Information on EC 1.2.1.B25 - long-chain-fatty-acyl-CoA reductase

for references in articles please use BRENDA:EC1.2.1.B25
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.2.1.B25
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
long-chain-fatty-acyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hexadecanal + CoA + NADP+ = hexadecanoyl-CoA + NADPH
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NADP+ oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
enzyme is responsible for generating primary fatty alcohols associated with suberin biosynthesis; enzyme is responsible for generating primary fatty alcohols associated with suberin biosynthesis; enzyme is responsible for generating primary fatty alcohols associated with suberin biosynthesis
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
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
show the reaction diagram
dodecanoyl-CoA + NADPH
dodecanal + CoA + NADP+
show the reaction diagram
eicosanoyl-CoA + NADPH
eicosanal + CoA + NADP+
show the reaction diagram
-
-
-
-
?
hexadecanoyl-CoA + NADPH
hexadecanal + CoA + NADP+
show the reaction diagram
oleoyl-CoA + NADPH
(9Z)-octadecenal + CoA + NADP+
show the reaction diagram
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low activity
-
-
?
stearoyl-CoA + NADPH
octadecanal + CoA + NADP+
show the reaction diagram
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
stearoyl-CoA + NADPH
octadecanal + CoA + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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specific for
additional information
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no activity with NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activates, inhibitory as it causes precipitation of the acyl-CoA substrate at 5 mM
K+
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activates about 10fold
Mg2+
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best activating divalent cation
Mn2+
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activates, inhibitory as it causes precipitation of the acyl-CoA substrate at 2 mM
additional information
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ACR requires divalent metal ions for activity. 2-mercaptoethanol and Na+ have no effect on activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
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activates about by 75% at 0.2%, inhibitory at above 0.5%
Digitonin
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activates about at 0.1%, inhibitory at above 0.5%
dithiothreitol
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inhibits the enzyme at 5 mM
glutathione
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inhibits the enzyme at 5 mM
iodoacetamide
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inactivation at 1 mM, stearoyl-CoA protects, probably due to competition between the two reagents for the active site cysteine
octyl glucoside
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activates slightly about at 0.2%, inhibitory at above 0.5%
Triton
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inhibitory at above 0.5%
additional information
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once acylated by stearoyl-CoA the enzyme is protected from inactivation by iodoacetamide and the cACR activity remains unchanged
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
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activates 3fold at 1 mg/ml
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CHAPS
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activates about by 75% at 0.2%, inhibitory at above 0.5%
Digitonin
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activates about at 0.1%, inhibitory at above 0.5%
octyl glucoside
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activates slightly about at 0.2%, inhibitory at above 0.5%
tris(hydroxylpropyl)phosphine
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activates 2fold at 20 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0356
NADPH
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pH 7.5, 37C, recombinant enzyme
0.0319
stearoyl-CoA
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pH 7.5, 37C, recombinant enzyme
additional information
additional information
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steady-state kinetic analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
stearoyl-CoA
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pH 7.5, 37C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
; slight accumulation; slight accumulation
Manually annotated by BRENDA team
young; young and mature one; young and mature one
Manually annotated by BRENDA team
slight accumulation; slight accumulation
Manually annotated by BRENDA team
developing one; slight accumulation in developing ones; slight accumulation in developing ones
Manually annotated by BRENDA team
gene expressed predominantly
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified cACR is quite unstable and tends to precipitate after 3-4 days when stored at 4C, although it can be stored for prolonged periods at -80C without loss of activity
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4C, purified cACR is quite unstable and tends to precipitate after 3-4 days when stored at 4C, although it can be stored for prolonged periods at -80C without loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
open reading frame subcloned into yeast expression vector pVT102U Saccharomyces cerevisiae; open reading frame subcloned into yeast expression vector pVT102U Saccharomyces cerevisiae; open reading frame subcloned into yeast expression vector pVT102U Saccharomyces cerevisiae
recombinant overexpression of His-tagged enzyme in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by wounding in the epidermal layer of mature stem internodes, transcript levels increase more than 2fold after 30 min of wounding
FAR1 transcript detectable by RT-PCR at 1 h after wounding and peaks at 48 h and remained high after 96 h, further induction after 4 h at salt concentrations of 50, 100, and 200 mM NaCl - FAR1 levels remain induced at 24 h only in the presence of 200 mM NaCl; FAR4 transcript detectable by RT-PCR at 24 h after wounding and peaks at 48 h and remained high after 96 h, further induction after 4 h at salt concentrations of 50, 100, and 200 mM NaCl - induced expression levels remain high after 24 h at all three salt concentrations; FAR5 transcript detectable by RT-PCR at 1 h after wounding and peaks at 48 h and remained high after 96 h, further induction after 4 h at salt concentrations of 50, 100, and 200 mM NaCl - induced expression levels remain high after 24 h at all three salt concentrations
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production