Information on EC 1.2.1.50 - long-chain acyl-protein thioester reductase

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

EC NUMBER
COMMENTARY hide
1.2.1.50
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RECOMMENDED NAME
GeneOntology No.
long-chain acyl-protein thioester reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+
show the reaction diagram
together with EC 6.2.1.19 forms a fatty acid reductase system which produces the substrate of EC 1.14.14.3, thus being a part of the bacterial luciferase system
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacterial bioluminescence
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Cutin, suberine and wax biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NADP+ oxidoreductase (protein thioesther-forming)
Together with a transferase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
50936-56-6
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75718-33-1
complex of three enzymes
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain M-1
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
honey bee
UniProt
Manually annotated by BRENDA team
FAR1
SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
pea
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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 acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
show the reaction diagram
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?
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
show the reaction diagram
AmFAR1 converts saturated fatty acids ranging from 16 to 22 carbon chains to their corresponding alcohols with the highest conversion efficiency shown on 18:0, AmFAR1 also shows some activities on ricinoleic acid, 16:1n-7 and 18:1n-9
aldehyde intermediate is immediately reduced to the corresponding alcohol
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?
arachidonoyl-CoA + NADPH
cis-5,8,11,14-eicosatetraenal + NADP+ + CoA
show the reaction diagram
low activity
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?
arachidonoyl-CoA + NADPH + H+
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenal + CoA + NADP+
show the reaction diagram
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further reduction of (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenal into the corresponding (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraen-1-ol
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arachidoyl-CoA + NADP+
eicosanal + CoA + NADPH
show the reaction diagram
erucoyl-CoA + NADPH + H+
(13Z)-docos-13-enal + CoA + NADP+
show the reaction diagram
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erucoyl-CoA i.e. (13Z)-docos-13-enoyl-CoA
further direct reduction of (13Z)-docos-13-enal into the corresponding (13Z)-docos-13-en-1-ol
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?
fatty acyl-CoA + NADPH + H+
fatty aldehyde + CoA + NADP+
show the reaction diagram
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reaction intermediate, enzyme converts fatty acyl-CoA directly into the corresponding fatty alcohol by four-electron reduction, free fatty aldehyde intermediate is not accessible
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hexadecanoyl-CoA + NADPH
hexadecanal + CoA + NADP+
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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?
icosanoyl-CoA + NADPH + H+
icosanal + CoA + NADP+
show the reaction diagram
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further direct reduction of icosanal into the corresponding icosan-1-ol
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?
lauroyl-CoA + NADP+
dodecanal + CoA + NADPH
show the reaction diagram
lauroyl-CoA + NADPH + H+
dodecanal + CoA + NADP+
show the reaction diagram
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further reduction of dodecanal into the corresponding dodecan-1-ol
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linoleoyl-CoA + NADPH
cis-9,12-octadecadienal + NADP+ + CoA
show the reaction diagram
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?
myristoyl-CoA + NADP+
? + CoA + NADPH
show the reaction diagram
myristoyl-CoA + NADPH
?
show the reaction diagram
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?
myristoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
show the reaction diagram
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further reduction of tetradecanal into the corresponding tetradecan-1-ol
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octanoyl-CoA + NADPH + H+
octanal + NADP+
show the reaction diagram
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further reduction of octanal into the corresponding octan-1-ol
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oleoyl-CoA + NADPH
cis-9-octadecenal + NADP+ + CoA
show the reaction diagram
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?
oleoyl-CoA + NADPH + H+
(9Z)-octadec-9-enal + CoA + NADP+
show the reaction diagram
palmitoleoyl-CoA + NADPH + H+
(9Z)-hexadec-9-enal + CoA + NADP+
show the reaction diagram
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further reduction of (9Z)-hexadec-9-enal into the corresponding (9Z)-hexadec-9-en-1-ol
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palmitoyl-ACP + NADPH
1-hexadecanol + acyl-carrier protein + NADP+
show the reaction diagram
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the recombinant acyl-CoA reductase from Simmondsia chinensis exhibits a specificty to palmitoyl-ACP and not palmitoyl-CoA when expressed in Escherichia coli
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?
palmitoyl-CoA + NADP+
hexadecanal + CoA + NADPH
show the reaction diagram
palmitoyl-CoA + NADPH
hexadecanal + NADP+ + CoA
show the reaction diagram
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?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
show the reaction diagram
palmitoyl-[acyl-carrier protein] + NADPH + H+
hexadecanal + [acyl-carrier protein] + NADP+
show the reaction diagram
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further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
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?
ricinoleoyl-CoA + NADPH + H+
(9Z,12R)-12-hydroxyoctadec-9-enal + CoA + NADP+
show the reaction diagram
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ricinoleoyl-CoA i.e. (9Z,12R)-12-hydroxyoctadec-9-enoyl-CoA
further direct reduction of (9Z,12R)-12-hydroxyoctadec-9-enal into the corresponding (9Z,12R)-octadec-9-ene-1,12-diol
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?
stearoyl-CoA + NADP+
octadecanal + CoA + NADPH
show the reaction diagram
44% of the activity with myristoyl-CoA
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?
stearoyl-CoA + NADPH
octadecanal + NADP+ + CoA
show the reaction diagram
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?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
show the reaction diagram
tetradecanoyl-CoA + NADPH
tetradecanal + CoA + NADP+
show the reaction diagram
tetraeicos-cis-15-enoyl-CoA + NADPH
tetraeicos-cis-15-en-1-ol + CoA + NADP+
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
tetradecanoyl-CoA + NADPH
tetradecanal + CoA + NADP+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cerulenin
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i.e. (2S,3R)-2,3-epoxy-4-oxy-7,10-dodecadienoylamide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
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2 mg per ml increases activity by more than 5 times
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.067
NADPH
0.029
palmitoyl-CoA
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0.001
tetradecanoyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0273
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ricinoleoyl-CoA, pH 7.0, 30C
0.043
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palmitoyl-CoA, pH 7.0, 30C
0.0677
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stearoyl-CoA, pH 7.0, 30C
0.0774
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icosanoyl-CoA, pH 7.0, 30C
0.1082
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oleoyl-CoA, pH 7.0, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
reaction with palmitoyl-CoA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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activity falling dramatically below pH 6.5 and above 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
; most abundant in
Manually annotated by BRENDA team
predominance, expression level of AmFAR1 in head approximately three times higher than in thorax and abdomen
Manually annotated by BRENDA team
tissue with highest mRNA level
Manually annotated by BRENDA team
; 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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
theoretical value, verified by SDS-PAGE
55500
theoretical value, verified by SDS-PAGE
56000
theoretical value, verified by SDS-PAGE
59200
calculated from sequence
61600
theoretical value, verified by SDS-PAGE
68400
theoretical value, verified by SDS-PAGE, heavily degraded
116000
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SDS-PAGE, in agreement with mass calculated from amino acid sequence
140000
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recombinant CpFAS1-R domain as maltose binding protein fusion protein, SDS-PAGE
205000 - 223000
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reductase component of fatty acid reductase enzyme complex, gel filtration, SDS-PAGE after cross-linkage with bis(sulfosuccinimidyl)suberate
450000
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fatty acid reductase enzyme complex composed of synthetase (s), reductase (r) and transferase (t), molar ratio s: r: t is 1: 1: 0.5, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
polymer
tetramer
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4 * 50000-58000, reductase component of fatty acid reductase enzyme complex, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
requires thiol reducing agents for stability and activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM phosphate buffer, pH 7.0, 0.2 M NaCl, 5 mM dithiothreitol, 30-35% glycerol, 1 month
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-20C, 50 mM phosphate buffer, pH 7.0, 0.2 M NaCl, 50 mM beta-mercaptoethanol, 30% glycerol, several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose resin-based chromatography purification
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by amylose affinity chromatography and metal affinity chromatography with nickel
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via fusion protein with maltose binding protein and an N-terminal His-tag fusion
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of CpFAS1-R domain in a pMAL-c2x vector with maltose binding protein-fusion protein and expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
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expression in Escherichia coli; overexpression in Escherichia coli
expression in HEK 293 cells
heterologous expression of pYES2.1 plasmid harbouring AmFAR1 in Saccharomyces cerevisiae strain INVSc1
into the vector pET15b for expression in Escherichia coli Rosetta cells; into the vector pET15b for expression in Escherichia coli Rosetta cells; into the vector pET15b for expression in Escherichia coli Rosetta cells; into the vector pET15b for expression in Escherichia coli Rosetta cells; into the vector pET15b for expression in Escherichia coli Rosetta cells
plasmid pHisMBPMarFAR harbouring the sequence of hypothetical protein Maqu_2220 added by His-tag and maltose binding protein transformed to Escherichia coli strain Rosetta (DE3) for heterologous protein expression
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plasmid pPCRMALD8 containing the FACoAR from Marinobacter aquaeolei VT8 with an N-terminal maltose binding protein fusion and a C-terminal His-tag transformed into the Escherichia coli TB1 strain for protein expression
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C171S
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acylation and specific activity similar to the wild-type
C279S
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acylation and specific activity similar to the wild-type
C286S
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no acylation and no activity
C171S
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acylation and specific activity similar to the wild-type
C279S
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acylation and specific activity similar to the wild-type
C286S
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no acylation and no activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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production of jojoba plant wax esters
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