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(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
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
-
-
-
?
oleic acid + ?
linoleic acid + ?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
oleic acid + reduced acceptor + O2
linoleic acid + alpha-linolenic acid + acceptor + H2O
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
oleoyl-CoA + 2 reduced acceptor + O2 + 2 H+
linoleoyl-CoA + 2 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
palmitoleic acid + reduced acceptor + O2
(9Z,12Z)-hexadeca-9,12-dienoic acid + acceptor + H2O
palmitoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
pentadecyloleic acid + reduced acceptor + O2
C15:2DELTA9,12 + acceptor + H2O + acceptor
-
-
-
?
stearolic acid + reduced acceptor + O2
trans-12-octadecen-9-ynoic acid + acceptor + H2O
additional information
?
-
(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
-
-
-
-
?
(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
-
-
-
-
?
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 + ?
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
?
oleic acid + ?
linoleic acid + ?
linoleic acid was detectable when expressing Fm2 in DELTA12 desaturase knockout Yarrowia lipolytica
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
-
?
oleic acid + ?
linoleic acid + ?
expression in Saccharomyces cerevisiae leads to endogenous production of linoleic acid
-
-
?
oleic acid + ?
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
-
-
-
?
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 + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
oleoyl-CoA + 2 reduced acceptor + O2 + 2 H+
linoleoyl-CoA + 2 acceptor + 2 H2O
-
-
-
?
oleoyl-CoA + 2 reduced acceptor + O2 + 2 H+
linoleoyl-CoA + 2 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
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
?
-
recombinantly expressed enzyme CSFAD2A is a DELTA12 desaturase and has DELTAx+3 activity
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
62% conversion
-
-
?
oleic acid + ?
linoleic acid + ?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
oleoyl-CoA + 2 reduced acceptor + O2 + 2 H+
linoleoyl-CoA + 2 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
-
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
palmitoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
(9Z,12Z)-hexadeca-9,12-dienoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
stearolic acid + reduced acceptor + O2
trans-12-octadecen-9-ynoic acid + acceptor + H2O
additional information
?
-
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
-
-
-
-
?
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 + ?
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
?
oleic acid + ?
linoleic acid + ?
linoleic acid was detectable when expressing Fm2 in DELTA12 desaturase knockout Yarrowia lipolytica
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
-
?
oleic acid + ?
linoleic acid + ?
expression in Saccharomyces cerevisiae leads to endogenous production of linoleic acid
-
-
?
oleic acid + ?
linoleic acid + ?
-
-
-
-
?
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
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 + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
oleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
oleoyl-CoA + 2 reduced acceptor + O2 + 2 H+
linoleoyl-CoA + 2 acceptor + 2 H2O
-
-
-
?
oleoyl-CoA + 2 reduced acceptor + O2 + 2 H+
linoleoyl-CoA + 2 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
9,12-octadecadienoyl-CoA + acceptor + 2 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
-
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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evolution
all members of the CSFAD2 and CSD6 subclasses of microsomal desaturases consist of a single exon. Evolutionary relationship of Cannabis sativa putative desaturases, overview
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
the enzyme belongs to the acyl-CoA desaturase family and possesses a fatty acid desaturase domain
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
fatty acid desaturases, FADs, play an essential role in fatty acid metabolism and the maintenance of biological membranes
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
-
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
recombinant enzyme expression improves potato plant resistance to Phytophthora infestans infection
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 enzyme increases the tolerance to low temperature
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
Cofad2-2 might be one of the key genes to regulate oil quality in Camellia oleifera seeds
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
the FAD2 enzyme is responsible for the DELTA12 desaturation of oleic acid (18:1DELTA9) to linoleic acid (18:2DELTA9,12)
physiological function
-
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
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 belongs to the plastidial D12-FAD with conserved histidine boxes
additional information
the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes
additional information
the enzyme contains three histidine-rich domains and four membrane-spanning domains characteristic for DELTA12-fatty acid desaturases
additional information
hemp seeds contain seven DELTA12 desaturases, FAD2A is the major DELAT12 desaturase in hemp seed
additional information
-
the enzyme belongs to the plastidial D12-FAD with conserved histidine boxes
-
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DNA and amino acid sequence determination and analysis, high level expression in Escherichia coli strains JM109 and BL21(DE3)
-
expressed in Anacystis nidulans strain R2-SPc
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum cells
expressed in Mus musculus strains C57BL/6 and DBA/2
-
expressed in Nicotiana tabacum cultivar Wisconsin
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
expressed in Saccharomyces cerevisiae INVSc1 cells and Aurantiochytrium limacinum mh0186 cells
-
expressed in Saccharomyces cerevisiae INVScI and Pichia pastoris GS115 cells
-
expressed in Saccharomyces cerevisiae strain IFO10150
-
expressed in Saccharomyces cerevisiae strain InvSc1
-
expressed in Solanum lycopersicum cultivar Desnitsa
expressed in Solanum tuberosum cultivar Desnitsa
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
-
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 BYdesa
-
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 Cofad2-2, DNA and amino acid sequence determination and analysis, sequence comparisons
gene Cop-odeA, DNA and amino acid sequence determination and analysis, functional expression in Saccharomyces cerevisiae strain EH1315
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 desA, recombinant expression of the desA-licBM3 hybrid in transgenic Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum plants
gene egFAD2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, quantitative real-time PCR enzyme expression analysis, functional recombinant expression in Saccharomyces cerevisiae strain INVSc1 leading to production of linoleic acids (18:2DELTA9,12), not normally present in wild-type yeast cells, evaluation of fatty acids profiles of the transformed yeast cells by GC/MS analysis, overview
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2A, quantitative RT-PCR enzyme expression analysis, CSFAD2A is cloned into the expression vector pESCTRP containing the galactose-inducible GAL1 promoter, recombinant expression in Saccharomyces cerevisiae
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
-
recombinant expression in Rhodosporidium toruloides with integration into the genome using Agrobacterium tumefaciens strain AGL1, the recombinnat expression leads to increased production of linoleic acid from oleic acid in the tranformed cells, while no significant decrease in the relative contents of the other fatty acids, namely, C14:0 (myristic acid), C16:0 (palmitic acid), and C16:1 (palmitoleic acid) is observed
recombinant expression of His6-tagged enzyme FADS1 in Rhodosporidium toruloides with integration into the genome using Agrobacterium tumefaciens strain AGL1, the recombinnat expression leads to increased production of linoleic acid from oleic acid in the tranformed cells, while no significant decrease in the relative contents of the other fatty acids, namely, C14:0 (myristic acid), C16:0 (palmitic acid), and C16:1 (palmitoleic acid) is observed
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae and in Arabidopsis thaliana
-
expressed in Saccharomyces cerevisiae and in Arabidopsis thaliana
expressed in Solanum tuberosum cultivar Desnitsa
-
expressed in Solanum tuberosum cultivar Desnitsa
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
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Wilson, R.A.; Calvo, A.M.; Chang, P.K.; Keller, N.P.
Characterization of the Aspergillus parasiticus DELTA12-desaturase gene: A role for lipid metabolism in the Aspergillus-seed interaction
Microbiology
150
2881-2888
2004
Aspergillus parasiticus
brenda
Peyou-Ndi, M.M.; Watts, J.L.; Browse, J.
Identification and characterization of an animal DELTA12 fatty acid desaturase gene by heterologous expression in Saccharomyces cerevisiae
Arch. Biochem. Biophys.
376
399-408
2000
Caenorhabditis elegans
brenda
Borgeson, C.E.; De Renobales, M.; Blomquist, G.J.
Characterization of the DELTA12 desaturase in the American cockroach, Periplaneta americana: the nature of the substrate
Biochim. Biophys. Acta
1047
135-140
1990
Periplaneta americana
brenda
Jurenka, R.A.
Biosynthetic pathway for producing the sex pheromone component (Z,E)-9,12-tetradecadienyl acetate in moths involves a DELTA12 desaturase
Cell. Mol. Life Sci.
53
501-505
1997
Cadra cautella
brenda
Sakuradani, E.; Kobayashi, M.; Ashikari, T.; Shimizu, S.
Identification of DELTA12-fatty acid desaturase from arachidonic acid-producing Mortierella fungus by heterologous expression in the yeast Saccharomyces cerevisiae and the fungus Aspergillus oryzae
Eur. J. Biochem.
261
812-820
1999
Mortierella alpina (Q9Y8H5), Mortierella alpina 1S-4 (Q9Y8H5)
brenda
Borgeson, C.E.; Blomquist, G.J.
Subcellular location of the DELTA12-desaturase rules out bacteriocyte contribution to linoleate biosynthesis in the house cricket and the American cockroach
Insect Biochem. Mol. Biol.
23
297-302
1993
Periplaneta americana, Acheta domesticus
-
brenda
Avery, S.V.; Lloyd, D.; Harwood, J.L.
Changes in membrane fatty acid composition and DELTA12-desaturase activity during growth of Acanthamoeba castellanii in batch culture
J. Eukaryot. Microbiol.
41
396-401
1994
Acanthamoeba castellanii
-
brenda
Nugier-Chauvin, C.; Fauconnot, L.; Daligault, F.; Patin, H.
Enantioselective oxidation of thiafatty acids by an algal DELTA12-desaturase
J. Mol. Catal. B
11
1007-1012
2001
Chlorella vulgaris
-
brenda
Lomascolo, A.; Dubreucq, E.; Galzy, P.
Study of the DELTA12-desaturase system of Lipomyces starkeyi
Lipids
31
253-259
1996
Lipomyces starkeyi, Lipomyces starkeyi CBS 1807
brenda
Avery, S.V.; Rutter, A.J.; Harwood, J.L.; Lloyd, D.
Oxygen-dependent low-temperature DELTA12 (n6)-desaturase induction and alteration of fatty acid composition in Acanthamoeba castellanii
Microbiology
142
2213-2221
1996
Acanthamoeba castellanii
-
brenda
Sakamoto, T.; Bryant, D.A.
Synergistic effect of high-light and low temperature on cell growth of the DELTA12 fatty acid desaturase mutant in Synechococcus sp. PCC 7002
Photosynth. Res.
72
231-242
2002
Synechococcus sp. PCC 7002
brenda
Galle, A.M.; Oursel, A.; Joseph, M.; Kader, J.C.
Solubilization of membrane bound DELTA12- and DELTA6-fatty acid desaturases from borage seeds
Phytochemistry
45
1587-1590
1997
Borago officinalis
-
brenda
Domergue, F.; Spiekermann, P.; Lerchl, J.; Beckmann, C.; Kilian, O.; Kroth, P.G.; Boland, W.; Zahringer, U.; Heinz, E.
New insight into Phaeodactylum tricornutum fatty acid metabolism. Cloning and functional characterization of plastidial and microsomal DELTA12-fatty acid desaturases
Plant Physiol.
131
1648-1660
2003
Phaeodactylum tricornutum
brenda
Saeki, K.; Matsumoto, K.; Kinoshita, M.; Suzuki, I.; Tasaka, Y.; Kano, K.; Taguchi, Y.; Mikami, K.; Hirabayashi, M.; Kashiwazaki, N.; Hosoi, Y.; Murata, N.; Iritani, A.
Functional expression of a DELTA12 fatty acid desaturase gene from spinach in transgenic pigs
Proc. Natl. Acad. Sci. USA
101
6361-6366
2004
Spinacia oleracea (Q8H943)
brenda
Fofana, B.; Cloutier, S.; Duguid, S.; Ching, J.; Rampitsch, C.
Gene expression of stearoyl-ACP desaturase and delta12 fatty acid desaturase 2 is modulated during seed development of flax (Linum usitatissimum)
Lipids
41
705-712
2006
Linum usitatissimum
brenda
Zhang, S.; Sakuradani, E.; Ito, K.; Shimizu, S.
Identification of a novel bifunctional DELTA12/DELTA15 fatty acid desaturase from a basidiomycete, Coprinus cinereus TD#822-2
FEBS Lett.
581
315-319
2007
Coprinopsis cinerea (A2A1C4), Coprinopsis cinerea TD#822-2 (A2A1C4), Coprinopsis cinerea TD822-2 (A2A1C4)
brenda
Sakai, H.; Kajiwara, S.
Cloning and functional characterization of a DELTA12 fatty acid desaturase gene from the basidiomycete Lentinula edodes
Mol. Genet. Genomics
273
336-341
2005
Lentinula edodes (Q65YX3), Lentinula edodes
brenda
Damude, H.G.; Zhang, H.; Farrall, L.; Ripp, K.G.; Tomb, J.F.; Hollerbach, D.; Yadav, N.S.
Identification of bifunctional delta12/omega3 fatty acid desaturases for improving the ratio of omega3 to omega6 fatty acids in microbes and plants
Proc. Natl. Acad. Sci. USA
103
9446-9451
2006
Fusarium verticillioides (Q27ZJ7)
brenda
Li, M.C.; Li, H.; Wei, D.S.; Xing, L.J.
Cloning and molecular characterization of DELTA12-fatty acid desaturase gene from Mortierella isabellina
World J. Gastroenterol.
12
3373-3379
2006
Umbelopsis isabellina (P59668)
brenda
Kainou, K.; Kamisaka, Y.; Kimura, K.; Uemura, H.
Isolation of DELTA12 and omega3-fatty acid desaturase genes from the yeast Kluyveromyces lactis and their heterologous expression to produce linoleic and alpha-linolenic acids in Saccharomyces cerevisiae
Yeast
23
605-612
2006
Kluyveromyces lactis, Kluyveromyces lactis NK1
brenda
Cipak, A.; Jaganjac, M.; Tehlivets, O.; Kohlwein, S.D.; Zarkovic, N.
Adaptation to oxidative stress induced by polyunsaturated fatty acids in yeast
Biochim. Biophys. Acta
1781
283-287
2008
Hevea brasiliensis
brenda
Niu, B.; Ye, H.; Xu, Y.; Wang, S.; Chen, P.; Peng, S.; Ou, Y.; Tang, L.; Chen, F.
Cloning and characterization of a novel DELTA12-fatty acid desaturase gene from the tree Sapium sebiferum
Biotechnol. Lett.
29
959-964
2007
Triadica sebifera (A5J295), Triadica sebifera
brenda
Hoffmann, M.; Hornung, E.; Busch, S.; Kassner, N.; Ternes, P.; Braus, G.H.; Feussner, I.
A small membrane-peripheral region close to the active center determines regioselectivity of membrane-bound fatty acid desaturases from Aspergillus nidulans
J. Biol. Chem.
282
26666-26674
2007
Aspergillus nidulans (Q5AWX6), Aspergillus nidulans (Q5BEJ3), Aspergillus nidulans, Aspergillus nidulans FGSC A4 (Q5AWX6), Aspergillus nidulans FGSC A4 (Q5BEJ3)
brenda
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