoyl-CoA + acceptor + H2O
-
-
-
?
9,12-octadecadienoyl-CoA + reduced acceptor + O2
9,12,15-octadecatrienoyl-CoA + acceptor + H2O
high activity
-
-
?
9,12-octadecadienoyl-CoA + reduced acceptor + O2
9,12,15-octadecatrienoyl-CoA + acceptor + H2O
high activity
-
-
?
cis-9-hexadecenoic acid + reduced acceptor + O2
cis,cis-9,12-hexadecadienoic acid + acceptor + H2O
-
14.7% desaturation
-
-
?
cis-9-hexadecenoic acid + reduced acceptor + O2
cis,cis-9,12-hexadecadienoic acid + acceptor + H2O
-
70.3% desaturation
-
-
?
cis-9-octadecenoic acid + reduced acceptor + O2
cis,cis-9,12-octadecadienoic acid + acceptor + 2 H2O
-
PtFAD2 is involved in the biosynthesis of eicosapentaenoic acid
-
-
?
cis-9-octadecenoic acid + reduced acceptor + O2
cis,cis-9,12-octadecadienoic acid + acceptor + 2 H2O
-
20.6% desaturation
-
-
?
cis-9-octadecenoic acid + reduced acceptor + O2
cis,cis-9,12-octadecadienoic acid + acceptor + 2 H2O
-
cis-9-octadecenoic acid is the most efficient substrate for PtFAD2, 50.3% desaturation
-
-
?
oleic acid + ?
linoleic acid + ?
-
DELTA12-desaturase mutant shows delayed spore germination, a twofold reduction in growth, a reduced level of conidiation and complete loss of sclerotial development, compared with the wild-type enzyme
-
-
?
oleic acid + ?
linoleic acid + ?
linoleic acid was detectable when expressing Fm2 in DELTA12 desaturase knockout Yarrowia lipolytica
-
-
?
oleic acid + ?
linoleic acid + ?
expression in Saccharomyces cerevisiae leads to endogenous production of linoleic acid
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
best substrate with 72% conversion
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
best substrate with 23% conversion
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
FAD2 introduces a double bond in position DELTA12 in oleic acid (18:1) to form linoleic acid (18:2 n-6)
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
specific substrate
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
specific substrate
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
best substrate with 63.3% conversion
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + alpha-linolenic acid + acceptor + H2O
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + alpha-linolenic acid + acceptor + H2O
-
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + 2 H2O
-
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + 2 H2O
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + 2 H2O
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
octadec-9,11-dienoyl-CoA + acceptor + 2 H2O
-
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
octadec-9,11-dienoyl-CoA + acceptor + 2 H2O
-
the DELTA12 desaturase provides the key step for the cockroach to become nutritionally independent of dietary lipid and to synthesize eicosanoids de novo
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
-
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
43% conversion
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
-
-
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
-
4.1% conversion
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
-
26.7% conversion
-
-
?
stearolic acid + reduced acceptor + O2
trans-12-octadecen-9-ynoic acid + acceptor + H2O
-
4.8% conversion
-
-
?
stearolic acid + reduced acceptor + O2
trans-12-octadecen-9-ynoic acid + acceptor + H2O
-
35% conversion
-
-
?
additional information
?
-
-
oxygen availability alone can regulate de novo DELTA12-desaturase synthesis in Acanthamoeba castellanii and oxygen can limit the activity of preexisting DELTA12-desaturase
-
-
-
additional information
?
-
-
the main transition in fatty acid metabolism of Acanthamoeba castellanii during batch growth appears to be primarily related to a rapid decline in DELTA12-desaturase activity after 24 h. The resultant large growth-dependent changes in the degree of fatty acid unsaturation would be expected to affect the physical state and/or fluidity of membranes, and may be related to many of the distinctive physiological and biochemical characteristics displayed by Acanthamoeba castellanii in different stages of batch growth
-
-
-
additional information
?
-
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a processive bifunctional oleoyl-DELTA12/linoleoyl-DELTA3 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a processive bifunctional oleoyl-DELTA12/linoleoyl-DELTA3 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a processive bifunctional oleoyl-DELTA12/linoleoyl-DELTA3 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a strictly monofunctional oleoyl-DELTA12 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a strictly monofunctional oleoyl-DELTA12 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a strictly monofunctional oleoyl-DELTA12 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a processive bifunctional oleoyl-DELTA12/linoleoyl-DELTA3 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a processive bifunctional oleoyl-DELTA12/linoleoyl-DELTA3 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a strictly monofunctional oleoyl-DELTA12 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
one of two membrane-bound fatty acid desaturases occurring in Aspergillus nidulans, a strictly monofunctional oleoyl-DELTA12 desaturase, substrate specificity of the recombinant enzyme, overview
-
-
-
additional information
?
-
the enzyme can also catalyze DELTA15 desaturation
-
-
-
additional information
?
-
the enzyme is a bifunctional fatty acid desaturase with both high DELTA12 desaturase activity and unusual DELTA15 desaturase activities
-
-
-
additional information
?
-
the enzyme is a bifunctional fatty acid desaturase with both high DELTA12 desaturase activity and unusual DELTA15 desaturase activities
-
-
-
additional information
?
-
the enzyme is a bifunctional fatty acid desaturase with both high DELTA12 desaturase activity and unusual DELTA15 desaturase activities
-
-
-
additional information
?
-
-
the DELTA12-desaturase enzymatic complex shows a preference towards oleoyl-CoA versus elaidoyl-CoA. Study of substrate specificity of the DELTA12 desaturase system is difficult due to the involvement of numerous enzymes. At least two activities are involved: in a first step, acyl CoA synthetase catalyzes the formation of oleoyl-CoA from olic acid and CoA, then oleoyl-CoA is desaturated into linoleoyl-CoA. No desaturation occurs when CoA is absent in the reaction medium
-
-
-
additional information
?
-
-
the DELTA12-desaturase enzymatic complex shows a preference towards oleoyl-CoA versus elaidoyl-CoA. Study of substrate specificity of the DELTA12 desaturase system is difficult due to the involvement of numerous enzymes. At least two activities are involved: in a first step, acyl CoA synthetase catalyzes the formation of oleoyl-CoA from olic acid and CoA, then oleoyl-CoA is desaturated into linoleoyl-CoA. No desaturation occurs when CoA is absent in the reaction medium
-
-
-
additional information
?
-
-
PtFAD6 is involved in the biosynthesis of hexadecantrienic acid
-
-
-
additional information
?
-
-
no activity with cis-13-docosenoic acid
-
-
-
additional information
?
-
-
synergistic effect of high-light and low temperature on cell growth of the DELTA12 fatty acid desaturase mutant
-
-
-
additional information
?
-
-
no activity with myristoleic acid palmitoleic acid, heptadecenoic acid, elaidic acid, linolenic acid, dihomo-gamma-linolenic acid, arachidonic acid, or docosatetraenoic acid
-
-
-
additional information
?
-
-
the enzyme has dual specificities of a DELTA12-fatty acid desaturase and a v+3-fatty acid desaturase
-
-
-
additional information
?
-
-
no activity with myristoleic acid palmitoleic acid, heptadecenoic acid, elaidic acid, linolenic acid, dihomo-gamma-linolenic acid, arachidonic acid, or docosatetraenoic acid
-
-
-
additional information
?
-
-
the enzyme has dual specificities of a DELTA12-fatty acid desaturase and a v+3-fatty acid desaturase
-
-
-
additional information
?
-
-
no activity with myristoleic acid palmitoleic acid, heptadecenoic acid, elaidic acid, linolenic acid, dihomo-gamma-linolenic acid, arachidonic acid, or docosatetraenoic acid
-
-
-
additional information
?
-
-
the enzyme has dual specificities of a DELTA12-fatty acid desaturase and a v+3-fatty acid desaturase
-
-
-
additional information
?
-
gene Ssd12 encodes a DELTA12-FAD, which can convert 16:1 and 18:1 into 16:2 and 18:2 fatty acids, substrate specificity, overview
-
-
-
additional information
?
-
-
gene Ssd12 encodes a DELTA12-FAD, which can convert 16:1 and 18:1 into 16:2 and 18:2 fatty acids, substrate specificity, overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(Z)-9-tetradecenoic acid + ?
tetradec-9,12-dienoic acid
-
biosynthetic pathway for producing the sex pheromone component (Z,E)-9,12-tetradecadienyl acetate in moths involves a DELTA12 desaturase
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
cis-9-octadecenoic acid + reduced acceptor + O2
cis,cis-9,12-octadecadienoic acid + acceptor + 2 H2O
-
PtFAD2 is involved in the biosynthesis of eicosapentaenoic acid
-
-
?
eicosenoic acid + reduced acceptor + O2
20:2DELTA11,14 + acceptor + H2O
A0A088MFF4
62% conversion
-
-
?
oleoyl-CoA + reduced acceptor + O2
octadec-9,11-dienoyl-CoA + acceptor + 2 H2O
-
the DELTA12 desaturase provides the key step for the cockroach to become nutritionally independent of dietary lipid and to synthesize eicosanoids de novo
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
P20388
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
P20388
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
DELTA12-desaturase mutant shows delayed spore germination, a twofold reduction in growth, a reduced level of conidiation and complete loss of sclerotial development, compared with the wild-type enzyme
-
-
?
oleic acid + ?
linoleic acid + ?
Q27ZJ7
linoleic acid was detectable when expressing Fm2 in DELTA12 desaturase knockout Yarrowia lipolytica
-
-
?
oleic acid + ?
linoleic acid + ?
Q65YX3
expression in Saccharomyces cerevisiae leads to endogenous production of linoleic acid
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
A0A088MFF4
best substrate with 72% conversion
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
best substrate with 23% conversion
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
specific substrate
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
specific substrate
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
best substrate with 63.3% conversion
-
-
?
oleoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + 2 H2O
-
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + 2 H2O
Q5AWX6, Q5BEJ3
-
-
-
?
oleoyl-CoA + reduced acceptor + O2
9,12-octadecadienoyl-CoA + acceptor + 2 H2O
Q5AWX6, Q5BEJ3
-
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
A0A088MFF4
43% conversion
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
-
4.1% conversion
-
-
?
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
-
26.7% conversion
-
-
?
stearolic acid + reduced acceptor + O2
trans-12-octadecen-9-ynoic acid + acceptor + H2O
-
4.8% conversion
-
-
?
stearolic acid + reduced acceptor + O2
trans-12-octadecen-9-ynoic acid + acceptor + H2O
-
35% conversion
-
-
?
additional information
?
-
-
oxygen availability alone can regulate de novo DELTA12-desaturase synthesis in Acanthamoeba castellanii and oxygen can limit the activity of preexisting DELTA12-desaturase
-
-
-
additional information
?
-
-
the main transition in fatty acid metabolism of Acanthamoeba castellanii during batch growth appears to be primarily related to a rapid decline in DELTA12-desaturase activity after 24 h. The resultant large growth-dependent changes in the degree of fatty acid unsaturation would be expected to affect the physical state and/or fluidity of membranes, and may be related to many of the distinctive physiological and biochemical characteristics displayed by Acanthamoeba castellanii in different stages of batch growth
-
-
-
additional information
?
-
-
PtFAD6 is involved in the biosynthesis of hexadecantrienic acid
-
-
-
additional information
?
-
-
synergistic effect of high-light and low temperature on cell growth of the DELTA12 fatty acid desaturase mutant
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethyl-5-phenylisoxazolium 3'-sulfonate
-
DELTA12-desaturase system, enzymatic complex
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the proportion of linoleic acid in the total fatty acids produced by transformed Saccharomyces cerevisiae increases from 1.1 mol% when grown at 30°C to 2.9 mol% when grown at 15°C
additional information
the proportion of linoleic acid in the total fatty acids produced by transformed Saccharomyces cerevisiae increases from 1.1 mol% when grown at 30°C to 2.9 mol% when grown at 15°C
additional information
optimal condition for expressing DELTA12-fatty acid desaturase in Saccharomyces cerevisiae is 3% galactose induction for 24 h at 15°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
4.2fold increase in mRNA level in mature fruiting bodies compared to mycelium
3.5fold increase in mRNA level in fruiting body primordia and 4.2fold increase in mRNA level in mature fruiting bodies compared to mycelium
3.5fold increase in mRNA level in fruiting body primordia compared to mycelium
additional information
composition of major fatty acids in Sapium sebiferum seeds, overview
additional information
expression of FAD6 increases fourfold at 4°C compared to expression at 25°C; expression of FAD6 increases fourfold at 4°C compared to expression at 25°C
additional information
expression of FAD6 increases fourfold at 4°C compared to expression at 25°C; expression of FAD6 increases fourfold at 4°C compared to expression at 25°C
additional information
-
expression of FAD6 increases fourfold at 4°C compared to expression at 25°C; expression of FAD6 increases fourfold at 4°C compared to expression at 25°C
-
additional information
-
high expression level in bolls between 12 and 16 days after anthesis
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
endomembrane network-like distribution around chloroplasts
-
greatest in microsomal membranes isolated from early-exponential to mid-exponential phase cells, declines by approximately 50% as cultures progress towards stationary phase
-
-
enzyme activity is increased by up to 10fold during aeration of cultures
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40500
-
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE
43000
66000
-
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE; x * 66000, DesA As hybrid with lichenase LicBM3, SDS-PAGE
43000
SDS-PAGE of cell membranes of transformed Escherichia coli
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE; x * 66000, DesA As hybrid with lichenase LicBM3, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
soluble recombinant enzyme from Escherichia coli strains JM109 and BL21(DE3)
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, high level expression in Escherichia coli strains JM109 and BL21(DE3)
-
expressed in Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum cells; gene desA, recombinant expression of the desA-licBM3 hybrid in transgenic Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum plants
-
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae and in Arabidopsis thaliana
expressed in Saccharomyces cerevisiae and in the Arabidopsis thaliana fad2-1 mutant (knockout mutants lacking the single FAD2 gene)
expressed in Saccharomyces cerevisiae EH1315, 7.9% oleic acid and 29% linoleic acid in yeast expressing DELTA12 desaturase compared with 37% oleic acid and no detectable linoleic acid in control yeast, fatty acid composition analyzed by gas-liquid chromatography; gene Cop-odeA, DNA and amino acid sequence determination and analysis, functional expression in Saccharomyces cerevisiae strain EH1315
expressed in Saccharomyces cerevisiae INVSc1 cells and Aurantiochytrium limacinum mh0186 cells
-
expressed in Saccharomyces cerevisiae INVScI and Pichia pastoris GS115 cells
-
expressed in wild-type Yarrowia lipolytica and its DELTA12 desaturase knockout mutant, 62.6 weight percent of total fatty acid was linoleic acid produced in the mutant
expression in Saccharomyces cerevisiae leads to endogenous production of linoleic acid, the proportion of linoleic acid in the total fatty acids produced by transformed Saccharomyces cerevisiae increases from 1.1 mol% when grown at 30°C to 2.9 mol% when grown at 15°C
expression in Saccharomyces cerevisiae strain YHU3046-4A results in endogenous production of linoleic acid, increasement in production of linoleic acid from 0.66 to 1.19 microg/mg dry cell weight when 0.5 microM oleic acid as a substrate was exogenously added
-
expression of DELTA12-fatty acid desaturase genes in Escherichia coli strain BL21 and Saccharomyces cerevisiae strain IN-VSc1 leads to production of an active enzyme which converts 17.876% and 17.604% of oleic acid to linoleic acid, GC-MS detection in vitro and in vivo
functional expression of a DELTA12 fatty acid desaturase gene from Spinacia oleracea in transgenic Sus scrofa. Levels of linoleic acid (18:2n-6) in adipocytes that have differentiated in vitro from cells derived from the transgenic pigs are about 10times higher than those from wild-type pigs. In addition, the white adipose tissue of transgenic pigs contained about 20% more linoleic acid (18:2n-6) than that of wild-type pigs
gene An1, DNA and amino acid sequence determination and analysis, functional expression in Arabidopsis thaliana; gene An2, DNA and amino acid sequence determination and analysis, functional expression in Arabidopsis thaliana
gene Cs-fad2, DNA and amino acid sequence determination and analysis, transcriptional analysis, and functional expression in and complementation of enzyme-deficient Saccharomyces cerevisiae S288C mutant strain NBRC1136
gene FAD6, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Saccharomyces cerevisiae strain INVSc1, expression analysis; gene FAD6, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Saccharomyces cerevisiae strain INVSc1, expression analysis
gene Pc-fad2, DNA and amino acid sequence determination and analysis
gene Ssd12, DNA and amino acid sequence determination and analysis, two genomic copies, expression in Saccharomyces cerevisiae
heterologous expression in Saccharomyces cerevisiae and Aspergillus oryzae
heterologous expression in yeast Saccharomyces cerevisiae and Synechococcus
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of FAD6 increases fourfold at 4°C compared to expression at 25°C. FAD6 transcription is sensitive to saline stress with a 20fold increase at 6% NaCl; expression of FAD6 increases fourfold at 4°C compared to expression at 25°C. FAD6 transcription is sensitive to saline stress with a 20fold increase at 6% NaCl
FAD2 mRNA accumulates in leaf mesophyll cells and in root epidermis cells when exposed to 15°C for 4 days in dark conditions
induction of FAD2 expression following a 24 h incubation at 10°C is light dependent, no difference in FAD2 expression is found in plants grown between 32°C and 20°C
mRNA accumulation shows a periodic behaviour, decreasing to the 22°C levels following a 48 h incubation and re-establishing ist 24 h induction after 96 h
no enhancement of enzyme transcript is observed when cells are incubated in the dark at 22°C
shifting of the Mucor rouxii culture from anaerobic to aerobic conditions upregulates levels of expressions of the DELTA9-, DELTA12- and DELTA6-desaturases genes, overview. The transcriptional response is rapid and transient, with the maximal mRNA levels between 0.5 h and 1.0 h after the shift
-
the induction of FAD2 is inhibited by incubation at 10°C under dark conditions but appears unaffected by light intensity
the level of the enzyme transcript increases 10fold within 1 h upon a decrease in temperature from 36°C to 22°C
expression of FAD6 increases fourfold at 4°C compared to expression at 25°C. FAD6 transcription is sensitive to saline stress with a 20fold increase at 6% NaCl; expression of FAD6 increases fourfold at 4°C compared to expression at 25°C. FAD6 transcription is sensitive to saline stress with a 20fold increase at 6% NaCl
expression of FAD6 increases fourfold at 4°C compared to expression at 25°C. FAD6 transcription is sensitive to saline stress with a 20fold increase at 6% NaCl; expression of FAD6 increases fourfold at 4°C compared to expression at 25°C. FAD6 transcription is sensitive to saline stress with a 20fold increase at 6% NaCl
-
-
no enhancement of enzyme transcript is observed when cells are incubated in the dark at 22°C
-
no enhancement of enzyme transcript is observed when cells are incubated in the dark at 22°C
-
-
the level of the enzyme transcript increases 10fold within 1 h upon a decrease in temperature from 36°C to 22°C
-
the level of the enzyme transcript increases 10fold within 1 h upon a decrease in temperature from 36°C to 22°C
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the seed oil fatty acid composition of Arabidopsis plants expressing An1 is altered, overview
additional information
the seed oil fatty acid composition of Arabidopsis plants expressing An1 is altered, overview
additional information
the seed oil fatty acid composition of Arabidopsis plants expressing An1 is altered, overview
additional information
-
the seed oil fatty acid composition of Arabidopsis plants expressing An1 is altered, overview
-
additional information
a recombinant Saccharomyces cerevisiae strain EH1315 expressing gene Cop-odeA accumulates four additional fatty acids identified as 9,12-hexadecadienoic acid, 9,12,15-hexadecatrienoic acid, linoleic acid, and alinolenic acid, which comprised 8.8%, 1.0%, 29.0%, and 0.6% of the total fatty acids, respectively, overview
additional information
-
a recombinant Saccharomyces cerevisiae strain EH1315 expressing gene Cop-odeA accumulates four additional fatty acids identified as 9,12-hexadecadienoic acid, 9,12,15-hexadecatrienoic acid, linoleic acid, and alinolenic acid, which comprised 8.8%, 1.0%, 29.0%, and 0.6% of the total fatty acids, respectively, overview
-
additional information
-
a recombinant Saccharomyces cerevisiae strain EH1315 expressing gene Cop-odeA accumulates four additional fatty acids identified as 9,12-hexadecadienoic acid, 9,12,15-hexadecatrienoic acid, linoleic acid, and alinolenic acid, which comprised 8.8%, 1.0%, 29.0%, and 0.6% of the total fatty acids, respectively, overview
-
additional information
-
a transgenic Saccharomyces cerevisiae strain BYdesa, expressing the enzyme from Helvea brasiliensis, produces up to 15% polyunsaturated fatty acids, mostly 9Z,12Z-C18:2, linoleic acid, but also 9Z,12Z-C16:2 fatty acid under inducing conditions, production of 4-hydroxy-2-nonenal, one of the major end products of n-6 polyunsaturated fatty acid peroxidation. Desaturase expression causes adaptation to oxidative stress but not to hyperosmotic stress, phenotype, overview
additional information
the DELTA12 desaturase-defective mutant, Mut48, derived from Mortierella alpina 1S-4 produces several fatty acids of the n-9 family such as 6,9-octadecadienoic acid (18:2n-9), 8,11-eicosadienoic acid (20:2n-9), and mead acid. The mutants SR88 and TM912 exhibit a complete DELTA12 desaturation deficiency with no arachidonic acid accumulation
additional information
-
construction of a hybrid of desA and reporter gene encoding thermostable lichenase, licBM3. The desaturase can enhance tolerance to cold stress in potato, and desaturase and lichenase retain their functionality in the structure of the hybrid protein where the enzymatic activity of target gene product is higher than in the case of reporter lichenase gene absence in the construction, phenotypes, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
after functional expression of a DELTA12 fatty acid desaturase gene from Spinacia oleracea in transgenic Sus scrofa levels of linoleic acid (18:2n-6) in adipocytes that have differentiated in vitro from cells derived from the transgenic pigs are about 10 times higher than those from wild-type pigs. In addition, the white adipose tissue of transgenic pigs contained about 20% more linoleic acid (18:2n-6) than that of wild-type pigs. These results demonstrate the functional expression of a plant gene for a fatty acid desaturase in mammals, opening up the possibility of modifying the fatty acid composition of products from domestic animals by transgenic technology, using plant genes for fatty acid desaturases
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.6)
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