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(Z)-11-hexadecenoyl-CoA + 2 NADPH + 2 H+
(Z)-11-hexadecenal + CoA + 2 NADP+
-
-
-
?
2-methylhexadecanoyl-CoA + 2 NADPH + 2 H+
2-methylhexadecanol + 2 NADP+ + coenzyme A
low activity
-
-
?
2-methyloctadecanoyl-CoA + 2 NADPH + 2 H+
2-methyloctadecanol + 2 NADP+ + coenzyme A
low activity
-
-
?
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + CoA
Marinobacter nauticus
-
-
-
?
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
arachidonoyl-CoA + NADPH
cis-5,8,11,14-eicosatetraenal + NADP+ + CoA
low activity
-
-
?
arachidoyl-CoA + 2 NADPH + 2 H+
arachidol + 2 NADP+ + coenzyme A
low activity
-
-
?
cis-11-hexadecenal + NADPH + H+
cis-11-hexadecenol + NADP+
-
-
-
-
?
decanal + NADPH + H+
decanol + NADP+
-
-
-
-
?
decanoyl-CoA + 2 NADPH + 2 H+
decanol + 2 NADP+ + coenzyme A
low activity
-
-
?
docosanoyl-CoA + 2 NADPH + 2 H+
1-docosanol + CoA + 2 NADP+
docosanoyl-CoA + 2 NADPH + 2 H+
docosanol + CoA + 2 NADP+
-
-
-
-
?
dodecanal + NADPH + H+
dodecanol + NADP+
-
-
-
-
?
eicosanoyl-CoA + 2 NADPH + 2 H+
1-eicosanol + CoA + 2 NADP+
-
-
-
-
?
eicosanoyl-CoA + 2 NADPH + 2 H+
eicosanol + CoA + 2 NADP+
-
-
-
-
?
eicosenoyl-CoA + 2 NADPH + 2 H+
eicosanol + 2 NADP+ + coenzyme A
higher activity
-
-
?
eicosenoyl-CoA + NADPH + H+
eicosenyl alcohol + NADP+
about 50% of the activity with stearoyl-CoA
-
-
?
erucoyl-CoA + NADPH + H+
erucyl alcohol + NADP+
about 30% of the activity with stearoyl-CoA
-
-
?
erucyl-CoA + 2 NADPH + 2 H+
erucyl alcohol + 2 NADP+ + coenzyme A
moderate activity
-
-
?
heneicosanoyl-CoA + 2 NADPH + 2 H+
heneicosanol + CoA + 2 NADP+
-
-
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
1-hexacosanol + CoA + 2 NADP+
hexacosanoyl-CoA + 2 NADPH + 2 H+
hexacosanol + CoA + 2 NADP+
-
-
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
hexacosanoyl alcohol + 2 NADP+ + coenzyme A
-
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
hexacosanoyl alcohol + CoA + 2 NADP+
-
-
-
-
?
hexacosanoyl-CoA + NADPH + H+
hexacosanoyl alcohol + CoA + NADP+
-
-
-
?
hexadecanoyl-CoA + 2 NADPH + 2 H+
1-hexadecanol + CoA + 2 NADP+
hexadecanoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
hexadecenoyl-CoA + 2 NADPH + 2 H+
hexadecenol + CoA + 2 NADP+
-
-
-
?
homo-gamma-linolenoyl-CoA + NADPH
? + NADP+ + CoA
low activity
-
-
?
lauroyl-CoA + 2 NADPH + 2 H+
dodecanal + CoA + 2 NADP+
-
-
-
-
?
lauroyl-CoA + 2 NADPH + 2 H+
dodecanol + 2 NADP+ + coenzyme A
low activity
-
-
?
lauroyl-CoA + 2 NADPH + 2 H+
dodecanol + CoA + 2 NADP+
-
-
-
-
?
linoleoyl-CoA + NADPH
cis-9,12-octadecadienal + NADP+ + CoA
-
-
-
?
myristoyl-CoA + 2 NADPH + 2 H+
myristol + 2 NADP+ + coenzyme A
low activity
-
-
?
nonadecanoyl-CoA + 2 NADPH + 2 H+
nonadecanol + CoA + 2 NADP+
-
-
-
-
?
octacosanoyl-CoA + 2 NADPH + 2 H+
1-octacosanol + CoA + 2 NADP+
octadecanoyl-CoA + 2 NADPH + 2 H+
1-octadecanol + CoA + 2 NADP+
octadecanoyl-CoA + 2 NADPH + 2 H+
octadecanol + CoA + 2 NADP+
-
-
-
-
?
oleoyl-CoA + 2 NADPH + 2 H+
octadecenol + 2 NADP+ + coenzyme A
low activity
-
-
?
oleoyl-CoA + 2 NADPH + 2 H+
octadecenol + CoA + 2 NADP+
oleoyl-CoA + 2 NADPH + 2 H+
oleic alcohol + CoA + 2 NADP+
-
-
-
-
?
oleoyl-CoA + NADPH
cis-9-octadecenal + NADP+ + CoA
-
-
-
?
palmitoleoyl-CoA + 2 NADPH + 2 H+
palmitoleic alcohol + CoA + 2 NADP+
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanal + CoA + 2 NADP+
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
palmitoyl-CoA + NADPH
hexadecanal + NADP+ + CoA
-
-
-
?
pentacosanoyl-CoA + 2 NADPH + 2 H+
pentacosanol + CoA + 2 NADP+
-
-
-
-
?
ricinoleoyl-CoA + 2 NADPH + 2 H+
(9Z,12R)-octadec-9-ene-1,12-diol + 2 NADP+ + coenzyme A
low activity
-
-
?
stearoyl-CoA + 2 NADPH + 2 H+
octadecanal + CoA + 2 NADP+
-
-
-
-
?
stearoyl-CoA + 2 NADPH + 2 H+
octadecanol + 2 NADP+ + coenzyme A
best substrate
-
-
?
stearoyl-CoA + 2 NADPH + 2 H+
octadecanol + CoA + 2 NADP+
-
-
-
-
?
stearoyl-CoA + 2 NADPH + 2 H+
stearyl alcohol + CoA + 2 NADP+
-
-
-
-
?
stearoyl-CoA + NADPH
octadecanal + NADP+ + CoA
-
-
-
?
stearoyl-CoA + NADPH + H+
stearyl alcohol + NADP+
-
-
-
?
tetracosanoyl-CoA + 2 NADPH + 2 H+
1-tetracosanol + CoA + 2 NADP+
tetracosanoyl-CoA + 2 NADPH + 2 H+
tetracosanol + CoA + 2 NADP+
-
-
-
-
?
tetracosanoyl-CoA + 2 NADPH + 2 H+
tetracosanoyl alcohol + 2 NADP+ + coenzyme A
-
-
-
?
tetracosanoyl-CoA + NADPH + H+
tetracosanoyl alcohol + CoA + NADP+
-
-
-
?
tetradecanoyl-CoA + 2 NADPH + 2 H+
tetradecanol + CoA + 2 NADP+
-
-
-
-
?
tetradecenoyl-CoA + 2 NADPH + 2 H+
tetradecenol + CoA + 2 NADP+
-
-
-
?
tricosanoyl-CoA + 2 NADPH + 2 H+
tricosanol + CoA + 2 NADP+
-
-
-
-
?
additional information
?
-
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
-
-
-
?
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
Marinobacter nauticus
-
-
-
?
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
-
-
-
?
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
-
-
-
?
docosanoyl-CoA + 2 NADPH + 2 H+
1-docosanol + CoA + 2 NADP+
-
-
-
?
docosanoyl-CoA + 2 NADPH + 2 H+
1-docosanol + CoA + 2 NADP+
-
-
-
-
?
docosanoyl-CoA + 2 NADPH + 2 H+
1-docosanol + CoA + 2 NADP+
preferred substrate for isoform FAR1
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
1-hexacosanol + CoA + 2 NADP+
-
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
1-hexacosanol + CoA + 2 NADP+
preferred substrate for isoform FAR3
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
1-hexacosanol + CoA + 2 NADP+
-
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
1-hexacosanol + CoA + 2 NADP+
preferred substrate for isoform FAR2
-
-
?
hexacosanoyl-CoA + 2 NADPH + 2 H+
1-hexacosanol + CoA + 2 NADP+
preferred substrate for isoform FAR3
-
-
?
hexadecanoyl-CoA + 2 NADPH + 2 H+
1-hexadecanol + CoA + 2 NADP+
-
-
-
?
hexadecanoyl-CoA + 2 NADPH + 2 H+
1-hexadecanol + CoA + 2 NADP+
preferred substrate for isoform FAR1
-
-
?
hexadecanoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
-
-
-
?
hexadecanoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
-
-
-
-
?
octacosanoyl-CoA + 2 NADPH + 2 H+
1-octacosanol + CoA + 2 NADP+
-
-
-
?
octacosanoyl-CoA + 2 NADPH + 2 H+
1-octacosanol + CoA + 2 NADP+
preferred substrate for isoform FAR6
-
-
?
octadecanoyl-CoA + 2 NADPH + 2 H+
1-octadecanol + CoA + 2 NADP+
-
-
-
?
octadecanoyl-CoA + 2 NADPH + 2 H+
1-octadecanol + CoA + 2 NADP+
preferred substrate for isoform FAR2
-
-
?
oleoyl-CoA + 2 NADPH + 2 H+
octadecenol + CoA + 2 NADP+
-
-
-
-
?
oleoyl-CoA + 2 NADPH + 2 H+
octadecenol + CoA + 2 NADP+
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
lower activity
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
Marinobacter nauticus
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
-
-
-
-
?
tetracosanoyl-CoA + 2 NADPH + 2 H+
1-tetracosanol + CoA + 2 NADP+
-
-
-
?
tetracosanoyl-CoA + 2 NADPH + 2 H+
1-tetracosanol + CoA + 2 NADP+
preferred substrate for isoform FAR4
-
-
?
tetracosanoyl-CoA + 2 NADPH + 2 H+
1-tetracosanol + CoA + 2 NADP+
-
-
-
?
additional information
?
-
Waterproof is a Drosophila FAR with a preference for very long chain, saturated fatty acids of 24 and 26 carbons. In yeast cultures expressing Waterproof, tetracosanoyl-alcohol (24:0-OH) and hexacosanoyl-alcohol (26:0-OH) are identified by GC/MS analysis, unsaturated alcohols or alcohols of shorter chain-lengths are either absent or below the detection limit. Neither of these fatty alcohols is detected in the vector control yeast culture or the wat gene containing culture grown under non-inducing conditions
-
-
?
additional information
?
-
no activity with (Z)-11-octadecenoyl-CoA and (Z)-9-oleoyl-CoA
-
-
-
additional information
?
-
no activity with oleoyl-CoA, linoleoyl-CoA, homo-gamma-linoleoyl-CoA or arachidonoyl-CoA
-
-
?
additional information
?
-
no activity with oleoyl-CoA, linoleoyl-CoA, homo-gamma-linoleoyl-CoA or arachidonoyl-CoA
-
-
?
additional information
?
-
isoform FAR1 prefers C16, C18, C18:1, and C18:2 fatty acids and is less active against other lipids
-
-
?
additional information
?
-
isoform FAR1 prefers C16, C18, C18:1, and C18:2 fatty acids and is less active against other lipids
-
-
?
additional information
?
-
isoform FAR2 prefers saturated C16 and C18 fatty acids
-
-
?
additional information
?
-
isoform FAR2 prefers saturated C16 and C18 fatty acids
-
-
?
additional information
?
-
-
no activity is detected when NADPH is substituted with NADH
-
-
-
additional information
?
-
enzyme substrate specificity, overview. Poor activity with linoleoyl-CoA and linolenoyl-CoA
-
-
?
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additional information
FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. FLAG-Far1 is largely resistant to trypsin digestion and is partially digested upon incubation with a large amount of trypsin
malfunction
in waterproof mutant embryos the formation of the outermost tracheal cuticle sublayer, the envelope is disrupted and the hydrophobic tracheal coating is damaged
malfunction
-
enzyme mutation has significant effects on reducing cutin monomers and internal lipids, and altering the composition of cuticular wax in anthers. Moreover, loss of function of the enzyme significantly affects the expression of its four paralogous genes and five cloned lipid metabolic male-sterility genes in maize
malfunction
-
knockdown of isoforms FAR5, 6, 11 or 15 is lethal and causes a slender body shape, while the old cuticles of the respective animals remain attached to the abdomen or failed to split open from the nota. Knockdown of isoform FAR9 results in a phenotype, with a smooth body surface and a decrease in cuticular hydrocarbon amounts. Knockdown of isoforms FAR1, 4, 5, 6, 8, 9, 11 and 13 additionally results in female adult infertility
metabolism
degradation of Far1 is accelerated by inhibiting dynamin-, Src kinase-, or flotillin-1-mediated endocytosis without increasing the cellular level of plasmalogens. Far1 is stabilized by sequestering cholesterol with nystatin
metabolism
fatty acyl-CoA reductases (FARs) are key enzymes involved in fatty alcohol synthesis
metabolism
isoform FAR1 is involved in the biosynthesis of primary alcohols in the leaf blades of Aegilops tauschii
metabolism
isoform FAR2 is involved in the biosynthesis of primary alcohols in the leaf blades of Aegilops tauschii
metabolism
isoform FAR3 is involved in the biosynthesis of primary alcohols in the leaf blades of Aegilops tauschii
metabolism
isoform FAR4 is involved in the biosynthesis of primary alcohols in the leaf blades of Aegilops tauschii
metabolism
isoform FAR6 is involved in the biosynthesis of primary alcohols in the leaf blades of Aegilops tauschii
physiological function
Arabidopsis cer4 mutants exhibit major decreases in stem primary alcohols and wax esters, and slightly elevated levels of aldehydes, alkanes, secondary alcohols, and ketones. C24, C26, and C28 primary alcohols are reduced to trace amounts in the stem wax of mutant lines. Expression of CER4 cDNA in Saccharomyces cerevisiae results in the accumulation of C24:0 and C26:0 primary alcohols
physiological function
expression of a cDNA in Escherichia coli confers fatty acyl-coenzyme A reductase activity upon those cells and results in the accumulation of fatty alcohols. Upon expression in embryos of Brassica napus, long-chain alcohols can be detected in transmethylated seed oils. In addition to free alcohols, novel wax esters are detected in the transgenic seed oils
physiological function
in a T-DNA-insertion mutant, suberin composition of root and seed coat is reduced in C18:0 primary alcohol, and wounding does not induce an increase in C18:0 primary alcohol. Heterologous expression in yeast confirms that FAR4 is an active alcohol-forming fatty acyl-coenzyme A reductase
physiological function
in a T-DNA-insertion mutant, suberin composition of root and seed coat is reduced in C20:0 primary alcohol, and wounding does not induce an increase in C20:0 primary alcohol. Heterologous expression in yeast confirms that FAR4 is an active alcohol-forming fatty acyl-coenzyme A reductase
physiological function
in a T-DNA-insertion mutant, suberin composition of root and seed coat is reduced in C22:0 primary alcohol, and wounding does not induce an increase in C22:0 primary alcohol. Heterologous expression in yeast confirms that FAR1 is an active alcohol-forming fatty acyl-coenzyme A reductase
physiological function
expression in yeast leads to production of mainly 18:0 and 16:0 alcohols, which account for 57% and 29% of the total fatty alcohol production respectively, while18:1-0H and 20:0-OH are formed in lower quantities
physiological function
expression of FAR1 in Saccharomyces cerevisiae and in the Arabidopsis thaliana cer4-3 mutant leads to production of C22 primary alcohol and C22-C24 primary alcohols, respectively, and expression in Solanum lycopersicum cv MicroTom leaves and fruits results in the accumulation of C26-C30 primary alcohols and C30-C34 primary alcohols, respectively. A nullisomic-tetrasomic wheat line lacking FAR1 has significantly reduced levels of primary alcohols in its leaf blade and anther wax
physiological function
involved in biosynthesis of primary alcohols of leaf blade cuticular wax in wheat. Expression of FAR5 cDNA in Saccharomyces cerevisiae leads to production of C22:0 primary alcohol. Expression in Solanum lycopersicum cv MicroTom leaves results in the accumulation of C26:0, C28:0, and C30:0 primary alcohols
physiological function
fatty acyl-CoA reductases (FARs) are key enzymes involved in fatty alcohol synthesis, fatty alcohols are not only the precursors of sex pheromone components but also the precursors of wax-ester in insects. The two FAR genes, PsFAR I and PsFAR II, show different expression patterns during insect development and after pesticide treatment, suggesting that they play different roles in insect development and detoxification against pesticides
physiological function
peroxisomal fatty acyl-CoA reductase 1 (Far1) is essential for supplying fatty alcohols required for ether bond formation in ether glycerophospholipid synthesis. The stability of Far1 is regulated by a mechanism that is dependent on cellular plasmalogen levels. Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Far1 is a rate-limiting enzyme for plasmalogen synthesis. The transmembrane-flanking region of Far1 is required for its plasmalogen-dependent degradation
physiological function
Waterproof, encoding a fatty acyl-CoA reductase (FAR), is essential for the gas filling of the tracheal tubes during Drosophila embryogenesis, and does not affect branch network formation or key tracheal maturation processes. A non-cell-autonomous waterproof function for the beginning of the tracheal gas filling process, overview. Waterproof plays a key role in tracheal gas filling by providing very long chain fatty alcohols that serve as potential substrates for wax ester synthesis or related hydrophobic substances that ultimately coat the inner lining of the trachea. The hydrophobicity in turn reduces the tensile strength of the liquid inside the trachea, leading to the formation of a gas bubble, the focal point for subsequent gas filling. Enzyme activity is specifically required for the tracheal liquid clearance (LC). Waterproof is essential for outer envelope formation of the tracheal cuticle
physiological function
isoform FAR1 is involved in (Z)-11-hexadecenal production in female prostate gland and male tarsi
physiological function
isoform FAR1 is involved in cuticular wax primary alcohol biosynthesis
physiological function
isoform FAR2 is involved in cuticular wax primary alcohol biosynthesis
physiological function
isoform FAR3 is involved in cuticular wax primary alcohol biosynthesis
physiological function
-
isoform FAR4 is essential for the production of root suberin-associated fatty alcohols, especially under stress conditions
physiological function
-
the enzyme is critical for anther and pollen development in maize
physiological function
-
the enzyme promotes wax ester accumulation in Rhodococcus jostii RHA1
physiological function
-
involved in biosynthesis of primary alcohols of leaf blade cuticular wax in wheat. Expression of FAR5 cDNA in Saccharomyces cerevisiae leads to production of C22:0 primary alcohol. Expression in Solanum lycopersicum cv MicroTom leaves results in the accumulation of C26:0, C28:0, and C30:0 primary alcohols
-
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K156A
Marinobacter nauticus
-
the mutant shows increased activity compared to the wild type enzyme
K527A
Marinobacter nauticus
-
inactive
S126D
Marinobacter nauticus
-
the mutant shows reduced activity compared to the wild type enzyme
S126D/Y152F/K156A
Marinobacter nauticus
-
the mutant shows increased activity compared to the wild type enzyme
S515A
Marinobacter nauticus
-
inactive
Y152F
Marinobacter nauticus
-
the mutant shows about wild type activity
Y532F
Marinobacter nauticus
-
inactive
G101A
-
the activity of the variant is decreased by 62.2% after incubation with short-chain lauroyl-CoA at pH 8.0 and 30°C for 180 min, but 100% activity is lost when using long-chain palmitoyl- and stearoyl-CoAs as the substrate
G104A
-
the activities of the variant are decreased by 56.1%, 65.9%, and 68.3% toward lauroyl-, palmitoyl-, and stearoyl-CoAs, respectively after 180 min incubation, compared with the wild type enzyme
Y327F
-
the activities of the variant drop to 0-6.6% toward lauroyl-, palmitoyl-, and stearoyl-CoAs after 180 min incubation, compared with the wild type enzyme
Y331I
-
the activities of the variant are decreased by 86.2%, 88.3%, and 93.2% toward lauroyl-, palmitoyl-, and stearoyl-CoAs, respectively, compared with the wild type enzyme
additional information
construction of enzyme-defective mutants, phenotypes, overview
additional information
Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Experiments in which regions of Far1 or Far2 are replaced with the corresponding region of the other protein show that the region flanking the transmembrane domain of Far1 is required for plasmalogen-dependent modulation of Far1 stability. Expression of Far1 increased plasmalogen synthesis in wild-type Chinese hamster ovary (CHO) cells. FLAG-tagged truncated enzyme mutants Far1490 and FLAG-Far1467 are localized in the mitochondrion and cytosol, respectively, localization analysis of tagged enzyme mutants, overview. Mutants FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. Expression of FLAG-tagged mutant Far1490-Far2 increases plasmalogen synthesis
additional information
Marinobacter nauticus
de novo fatty alcohol production in Escherichia coli strain AL338 containing plasmidpAL144 or strain AL306, with fadD gene, encoding fatty acyl-CoA synthase, and maqu_2507 gene, method optimization. Biosynthetic pathways of fatty alcohols in genetically engineered Escherichia coli, overview. The amount of fatty alcohols in AL339 is significantly increased to 218.2 mg/l, 9fold higher than that of the control strain AL338. The percentage of medium chain fatty alcohols (12:1, 12:0, 14:1, 14:0, and 16:1) in total fatty alcohols are dramatically increased, especially the C12 and C14 fatty alcohols, accounting for 89% of total fatty alcohols. At the same time, the percentage of C16 and C18 fatty alcohols drops drastically from more than 60% to about 9% and from more than 15% to less than 2%, respectively
additional information
Marinobacter nauticus
de novo fatty alcohol production in Escherichia coli strain AL338 containing plasmidpAL144 or strain AL306, with fadD gene, encoding fatty acyl-CoA synthase, and maqu_2507 gene, method optimization. Biosynthetic pathways of fatty alcohols in genetically engineered Escherichia coli, overview. The amount of fatty alcohols in AL339 is significantly increased to 218.2 mg/l, 9fold higher than that of the control strain AL338. The percentage of medium chain fatty alcohols (12:1, 12:0, 14:1, 14:0, and 16:1) in total fatty alcohols are dramatically increased, especially the C12 and C14 fatty alcohols, accounting for 89% of total fatty alcohols. At the same time, the percentage of C16 and C18 fatty alcohols drops drastically from more than 60% to about 9% and from more than 15% to less than 2%, respectively
additional information
Marinobacter nauticus
de novo fatty alcohol production in Escherichia coli strain AL379 containing plasmidpAL144 or in strain AL307, with fadD gene, encoding fatty acyl-CoA synthase, and maqu_2220 gene, method optimization. Biosynthetic pathways of fatty alcohols in genetically engineered Escherichia coli, composition and amounts of fatty alcohols, overview
additional information
Marinobacter nauticus
de novo fatty alcohol production in Escherichia coli strain AL379 containing plasmidpAL144 or in strain AL307, with fadD gene, encoding fatty acyl-CoA synthase, and maqu_2220 gene, method optimization. Biosynthetic pathways of fatty alcohols in genetically engineered Escherichia coli, composition and amounts of fatty alcohols, overview
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Metz, J.G.; Pollard, M.R.; Anderson, L.; Hayes, T.R.; Lassner, M.W.
Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed
Plant Physiol.
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2000
Simmondsia chinensis (Q9XGY7), Simmondsia chinensis
brenda
Cheng, J.B.; Russell, D.W.
Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions
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Mus musculus (Q7TNT2), Mus musculus (Q922J9), Homo sapiens (Q8WVX9)
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Burdett, K.; Larkins, L.K.; Das, A.K.; Hajra, A.K.
Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells
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Cavia porcellus
brenda
Rowland, O.; Zheng, H.; Hepworth, S.; Lam, P.; Jetter, R.; Kunst, L.
CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved in cuticular wax production in Arabidopsis
Plant Physiol.
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2006
Arabidopsis thaliana (Q93ZB9)
brenda
Domergue, F.; Vishwanath, S.; Joubes, J.; Ono, J.; Lee, J.; Bourdon, M.; Alhattab, R.; Lowe, C.; Pascal, S.; Lessire, R.; Rowland, O.
Three Arabidopsis fatty acyl-coenzyme a reductases, FAR1, FAR4, and FAR5, generate primary fatty alcohols associated with suberin deposition
Plant Physiol.
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2010
Arabidopsis thaliana (Q0WRB0), Arabidopsis thaliana (Q39152), Arabidopsis thaliana (Q9LXN3)
brenda
Wang, Y.; Wang, M.; Sun, Y.; Wang, Y.; Li, T.; Chai, G.; Jiang, W.; Shan, L.; Li, C.; Xiao, E.; Wang, Z.
FAR5, a fatty acyl-coenzyme A reductase, is involved in primary alcohol biosynthesis of the leaf blade cuticular wax in wheat (Triticum aestivum L.)
J. Exp. Bot.
66
1165-1178
2015
Triticum aestivum (Q8L4V2), Triticum aestivum, Triticum aestivum cv Xinong 2718 (Q8L4V2)
brenda
Wang, Y.; Wang, M.; Sun, Y.; Hegebarth, D.; Li, T.; Jetter, R.; Wang, Z.
Molecular characterization of TaFAR1 involved in primary alcohol biosynthesis of cuticular wax in hexaploid wheat
Plant Cell Physiol.
56
1944-1961
2015
Triticum aestivum (A0A0A0R526)
brenda
Miklaszewska, M.; Banas, A.
Biochemical characterization and substrate specificity of jojoba fatty acyl-CoA reductase and jojoba wax synthase
Plant Sci.
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2016
Simmondsia chinensis (Q9XGY7)
brenda
Honsho, M.; Abe, Y.; Fujiki, Y.
Plasmalogen biosynthesis is spatiotemporally regulated by sensing plasmalogens in the inner leaflet of plasma membranes
Sci. Rep.
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43936
2017
Homo sapiens (Q8WVX9)
brenda
Liu, A.; Tan, X.; Yao, L.; Lu, X.
Fatty alcohol production in engineered E. coli expressing Marinobacter fatty acyl-CoA reductases
Appl. Microbiol. Biotechnol.
97
7061-7071
2013
Marinobacter nauticus (A1U2T0), Marinobacter nauticus (A1U3L3)
brenda
Jaspers, M.H.; Pflanz, R.; Riedel, D.; Kawelke, S.; Feussner, I.; Schuh, R.
The fatty acyl-CoA reductase Waterproof mediates airway clearance in Drosophila
Dev. Biol.
385
23-31
2014
Drosophila melanogaster (Q8MS59)
brenda
Honsho, M.; Asaoku, S.; Fukumoto, K.; Fujiki, Y.
Topogenesis and homeostasis of fatty acyl-CoA reductase 1
J. Biol. Chem.
288
34588-34598
2013
Homo sapiens (Q8WVX9)
brenda
Li, X.; Zheng, T.; Zheng, X.; Han, N.; Chen, X.; Zhang, D.
Molecular characterization of two fatty acyl-CoA reductase genes from Phenacoccus solenopsis (Hemiptera Pseudococcidae)
J. Insect Sci.
16
1-7
2016
Phenacoccus solenopsis (A0A193CHN5), Phenacoccus solenopsis (A0A193CHN6), Phenacoccus solenopsis
brenda
Miklaszewska, M.; Banas, A.
Biochemical characterization and substrate specificity of jojoba fatty acyl-CoA reductase and jojoba wax synthase
Plant Sci.
249
84-92
2016
Simmondsia chinensis (Q9XGY7)
brenda
Lanfranconi, M.; Alvarez, H.
Rewiring neutral lipids production for the de novo synthesis of wax esters in Rhodococcus opacus PD630
J. Biotechnol.
260
67-73
2017
Marinobacter nauticus (A1U2T0)
brenda
Round, J.; Roccor, R.; Li, S.N.; Eltis, L.D.
A fatty acyl coenzyme A reductase promotes wax ester accumulation in Rhodococcus jostii RHA1
Appl. Environ. Microbiol.
83
e00902-17
2017
Rhodococcus jostii
brenda
Hu, Y.H.; Chen, X.M.; Yang, P.; Ding, W.F.
Characterization and functional assay of a fatty acyl-CoA reductase gene in the scale insect, Ericerus pela Chavannes (Hemiptera Coccoidae)
Arch. Insect Biochem. Physiol.
97
e21445
2018
Ericerus pela
brenda
Chai, G.; Li, C.; Xu, F.; Li, Y.; Shi, X.; Wang, Y.; Wang, Z.
Three endoplasmic reticulum-associated fatty acyl-coenzyme A reductases were involved in the production of primary alcohols in hexaploid wheat (Triticum aestivum L.)
BMC Plant Biol.
18
41
2018
Triticum aestivum (A0A345D1M5), Triticum aestivum (A0A345YTX7), Triticum aestivum (A0A345YTX8)
brenda
Foo, J.L.; Rasouliha, B.H.; Susanto, A.V.; Leong, S.S.J.; Chang, M.W.
Engineering an alcohol-forming fatty acyl-CoA reductase for aldehyde and hydrocarbon biosynthesis in Saccharomyces cerevisiae
Front. Bioeng. Biotechnol.
8
585935
2020
Marinobacter nauticus
brenda
Hambalko, J.; Gajdos, P.; Nicaud, J.M.; Ledesma-Amaro, R.; Tupec, M.; Pichova, I.; Certik, M.
Production of long chain fatty alcohols found in bumblebee pheromones by Yarrowia lipolytica
Front. Bioeng. Biotechnol.
8
593419
2020
Bombus lucorum, Bombus lapidarius
brenda
Wang, M.; Wu, H.; Xu, J.; Li, C.; Wang, Y.; Wang, Z.
Five fatty acyl-coenzyme A reductases are involved in the biosynthesis of primary alcohols in Aegilops tauschii leaves
Front. Plant Sci.
8
1012
2017
Aegilops tauschii, Aegilops tauschii (A0A0A7NWR9), Aegilops tauschii (A0A0A7NZT1), Aegilops tauschii (A0A140CQH8)
brenda
Dou, X.; Zhang, A.; Jurenka, R.
Functional identification of fatty acyl reductases in female pheromone gland and tarsi of the corn earworm, Helicoverpa zea
Insect Biochem. Mol. Biol.
116
103260
2020
Helicoverpa zea (A0A5Q0TZK6)
brenda
Exner, T.; Romero-Brey, I.; Yifrach, E.; Rivera-Monroy, J.; Schrul, B.; Zouboulis, C.C.; Stremmel, W.; Honsho, M.; Bartenschlager, R.; Zalckvar, E.; Poppelreuther, M.; Fuellekrug, J.
An alternative membrane topology permits lipid droplet localization of peroxisomal fatty acyl-CoA reductase 1
J. Cell Sci.
132
jcs223016
2019
Homo sapiens (Q8WVX9), Homo sapiens
brenda
Zhang, S.; Wu, S.; Niu, C.; Liu, D.; Yan, T.; Tian, Y.; Liu, S.; Xie, K.; Li, Z.; Wang, Y.; Zhao, W.; Dong, Z.; Zhu, T.; Hou, Q.; Ma, B.; An, X.; Li, J.; Wan, X.
ZmMs25 encoding a plastid-localized fatty acyl reductase is critical for anther and pollen development in maize
J. Exp. Bot.
72
4298-4318
2021
Zea mays
brenda
McNeil, B.A.; Stuart, D.T.
Optimization of C16 and C18 fatty alcohol production by an engineered strain of Lipomyces starkeyi
J. Ind. Microbiol. Biotechnol.
45
1-14
2018
Mus musculus
brenda
Li, D.T.; Dai, Y.T.; Chen, X.; Wang, X.Q.; Li, Z.D.; Moussian, B.; Zhang, C.X.
Ten fatty acyl-CoA reductase family genes were essential for the survival of the destructive rice pest, Nilaparvata lugens
Pest Manag. Sci.
76
2304-2315
2020
Nilaparvata lugens
brenda
Wang, Y.; Sun, Y.; You, Q.; Luo, W.; Wang, C.; Zhao, S.; Chai, G.; Li, T.; Shi, X.; Li, C.; Jetter, R.; Wang, Z.
Three fatty acyl-coenzyme A reductases, BdFAR1, BdFAR2 and BdFAR3, are involved in cuticular wax primary alcohol biosynthesis in Brachypodium distachyon
Plant Cell Physiol.
59
527-543
2018
Brachypodium distachyon, Brachypodium distachyon (I1ISS8), Brachypodium distachyon (I1IT05)
brenda
Wang, Y.; Xu, J.; He, Z.; Hu, N.; Luo, W.; Liu, X.; Shi, X.; Liu, T.; Jiang, Q.; An, P.; Liu, L.; Sun, Y.; Jetter, R.; Li, C.; Wang, Z.
BdFAR4, a root-specific fatty acyl-coenzyme A reductase, is involved in fatty alcohol synthesis of root suberin polyester in Brachypodium distachyon
Plant J.
106
1468-1483
2021
Brachypodium distachyon
brenda