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Information on EC 1.2.1.50 - long-chain acyl-protein thioester reductase
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EC Tree
1.2.1.50 long-chain acyl-protein thioester reductaseIUBMB Comments
Together with a hydrolase 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.
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Word Map
- 1.2.1.50
- plasmalogens
- phosphoreum
-
preputial
-
photobacterium
-
ether-linked
- aquaeolei
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acyl-coa reductase, fatty acyl-coa reductase 1, amfar1, acyl coenzyme a reductase, fatty acyl-coa reductase 6, fatty acyl-coa reductase 2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl coenzyme A reductase
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-
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acyl-CoA reductase
fatty acyl-CoA reductase
long-chain-fatty-acyl-CoA reductase
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-
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acyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+
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
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NADP+ oxidoreductase (protein thioesther-forming)
Together with a hydrolase 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.
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CAS REGISTRY NUMBER
COMMENTARY
50936-56-6
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75718-33-1
complex of three enzymes
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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
a long-chain acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
-
-
-
-
?
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
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
-
?
arachidonoyl-CoA + NADPH + H+
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenal + CoA + NADP+
Marinobacter nauticus
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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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?
erucoyl-CoA + NADPH + H+
(13Z)-docos-13-enal + CoA + NADP+
Marinobacter nauticus
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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
-
?
fatty acyl-CoA + NADPH + H+
fatty aldehyde + CoA + NADP+
Marinobacter nauticus
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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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?
icosanoyl-CoA + NADPH + H+
icosanal + CoA + NADP+
Marinobacter nauticus
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further direct reduction of icosanal into the corresponding icosan-1-ol
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?
lauroyl-CoA + NADPH + H+
dodecanal + CoA + NADP+
Marinobacter nauticus
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-
further reduction of dodecanal into the corresponding dodecan-1-ol
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?
myristoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
Marinobacter nauticus
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further reduction of tetradecanal into the corresponding tetradecan-1-ol
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?
octanoyl-CoA + NADPH + H+
octanal + NADP+
Marinobacter nauticus
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further reduction of octanal into the corresponding octan-1-ol
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?
palmitoleoyl-CoA + NADPH + H+
(9Z)-hexadec-9-enal + CoA + NADP+
Marinobacter nauticus
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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+
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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-[acyl-carrier protein] + NADPH + H+
hexadecanal + [acyl-carrier protein] + NADP+
Marinobacter nauticus
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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+
Marinobacter nauticus
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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
44% of the activity with myristoyl-CoA
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?
tetraeicos-cis-15-enoyl-CoA + NADPH
tetraeicos-cis-15-en-1-ol + CoA + NADP+
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?
arachidoyl-CoA + NADP+
eicosanal + CoA + NADPH
29% of the activity with NADPH
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?
arachidoyl-CoA + NADP+
eicosanal + CoA + NADPH
29% of the activity with NADPH
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?
lauroyl-CoA + NADP+
dodecanal + CoA + NADPH
33% of the activity with myristoyl-CoA
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?
lauroyl-CoA + NADP+
dodecanal + CoA + NADPH
33% of the activity with myristoyl-CoA
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?
oleoyl-CoA + NADPH + H+
(9Z)-octadec-9-enal + CoA + NADP+
Marinobacter nauticus
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further direct reduction of (9Z)-octadec-9-enal into the corresponding (9Z)-octadec-9-en-1-ol
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?
oleoyl-CoA + NADPH + H+
(9Z)-octadec-9-enal + CoA + NADP+
Marinobacter nauticus
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further reduction of (9Z)-octadec-9-enal into the corresponding (9Z)-octadec-9-en-1-ol
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?
palmitoyl-CoA + NADP+
hexadecanal + CoA + NADPH
90% of the activity with myristoyl-CoA
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?
palmitoyl-CoA + NADP+
hexadecanal + CoA + NADPH
90% of the activity with myristoyl-CoA
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?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Marinobacter nauticus
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further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
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?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Marinobacter nauticus
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further reduction of hexadecanal into the corresponding hexadecan-1-ol
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?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Marinobacter nauticus
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further direct reduction of octadecanal into the corresponding octadecan-1-ol
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?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Marinobacter nauticus
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further reduction of octadecanal into the corresponding octadecan-1-ol
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?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
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?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
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?
additional information
?
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substrates with carbon chain lengths shorter thah 8 do not show any activity
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?
additional information
?
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substrates with carbon chain lengths shorter thah 8 do not show any activity
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?
additional information
?
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substrates with carbon chain lengths shorter thah 8 do not show any activity
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?
additional information
?
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no activity observed on 18:2n-6 and 18:3n-3
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?
additional information
?
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no activity observed on 18:2n-6 and 18:3n-3
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?
additional information
?
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catalyses the formation of a fatty alcohol from an acyl-CoA
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?
additional information
?
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catalyses the formation of a fatty alcohol from an acyl-CoA
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?
additional information
?
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catalyses the formation of a fatty alcohol from an acyl-CoA
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?
additional information
?
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catalyses the formation of a fatty alcohol from an acyl-CoA
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?
additional information
?
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catalyses the formation of a fatty alcohol from an acyl-CoA
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?
additional information
?
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enzyme only utilizes very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16, enzyme is capable of using NADPH and NADH as electron donors, but prefers NADPH to NADH
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?
additional information
?
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Marinobacter nauticus
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in contrast to other prokaryotes, the enzyme performs the two reduction steps from acyl-CoA to fatty alcohol in a single step which is typical for eukaryotes
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?
additional information
?
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Marinobacter nauticus
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no reaction product detected with NADH or free fatty acids
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?
additional information
?
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Marinobacter nauticus
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shorter acyl chains than 16 carbon are less effectively utilized and with these substrates substantial amounts of both free fatty acids and fatty aldehyde are formed
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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
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
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-
-
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?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
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-
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?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
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-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
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-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
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-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
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-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
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2 mg per ml increases activity by more than 5 times
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cataract
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Epilepsy
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Intellectual Disability
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
long-chain acyl-protein thioester reductase deficiency
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
long-chain acyl-protein thioester reductase deficiency
A rare case of fatty acyl-CoA reductase 1 deficiency in an Indian infant manifesting rhizomelic chondrodystrophy phenotype.
long-chain acyl-protein thioester reductase deficiency
Familial Mitral Arcade, Tricuspid Dysplasia, Left Ventricular Noncompaction and Short-Chain Acyl-CoA Reductase Deficiency.
long-chain acyl-protein thioester reductase deficiency
Fatty Acyl-CoA Reductase 1 Deficiency.
Microcephaly
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Neoplasms
Acyl-CoA reductase specificity and synthesis of wax esters in mouse preputial gland tumors.
Peroxisomal Disorders
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Tuberculosis
Catabolism of the Last Two Steroid Rings in Mycobacterium tuberculosis and Other Bacteria.
Zellweger Syndrome
Properties of the enzymes catalyzing the biosynthesis of lysophosphatidate and its ether analog in cultured fibroblasts from Zellweger syndrome patients and normal controls.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
predominance, expression level of AmFAR1 in head approximately three times higher than in thorax and abdomen
brenda
additional information
additional information
AmFAR1 ubiquitously expressed in all body segments
brenda
additional information
-
AmFAR1 ubiquitously expressed in all body segments
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
CpFAS1-R enzyme is part of the CpFAS1 multifunctional Type I fatty acid synthase complex with at least 21 enzymatic domains, complex is predicted to function as a fatty acyl elongase preferring long chain fatty acids as substrates
metabolism
enzyme is involved in the conversion of a wide range of fatty acids to their corresponding alcohols, which are the essential components of pheromones, wax esters or ether lipids
Show AA Sequence and Transmembrane Helices (1742 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
116000
Marinobacter nauticus
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SDS-PAGE, in agreement with mass calculated from amino acid sequence
140000
-
recombinant CpFAS1-R domain as maltose binding protein fusion protein, SDS-PAGE
205000 - 223000
-
reductase component of fatty acid reductase enzyme complex, gel filtration, SDS-PAGE after cross-linkage with bis(sulfosuccinimidyl)suberate
34000
450000
-
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
50000
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
51000
theoretical value, verified by SDS-PAGE
52000
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
55500
theoretical value, verified by SDS-PAGE
56000
57000
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
58000
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
61600
theoretical value, verified by SDS-PAGE
68400
theoretical value, verified by SDS-PAGE, heavily degraded
34000
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
34000
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
56000
theoretical value, verified by SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
polymer
tetramer
-
4 * 50000-58000, reductase component of fatty acid reductase enzyme complex, SDS-PAGE
polymer
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
polymer
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM phosphate buffer, pH 7.0, 0.2 M NaCl, 5 mM dithiothreitol, 30-35% glycerol, 1 month
-
-20°C, 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
by amylose affinity chromatography and metal affinity chromatography with nickel
Marinobacter nauticus
-
via fusion protein with maltose binding protein and an N-terminal His-tag fusion
Marinobacter nauticus
-
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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
-
expression in Escherichia coli
heterologous expression of pYES2.1 plasmid harbouring AmFAR1 in Saccharomyces cerevisiae strain INVSc1
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
Marinobacter nauticus
-
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
Marinobacter nauticus
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wall, L.; Meighen, E.A.
Subunit structure of the fatty acid reductase complex from Photobacterium phosphoreum
Biochemistry
25
4315-4321
1986
Photobacterium phosphoreum
-
brenda
Riendeau, D.; Rodriguez, A.; Meighen, E.
Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex
J. Biol. Chem.
257
6908-6915
1982
Photobacterium phosphoreum
brenda
Rodriguez, A.; Wall, L.; Raptis, S.; Zarkadas, C.G.; Meighen, E.
Different sites for fatty acid activation and acyl transfer by the synthetase subunit of fatty acid reductase: acylation of a cysteinyl residue
Biochim. Biophys. Acta
964
266-275
1988
Photobacterium phosphoreum
-
brenda
Wang, X.; Kolattukudy, P.E.
Solubilization, purification and characterization of fatty acyl-CoA reductase from duck uropygial gland
Biochem. Biophys. Res. Commun.
208
210-215
1995
Anas platyrhynchos
brenda
Lee, C.Y.; Meighen, E.A.
Cysteine-286 as the site of acylation of the lux-specific fatty acyl-CoA reductase
Biochim. Biophys. Acta
1338
215-222
1997
Photobacterium leio