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Information on EC 1.2.1.B25 - long-chain-fatty-acyl-CoA reductase
for references in articles please use BRENDA:EC1.2.1.B25preliminary BRENDA-supplied EC number
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EC Tree
1.2.1.B25 long-chain-fatty-acyl-CoA reductaseSpecify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
Acr, aldehyde-forming fatty acyl-CoA reductase, cACR, cyanobacterial acyl-CoA reductase, FAR1, FAR4, FAR5, FAR6, long-chain ACR, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acr
aldehyde-forming fatty acyl-CoA reductase
cACR
cyanobacterial acyl-CoA reductase
long-chain ACR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hexadecanal + CoA + NADP+ = hexadecanoyl-CoA + NADPH
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hexadecanal + CoA + NADP+ = hexadecanoyl-CoA + NADPH
the enzyme operates by a Ping-Pong mechanism
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hexadecanal + CoA + NADP+ = hexadecanoyl-CoA + NADPH
the enzyme operates by a Ping-Pong mechanism
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NADP+ oxidoreductase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oleoyl-CoA + NADPH
(9Z)-octadecenal + CoA + NADP+
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low activity
-
-
?
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
recombinant protein nearly exclusively produces C18:0 fatty alcohol
aldehyde intermediate is immediately reduced into the corresponding alcohol, chain lengths of primary alcohols produced by FAR heterologous expression in yeast are consistent with the chain lengths of primary alcohols found in Arabidopsis suberin
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?
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
recombinant protein produces C18:0 and C20:0 fatty alcohols
aldehyde intermediate is immediately reduced into the corresponding alcohol, chain lengths of primary alcohols produced by FAR heterologous expression in yeast are consistent with the chain lengths of primary alcohols found in Arabidopsis suberin
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?
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
recombinant protein produces C18:0 and C22:0 fatty alcohols, C16:0-OH, C20:0-OH, and C24:0-OH also detectable
aldehyde intermediate is immediately reduced into the corresponding alcohol, chain lengths of primary alcohols produced by FAR heterologous expression in yeast are consistent with the chain lengths of primary alcohols found in Arabidopsis suberin
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?
dodecanoyl-CoA + NADPH
dodecanal + CoA + NADP+
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low activity
-
-
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
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low activity
-
-
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
low activity
-
-
?
stearoyl-CoA + NADPH
octadecanal + CoA + NADP+
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best substrate. When the enzyme is incubated with both stearoyl-CoA and NADPH, the acyl-enzyme accumulates to comprise about 50% of the enzyme. This observation suggests that the rates of acylation and reduction are approximately the same
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-
?
stearoyl-CoA + NADPH
octadecanal + CoA + NADP+
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best substrate. When the enzyme is incubated with both stearoyl-CoA and NADPH, the acyl-enzyme accumulates to comprise about 50% of the enzyme. This observation suggests that the rates of acylation and reduction are approximately the same
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?
additional information
?
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detailed analysis of FAR6 gene promotor
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?
additional information
?
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the enzyme cACR is specific for NADPH and specifically catalyzes the reduction of fatty acyl-CoA esters to the corresponding aldehydes, rather than alcohols. Stearoyl-CoA is the most effective substrate, being reduced more rapidly than either longer or shorter chain acyl-CoAs. The enzyme is acylated on incubation with stearoyl-CoA, suggesting that the reduction occurs through an enzyme-thioester intermediate, cf. EC 1.2.1.50, formation of an acyl thioester on an active site cysteinyl residue as an intermediate in the mechanism of reduction. No activity with octanoyl-CoA
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-
?
additional information
?
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the enzyme cACR is specific for NADPH and specifically catalyzes the reduction of fatty acyl-CoA esters to the corresponding aldehydes, rather than alcohols. Stearoyl-CoA is the most effective substrate, being reduced more rapidly than either longer or shorter chain acyl-CoAs. The enzyme is acylated on incubation with stearoyl-CoA, suggesting that the reduction occurs through an enzyme-thioester intermediate, cf. EC 1.2.1.50, formation of an acyl thioester on an active site cysteinyl residue as an intermediate in the mechanism of reduction. No activity with octanoyl-CoA
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activates, inhibitory as it causes precipitation of the acyl-CoA substrate at 5 mM
Mn2+
-
activates, inhibitory as it causes precipitation of the acyl-CoA substrate at 2 mM
additional information
-
ACR requires divalent metal ions for activity. 2-mercaptoethanol and Na+ have no effect on activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
-
inactivation at 1 mM, stearoyl-CoA protects, probably due to competition between the two reagents for the active site cysteine
octyl glucoside
-
activates slightly about at 0.2%, inhibitory at above 0.5%
additional information
-
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
LITERATURE
IMAGE
octyl glucoside
-
activates slightly about at 0.2%, inhibitory at above 0.5%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetic analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
slight accumulation in developing ones
brenda
additional information
FAR1 transcript not found in stem and gene expression patterns of the enzyme is associated with known sites of suberin deposition
brenda
additional information
FAR1 transcript not found in stem and gene expression patterns of the enzyme is associated with known sites of suberin deposition
brenda
additional information
FAR1 transcript not found in stem and gene expression patterns of the enzyme is associated with known sites of suberin deposition
brenda
additional information
FAR6 expression completely absent in leaves and root tissues
brenda
additional information
gene expression patterns of the enzyme is associated with known sites of suberin deposition
brenda
additional information
gene expression patterns of the enzyme is associated with known sites of suberin deposition
brenda
additional information
gene expression patterns of the enzyme is associated with known sites of suberin deposition
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
enzyme is responsible for generating primary fatty alcohols associated with suberin biosynthesis
physiological function
physiological function
observations reveal the association of the FAR6 gene with wound response
physiological function
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long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes
physiological function
-
long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FACR6_ARATH
548
0
61626
Swiss-Prot
Secretory Pathway (Reliability: 2)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified cACR is quite unstable and tends to precipitate after 3-4 days when stored at 4°C, although it can be stored for prolonged periods at -80°C without loss of activity
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4°C, purified cACR is quite unstable and tends to precipitate after 3-4 days when stored at 4°C, although it can be stored for prolonged periods at -80°C 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
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
biofuel production
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long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes. As such they are attractive as components in engineered metabolic pathways for drop in biofuels. The slow turnover number measured for Synechococcus elongatus ACR poses a challenge for its use in biofuel applications where highly efficient enzymes are needed
biofuel production
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long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes. As such they are attractive as components in engineered metabolic pathways for drop in biofuels. The slow turnover number measured for Synechococcus elongatus ACR poses a challenge for its use in biofuel applications where highly efficient enzymes are needed
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
153
1539-1554
2010
Arabidopsis thaliana (Q0WRB0), Arabidopsis thaliana (Q39152), Arabidopsis thaliana (Q9LXN3)
brenda
Gupta, N.C.; Jain, P.K.; Bhat, S.R.; Srinivasan, R.
Upstream sequence of fatty acyl-CoA reductase (FAR6) of Arabidopsis thaliana drives wound-inducible and stem-specific expression
Plant Cell Rep.
31
839-850
2012
Arabidopsis thaliana (B9TSP7)
brenda
Lin, F.; Das, D.; Lin, X.N.; Marsh, E.N.
Aldehyde-forming fatty acyl-CoA reductase from cyanobacteria expression, purification and characterization of the recombinant enzyme
FEBS J.
280
4773-4781
2013
Synechococcus elongatus, Synechococcus elongatus PCC7942
brenda
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Release 2023.1 (January 2023)
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