Information on EC 1.2.1.84 - alcohol-forming fatty acyl-CoA reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.2.1.84
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RECOMMENDED NAME
GeneOntology No.
alcohol-forming fatty acyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain acyl-CoA + 2 NADPH + 2 H+ = a long-chain alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
plasmalogen biosynthesis
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Spodoptera littoralis pheromone biosynthesis
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sporopollenin precursors biosynthesis
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wax esters biosynthesis I
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Cutin, suberine and wax biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
long-chain acyl-CoA:NADPH reductase
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
CAS REGISTRY NUMBER
COMMENTARY hide
37350-23-5
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
in waterproof mutant embryos the formation of the outermost tracheal cuticle sublayer, the envelope is disrupted and the hydrophobic tracheal coating is damaged
metabolism
physiological function
additional information
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methylhexadecanoyl-CoA + 2 NADPH + 2 H+
2-methylhexadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
2-methyloctadecanoyl-CoA + 2 NADPH + 2 H+
2-methyloctadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
arachidonoyl-CoA + NADPH
cis-5,8,11,14-eicosatetraenal + NADP+ + CoA
show the reaction diagram
low activity
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?
arachidoyl-CoA + 2 NADPH + 2 H+
arachidol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
decanoyl-CoA + 2 NADPH + 2 H+
decanol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
eicosenoyl-CoA + 2 NADPH + 2 H+
eicosanol + 2 NADP+ + coenzyme A
show the reaction diagram
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higher activity
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?
eicosenoyl-CoA + NADPH + H+
eicosenyl alcohol + NADP+
show the reaction diagram
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about 50% of the activity with stearoyl-CoA
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?
erucoyl-CoA + NADPH + H+
erucyl alcohol + NADP+
show the reaction diagram
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about 30% of the activity with stearoyl-CoA
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?
erucyl-CoA + 2 NADPH + 2 H+
erucyl alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
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moderate activity
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?
hexacosanoyl-CoA + 2 NADPH + 2 H+
hexacosanoyl alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
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?
homo-gamma-linolenoyl-CoA + NADPH
? + NADP+ + CoA
show the reaction diagram
low activity
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?
lauroyl-CoA + 2 NADPH + 2 H+
dodecanol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
linoleoyl-CoA + NADPH
cis-9,12-octadecadienal + NADP+ + CoA
show the reaction diagram
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?
myristoyl-CoA + 2 NADPH + 2 H+
myristol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
oleoyl-CoA + 2 NADPH + 2 H+
octadecenol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
oleoyl-CoA + NADPH
cis-9-octadecenal + NADP+ + CoA
show the reaction diagram
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?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
palmitoyl-CoA + NADPH
hexadecanal + NADP+ + CoA
show the reaction diagram
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?
ricinoleoyl-CoA + 2 NADPH + 2 H+
(9Z,12R)-octadec-9-ene-1,12-diol + 2 NADP+ + coenzyme A
show the reaction diagram
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low activity
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?
stearoyl-CoA + 2 NADPH + 2 H+
octadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
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best substrate
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?
stearoyl-CoA + NADPH
octadecanal + NADP+ + CoA
show the reaction diagram
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?
stearoyl-CoA + NADPH + H+
stearyl alcohol + NADP+
show the reaction diagram
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?
tetracosanoyl-CoA + 2 NADPH + 2 H+
tetracosanoyl alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
hexacosanoyl-CoA + 2 NADPH + 2 H+
hexacosanoyl alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
Q8MS59
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?
tetracosanoyl-CoA + 2 NADPH + 2 H+
tetracosanoyl alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
Q8MS59
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?
additional information
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Q8MS59
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
NADPH
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pH 6.8, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
reaction with palmitoyl-CoA
7.2
in vivo assay at; in vivo assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
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inactive at pH 4.0, gradual increase up to maximal activity at pH 6.5, 42% of maximal activity at pH 7.5, reduction of activity above
7.5
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42% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
in vivo assay at; in vivo assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
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over 50% of maximal activity within this range, 50% of maximal activity at 25°C
25
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twofold decrease in enzyme activity compared to 40°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
of stem and leaf
Manually annotated by BRENDA team
; and skin, tissues with highest expression; most abundant in
Manually annotated by BRENDA team
gene expression analysis performed at different developmental stages show that the expression of isozyme PsFar I is significantly higher than that of isozyme PsFar II in first and second instar nymphs and in male adults; gene expression analysis performed at different developmental stages show that the expression of isozyme PsFar I is significantly higher than that of isozyme PsFar II in first and second instar nymphs and in male adults
Manually annotated by BRENDA team
tissue with highest mRNA level
Manually annotated by BRENDA team
highest expression in preputial gland, a specialised sebaceous gland
Manually annotated by BRENDA team
; and eyelid, tissues with highest expression; most abundant in
Manually annotated by BRENDA team
; most abundant in
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme possesses 2 transmembrane domains, amino acid sites 20-42 and 499-521; the enzyme possesses 2 transmembrane domains, amino acid sites 340-358 and 496-504
Manually annotated by BRENDA team
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Far1 is a tail-anchored type II peroxisomal membrane protein. The transmembrane segment of Far1 is located in its C-terminus region (amino acids 466-483). The hydrophobic C-terminus of Far1 binds to Pex19p, a cytosolic receptor harboring a C-terminal CAAX motif, which is responsible for the targeting of Far1 to peroxisomes. The C-terminus of Far1 is exposed to the peroxisome matrix, whereas a large catalytic domain in its N-terminus is located outside of peroxisomes
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
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gel filtration
56000
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1 * 56000, SDS-PAGE
58400
x * 58400, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 56000, SDS-PAGE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable during storage, but sensitive to repeated freezing and thawing
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by microsomal membrane preparation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in HEK 293 cells
expression in HEK 293 cells; expression using baculoviral system; expression using baculoviral system
gene FAR, recombinant expression in Saccharomyces cerevisiae wild-type strain BY4742 and in quadruple mutant strain H1246 lacking genes involved in triacylglycerolsand sterol esters synthesis
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gene far, recombinant expression of EGFP-tagged or FLAG-tagged wild-type and diverse truncation mutants of FAR in CHO-K1 cells, construction and expresion of several chimeric FAR1-FAR2 constructs in CHO-K1 cells, overview. Recombinant expression of N- and C-terminally HA-tagged Far1 in CHO-K1 and ZPEG251 cells
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gene maqu_2220, recombinant expression in Escherichia coli leading to fatty alcohol production, coexpression with gene fadD in Escherichia coli strain BL21DELTAfadE; gene maqu_2507, recombinant expression in Escherichia coli leading to fatty alcohol production, coexpression with gene fadD in Escherichia coli strain BL21DELTAfadE
gene PsFAR I, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, quantitative real-time PCR enzyme expression analysis; gene PsFAR II, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, quantitative real-time PCR enzyme expression analysis
gene wat, recombinant expression in Saccharomyces cerevisiae strain H1246, recombinant expression of the enzyme and the peroxisomal marker mRFP-SKL in Drosophila S2 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abrogation of the asymmetric distribution of plasmalogens in the plasma membrane by reducing the expression of CDC50A encoding a beta-subunit of flippase elevates the expression level of Far1 and plasmalogen synthesis without reducing the total cellular level of plasmalogens
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expression is induced by drought and cold stress in an abscisic acid-dependent manner
expression is induced by wounding and salt stress, wounding results in increase in basal levels of C18:0-C22:0 primary alcohols; expression is induced by wounding and salt stress, wounding results in increase in basal levels of C18:0-C22:0 primary alcohols; expression is induced by wounding and salt stress, wounding results in increase in basal levles of C18:0-C22:0 primary alcohols
expression is upregulated in response to drought, cold, and abscisic acid
spirotetramat treatment at 125 mg/liter has no effect on the expression of PsFar II
spirotetramat treatment at 125 mg/liter significantly increases the expression of PsFar I in third instar nymphs
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
FAR genes may be potential targets for pest control; FAR genes may be potential targets for pest control
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