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1,2-di-oleoyl-sn-glycero-3-phosphorylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-di-linoleoyl-sn-glycero-3-phosphorylcholine + 2 ferricytochrome b5 + 2 H2O
-
desaturation takes place at both position-1 and position-2. The distearoyl or dielaidoyl phosphatidylcholines are not desaturated
-
-
?
1,2-di-oleoyl-sn-glycero-3-phosphorylcholine + O2 + ?
?
-
-
-
-
?
1,2-dioleoylphosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-linoleoylphosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
1-acyl-2-oleoyl-sn-glycero-3-phosphorylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphorylcholine + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
1-palmitoyl-2-oleoyl phosphatidylcholine + NAD+
1-palmitoyl-2-linoleoyl phosphatidylcholine + NADH
-
-
-
-
?
1-stearoyl-2-oleoyl phosphatidylcholine + NAD+
1-stearoyl-2-linoleoyl phosphatidylcholine + NADH
-
-
-
-
?
oleoyl-phosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-phosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
oleoyl-[CoA] + phosphatidylcholine + O2 + H+
?
-
-
-
-
?
oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
the IgG fraction from ascites fluid inhibits 62% of NADH-dependent cytochrome c reduction in safflower (Carthamus tinctorius L.) microsomes. These antibodies also block desaturation of oleic acid to linoleic acid in lipids of Carthamus tinctorius microsomes by 93%, suggesting that cytochrome b5 is the electron donor for the DELTA12 desaturase
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
oleoyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
linoleoyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
the enzyme inserts a double bond between the carbons 12 and 13 of monounsaturated oleic acid to generate polyunsaturated linoleic acid
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
additional information
?
-
1,2-dioleoylphosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-linoleoylphosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
-
the rate of desaturation of endogenous oleoyl phosphatidylcholine is much greater that of exogenous dioleoyl phosphatidylcholine
-
-
?
1,2-dioleoylphosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-linoleoylphosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
-
the rate of desaturation of endogenous oleoyl phosphatidylcholine is much greater that of exogenous dioleoyl phosphatidylcholine
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
additional information
?
-
-
wild-type enzyme has an inherent, low level of hydroxylation activity
-
-
?
additional information
?
-
-
a desaturase mutant that is unable to convert oleic acid to linoleic acid is impaired in polyunsaturated fatty acid biosynthesis, shows delayed spore germination, a twofold reduction in growth, a reduced level of conidiation and complete loss of eclerotial development, compared to the wild-type
-
-
?
additional information
?
-
-
CeFAT-2 displays characteristics of a bifunctional DELTA12/DELTA15-desaturase and has a great deal of elasticity with respect to fatty acid chain length in being able to desaturate fatty acids ranging from C14 to C18 at the DELTA12 and DELTA15 positions
-
-
?
additional information
?
-
-
yeast cells transformed with the plasmid construct pYES2/FAD2 produce a substantial amount of linoleic acid (18:2) after a period of galactose induction
-
-
?
additional information
?
-
-
yeast cells transformed with the plasmid construct pYES2/FAD2 produced a substantial amount of linoleic acid (18:2) after a period of galactose induction
-
-
?
additional information
?
-
-
esterification of oleate at position 1 and 2
-
-
?
additional information
?
-
-
yeast cells expressing CtFAD2-1 cDNA partially convert oleic fatty acid to linoleic fatty acid
-
-
?
additional information
?
-
-
esterification of oleate at position 1 and 2
-
-
?
additional information
?
-
LKFAD15 is a DELTA12/DELTA15 bifunctional fatty acid desaturase being able to produce linoleic acid and alpha-linolenic acid using oleic acid as substrate and also adjusting the omega-6/omega-3 fatty acids
-
-
?
additional information
?
-
-
recombinant yeast cells can convert oleic acid to linoleic acid
-
-
?
additional information
?
-
-
exogenously added oleic acid is converted to linoleic acid in the gene transformants but not mock transformants of Aurantiochytrium limacinum mh0186 and yeast cells
-
-
?
additional information
?
-
-
exogenously added oleic acid is converted to linoleic acid in the gene transformants but not mock transformants of Aurantiochytrium limacinum mh0186 and yeast cells
-
-
?
additional information
?
-
-
yeasts transformed with the tauDELTA12des converts endogenous oleic acid into linoleic acid
-
-
?
additional information
?
-
-
yeasts transformed with the tauDELTA12des converts endogenous oleic acid into linoleic acid
-
-
?
additional information
?
-
-
yeasts transformed with the tauDELTA12des converts endogenous oleic acid into linoleic acid
-
-
?
additional information
?
-
the enzyme may use a cytochrome b5-like domain in another desaturase as an electron donor
-
-
?
additional information
?
-
-
the enzyme may use a cytochrome b5-like domain in another desaturase as an electron donor
-
-
?
additional information
?
-
-
not: di-oleoyl phosphatidylcholine, dielaidoyl phosphatidylcholine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
oleoyl-[CoA] + phosphatidylcholine + O2 + H+
?
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
oleoyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
linoleoyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
the enzyme inserts a double bond between the carbons 12 and 13 of monounsaturated oleic acid to generate polyunsaturated linoleic acid
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
additional information
?
-
-
a desaturase mutant that is unable to convert oleic acid to linoleic acid is impaired in polyunsaturated fatty acid biosynthesis, shows delayed spore germination, a twofold reduction in growth, a reduced level of conidiation and complete loss of eclerotial development, compared to the wild-type
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
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metabolism
-
the enzyme is involved in providing polyunsaturated phosphatidylcholine to the chloroplast envelope
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)
malfunction
-
combinations of mutations in FAD2-1A and FAD2-1B produce high oleic acid levels in the seed oil
malfunction
-
the disruption of the tauDELTA12des in Thraustochytrium aureum by homologous recombination results in the accumulation of oleic acid and a decrease in the levels of linoleic acid and its downstream polyunsaturated fatty acids. The transformation of the tauDELTA 12des -disruption mutants with a tauDELTA 12des expression cassette restores the wild-type fatty acid profiles
malfunction
-
the PI 283327 FAD2-1B allele, carrying the mutant FAD2-1B P137R allele, is associated with an increase in seed oleic acid content. Although the FAD2-1B mutant alleles alone are not capable of producing a high oleic acid phenotype. When existing FAD2-1A mutations are combined with the novel mutant FAD2-1B alleles, a high oleic acid phenotype is recovered only for those lines which are homozygous for both of the mutant alleles
malfunction
-
transgenic Korean rapeseed Tammi containing high oleic acid contents (78 mol%) are developed via the expression of the BrFAD2-1 gene in an antisense orientation
malfunction
-
transgenic lines expressing an antisense CsFAD2 gene show a high increase in 18:1 content from 13-18% in wild type to 38-51% in transgenic seeds, and concomitantly significant decrease in 18:2 and 18:3 PUFAs. The levels of eicosenoic acid (20:1), another major monounsaturated fatty acid in camelina seed, are also slightly increased in transgenic seeds. These results clearly indicate that CsFAD2 genes encode microsomal oleate desaturases and contribute to PUFA synthesis in camelina seeds
malfunction
-
transgenic lines expressing an antisense CsFAD2 genes show a high increase in 18:1 content from 13-18% in wild type to 38-51% in transgenic seeds, and concomitantly significant decrease in 18:2 and 18:3 PUFAs. The levels of eicosenoic acid (20:1), another major monounsaturated fatty acid in camelina seed, are also slightly increased in transgenic seeds. These results clearly indicate that CsFAD2 genes encode microsomal oleate desaturases and contribute to PUFA synthesis in camelina seeds
malfunction
the increased oleate level in unexpanded leaves due to enzyme-silencing recedes significantly in fully expanded leaves
malfunction
the low protein density in fad2-deficient mitochondrial membranes is mainly responsible for the reduction in proton leak
malfunction
-
the disruption of the tauDELTA12des in Thraustochytrium aureum by homologous recombination results in the accumulation of oleic acid and a decrease in the levels of linoleic acid and its downstream polyunsaturated fatty acids. The transformation of the tauDELTA 12des -disruption mutants with a tauDELTA 12des expression cassette restores the wild-type fatty acid profiles
-
malfunction
-
the disruption of the tauDELTA12des in Thraustochytrium aureum by homologous recombination results in the accumulation of oleic acid and a decrease in the levels of linoleic acid and its downstream polyunsaturated fatty acids. The transformation of the tauDELTA 12des -disruption mutants with a tauDELTA 12des expression cassette restores the wild-type fatty acid profiles
-
physiological function
-
functional recombinant hybird desaturase-lichenase protein can enhance tolerance to cold stress in transgenic potato, overview
physiological function
-
sve1, a mutant allele of the endoplasmic reticulum-localized oleic acid desaturase FAD2 completely suppresses all vte2 low-temperature phenotype, sve1 expressing plant fatty acid composition, overview. The vte1 mutant is deficient in tocopherol cyclase activity and lacks also all tocopherols
physiological function
-
ectopic expression of BrFAD2-1:mRFP complement the Arabidopsis fad2-2 mutant
physiological function
-
heterologous expression of OsFAD2 enhances the yeast cells cold tolerance capacity compared to wild-type yeast. OsFAD2 enhances tolerance to low temperature when overexpressed in rice at the vegetative stage
physiological function
-
when expressed in yeast cells, CeFAT-2 displays characteristics of a bifunctional DELTA12/DELTA15-desaturase and has a great deal of elasticity with respect to fatty acid chain length in being able to desaturate fatty acids ranging from C14 to C18
physiological function
the enzyme is essential for the survival of Arabidopsis at low temperatures
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
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