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

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The enzyme appears in viruses and cellular organisms

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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
additional information
?
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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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
NADPH
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pH 6.8, 37°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
of stem and leaf
Manually annotated by BRENDA team
and skin, tissues with highest expression
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
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
after heterologous expression in yeast
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 56000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable during storage, but sensitive to repeated freezing and thawing
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression using baculoviral system; expression using baculoviral system
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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