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IUBMB Comments The enzyme has been characterized from the photosynthetic flagellate Euglena gracilis . The alcohol is formed by a four-electron reduction of fatty acyl-CoA by NADH. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. cf . EC 1.2.1.84 , alcohol-forming fatty acyl-CoA reductase (NADPH).
Synonyms FAR , long-chain acyl-CoA:NADH reductase,
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aldehyde-generating fatty acyl-CoA reductase
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long-chain acyl-CoA:NADH reductase
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FAR
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a long-chain acyl-CoA + 2 NADH + 2 H+ = a long-chain alcohol + 2 NAD+ + CoA
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NADH:long-chain acyl-CoA reductase
The enzyme has been characterized from the photosynthetic flagellate Euglena gracilis. The alcohol is formed by a four-electron reduction of fatty acyl-CoA by NADH. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. cf. EC 1.2.1.84, alcohol-forming fatty acyl-CoA reductase (NADPH).
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fatty acyl-CoA + 2 NADH + 2 H+
fatty alcohol + 2 NAD+ + CoA
myristoyl-CoA + 2 NAD(P)H + 2 H+
myristyl alcohol + 2 NAD(P)+ + CoA
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Substrates: preferred substrate
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palmitaldehyde + NADH + H+
palmityl alcohol + NAD+
palmitoyl-CoA + 2 NAD(P)H + 2 H+
palmityl alcohol + 2 NAD(P)+ + CoA
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Substrates: -
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palmitoyl-CoA + NADH + H+
palmitaldehyde + NAD+ + CoA
additional information
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fatty acyl-CoA + 2 NADH + 2 H+
fatty alcohol + 2 NAD+ + CoA
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Substrates: the enzyme converts fatty acyl-CoA to fatty alcohol in a two-step reduction involving aldehyde as intermediate
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fatty acyl-CoA + 2 NADH + 2 H+
fatty alcohol + 2 NAD+ + CoA
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Substrates: the enzyme converts fatty acyl-CoA to fatty alcohol in a two-step reduction involving aldehyde as intermediate
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palmitaldehyde + NADH + H+
palmityl alcohol + NAD+
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Substrates: -
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palmitaldehyde + NADH + H+
palmityl alcohol + NAD+
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Substrates: -
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palmitaldehyde + NADH + H+
palmityl alcohol + NAD+
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Substrates: -
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palmitoyl-CoA + NADH + H+
palmitaldehyde + NAD+ + CoA
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Substrates: -
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palmitoyl-CoA + NADH + H+
palmitaldehyde + NAD+ + CoA
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Substrates: -
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palmitoyl-CoA + NADH + H+
palmitaldehyde + NAD+ + CoA
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Substrates: -
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additional information
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Substrates: no activity with NADPH
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additional information
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Substrates: no activity with other saturated (10:0, 12:0 and 18:0) or unsaturated fatty acids (16:1n-9, 18:1n-9 and 18:2n-6)
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fatty acyl-CoA + 2 NADH + 2 H+
fatty alcohol + 2 NAD+ + CoA
fatty acyl-CoA + 2 NADH + 2 H+
fatty alcohol + 2 NAD+ + CoA
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Substrates: the enzyme converts fatty acyl-CoA to fatty alcohol in a two-step reduction involving aldehyde as intermediate
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fatty acyl-CoA + 2 NADH + 2 H+
fatty alcohol + 2 NAD+ + CoA
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Substrates: the enzyme converts fatty acyl-CoA to fatty alcohol in a two-step reduction involving aldehyde as intermediate
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ATP
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NADH
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the enzyme is specific for NADH
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Mg2+
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5 mM used in assay conditions
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6 - 7
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the enzyme is active at pH 6.0-7.0. There is very little reduction of fatty acids up to pH 5.5 beyond which there is sharp increase in activity. The enzyme activity sharply declines as the pH is raised from 7.0 to 9.0
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Highest Expressing Human Cell Lines
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physiological function
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the enzyme is probably involved in the wax synthesis observed in etiolated Euglena
physiological function
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the enzyme is involved in the biosynthesis of medium-chain wax esters
physiological function
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the enzyme is probably involved in the wax synthesis observed in etiolated Euglena
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the purified enzyme undergoes degradation during storage at -20°C
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Blue A agarose column chromatography and palmitoyl-CoA agarose affinity column chromatography
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expressed in Saccharomyces cerevisiae strain H1246
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Kolattukudy, P.E.
Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis
Biochemistry
9
1095-1102
1970
Euglena gracilis, Euglena gracilis Z
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Teerawanichpan, P.; Qiu, X.
Fatty acyl-CoA reductase and wax synthase from Euglena gracilis in the biosynthesis of medium-chain wax esters
Lipids
45
263-273
2010
Euglena gracilis
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Wang, X.; Kolattukudy, P.E.
Solubilization and purification of aldehyde-generating fatty acyl-CoA reductase from green alga Botryococcus braunii
FEBS Lett.
370
15-18
1995
Botryococcus braunii
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