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Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase and Organism(s) Rattus norvegicus and UniProt Accession Q924N5
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6.2.1.3 long-chain-fatty-acid-CoA ligaseIUBMB Comments
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
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Word Map
- 6.2.1.3
- peroxisome
- triglyceride
- palmitate
- adipose
-
acsls
-
ppars
- phospholipid
- cholesterol
- adipocytes
- obesity
-
arachidonic
- lipoprotein
- carnitine
- triacylglycerols
-
fatps
-
beta-oxidation
-
proliferator-activated
- lipase
- acyltransferase
- droplet
-
polyunsaturated
- triacsin
- translocase
-
high-fat
- palmitoyltransferase
-
lipogenesis
- oleate
- diacylglycerol
-
lipolysis
-
lcfas
-
docosahexaenoic
- steatosis
- esterification
-
ferroptosis
-
palmitoylation
-
medium-chain
- adrenoleukodystrophy
-
fabppm
- ichthyosis
- pparalpha
-
lipotoxicity
-
l-fabp
-
very-long-chain
-
lignoceric
- arachidonoyl-coa
- coash
-
npc1l1
- cutin
- acaca
-
perilipin
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
acsl1, fatp4, fatty acid transport protein, acsl3, acsl5, long-chain acyl-coa synthetase, fatty acyl-coa synthetase, acsl6, fatp2, acyl-coa synthetase long-chain, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACS1
ACS2
ACS3
ACSL1
ACSL3
ACSL4
ACSL6
Acyl coenzyme A synthetase
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Acyl-CoA ligase
-
-
-
-
Acyl-CoA synthetase
Acyl-CoA synthetase 3
-
-
-
-
Acyl-coenzyme A ligase
-
-
-
-
FAA1
-
-
-
-
Fatty acid CoA ligase
-
-
-
-
Fatty acid thiokinase (long chain)
-
-
-
-
Fatty acyl-coenzyme A synthetase
-
-
-
-
Fatty-acyl-CoA ligase
-
-
-
-
LACS
LCFA synthetase
-
-
-
-
long chain acyl-CoA synthetase
long chain acyl-CoA synthetase 1
long chain acyl-CoA synthetase 4
long chain acyl-CoA synthetase 5
Long chain fatty acyl CoA ligase
-
-
-
-
Long chain fatty acyl-CoA synthetase
-
-
-
-
Long-chain acyl CoA synthetase
-
-
-
-
Long-chain acyl-CoA synthetase I
-
-
-
-
Long-chain acyl-CoA synthetase II
-
-
-
-
Long-chain acyl-coenzyme A synthetase
Long-chain fatty acyl coenzyme A synthetase
-
-
-
-
mACS4
-
-
-
-
Oleoyl-CoA synthetase
-
-
-
-
Palmitoyl coenzyme A synthetase
-
-
-
-
Palmitoyl-CoA ligase
-
-
-
-
Palmityl-coenzyme A synthetase
-
-
-
-
Pristanoyl-CoA synthetase
-
-
-
-
Stearoyl-CoA synthetase
-
-
-
-
Thiokinase
-
-
-
-
ACS3
-
-
-
-
ACSL4
prefers longer chain polyunsaturated fatty acids as substrates
Acyl-CoA synthetase
-
-
-
-
LACS
-
-
-
-
Long-chain acyl-coenzyme A synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA
mitochondrial long chain fatty acyl-CoA ligase, unlike short chain ligases and medium chain ligases, does not utilize an adenylate as an intermediate in the formation of fatty acyl-CoA
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
Phosphorylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
long-chain fatty acid:CoA ligase (AMP-forming)
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
CAS REGISTRY NUMBER
COMMENTARY
9013-18-7
-
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
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
-
?
ATP + fatty acid + 4'-phosphopantetheine
AMP + diphosphate + acyl-4'-phosphopantetheine
-
-
-
-
?
ATP + fatty acid + dephospho-CoA
AMP + diphosphate + acyl-dephospho-CoA
-
-
-
-
?
ATP + fatty acid + pantetheine
AMP + diphosphate + acyl-pantetheine
-
-
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
4% of the activity with palmitate
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
?
ATP + (R)-ibuprofen + CoA
AMP + diphosphate + (R)-ibuprofenoyl-CoA
-
9% of the activity with palmitate
-
?
ATP + (R)-ibuprofen + CoA
AMP + diphosphate + (R)-ibuprofenoyl-CoA
-
(R)-ibuprofenoyl-CoA synthetase and long-chain acyl-CoA synthetase are identical enzymes that are involved in the metabolism of various xenobiotics
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
preferred substrate
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
85% of the activity with palmitate
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
the activity with arachidonate is twice as high as with palmitate
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
physiological significance of enzyme in fatty acid metabolism
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
enzyme is essential for both oxidation and esterification of fatty acids
-
-
?
ATP + long-chain carboxylic acid + CoA
?
the presence in the brain of multiple forms of enzyme with different fatty acid specificity is of considerable biological significance for controlling the synthesis of brain lipids. ACS3 mRNA is detectable 5 days after birth, increases to a maximum level at 15 days, and then decreases gradually to 10% of its maximum level in the adult
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
optimal activity at 12:0 with saturated fatty acids as substrate, at 14:1 with mono-unsaturated fatty acids. The mono-unsaturated fatty acids from 14:1 to 22:1 give higher activity than the corresponding saturated fatty acids. Position of the double bond and the cis/trans configuration have little effect on the velocity values except for 22:1(11) (cis) which reveals a 2fold higher activity than 22:1(13)(cis) fatty acid. Polyunsaturated fatty acid 22:6(all cis) is a much better substrate than other C22 fatty acids
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
18:3(n-3)
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
18:1
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
substrate specificity of microsomal and mitochondrial enzyme are indistinguishable
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
among the saturated fatty acids highest activity is obtained with 12:0 fatty acid, monounsaturated fatty acids (16:1, 18:1, 20:1 and 22:1) are equally good or slightly better substrates than the corresponding saturated fatty acids, polyunsaturated fatty acids are rather poor substrates
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
utilizes laurate and myristate most efficientyl among C8-C22 saturated fatty acids and arachidonate and eicosapentaenoate among the C16-C20 unsaturated fatty acids
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
20:3(n-6)
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
20% of the activity with palmitate
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
additional information
?
-
no activity for the very long chain fatty acid, lignoceric acid, and a medium chain fatty acid, decanoic acid
-
?
additional information
?
-
-
ACS1, ACS4 and ACS5 are regulated independently by fasting and refeeding. Fasting rats for 48 h results in a decrease in ACS4 protein and an increase in ACS5. ACS1 and ACS4 may be functionally channeled to specific metabolic pathways though different ACS isoforms in unique subcellular locations
-
?
additional information
?
-
-
Acsl6 functions primarily in docosagexaenoic acid metabolism, its overexpression increases docosahexaenoic acid and arachidonic acid internalization primarily during the first 24 h of neuronal differentiation to stimulate phospholipid and enhance neurite outgrowth
-
-
?
additional information
?
-
-
high glucose concentration and insulin induce ACS-5 expression. The effect of insulin is mediated by SREBP-1c. ACS-5 is involved in anabolism of fatty acids
-
-
?
additional information
?
-
-
it is hypothesized that the enzyme plays an important role in targeting free fatty acids to specific metabolic pathways or acylation sites in the cell, thus acting as an important control mechanism in fuel partitioning. Localization of the enzyme at the plasma membrane may serve to decrease free fatty acid efflux and trap free fatty acids within the cell as long-chain acyl CoA
-
-
?
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
ATP + (R)-ibuprofen + CoA
AMP + diphosphate + (R)-ibuprofenoyl-CoA
-
(R)-ibuprofenoyl-CoA synthetase and long-chain acyl-CoA synthetase are identical enzymes that are involved in the metabolism of various xenobiotics
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
preferred substrate
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
physiological significance of enzyme in fatty acid metabolism
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
enzyme is essential for both oxidation and esterification of fatty acids
-
-
?
ATP + long-chain carboxylic acid + CoA
?
the presence in the brain of multiple forms of enzyme with different fatty acid specificity is of considerable biological significance for controlling the synthesis of brain lipids. ACS3 mRNA is detectable 5 days after birth, increases to a maximum level at 15 days, and then decreases gradually to 10% of its maximum level in the adult
-
-
?
additional information
?
-
-
ACS1, ACS4 and ACS5 are regulated independently by fasting and refeeding. Fasting rats for 48 h results in a decrease in ACS4 protein and an increase in ACS5. ACS1 and ACS4 may be functionally channeled to specific metabolic pathways though different ACS isoforms in unique subcellular locations
-
?
additional information
?
-
-
Acsl6 functions primarily in docosagexaenoic acid metabolism, its overexpression increases docosahexaenoic acid and arachidonic acid internalization primarily during the first 24 h of neuronal differentiation to stimulate phospholipid and enhance neurite outgrowth
-
-
?
additional information
?
-
-
high glucose concentration and insulin induce ACS-5 expression. The effect of insulin is mediated by SREBP-1c. ACS-5 is involved in anabolism of fatty acids
-
-
?
additional information
?
-
-
it is hypothesized that the enzyme plays an important role in targeting free fatty acids to specific metabolic pathways or acylation sites in the cell, thus acting as an important control mechanism in fuel partitioning. Localization of the enzyme at the plasma membrane may serve to decrease free fatty acid efflux and trap free fatty acids within the cell as long-chain acyl CoA
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
maximal activity at 15-20 mM MgCl2, no inhibition at higher concentrations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoic acid
-
competitive inhibitor of palmitoleic acid activation
2-Bromopalmitate
-
inhibition can be overcome by addition of phospholipid vesicles
2-bromopalmitoyl-CoA
-
inhibition can be overcome by addition of phospholipid vesicles
cis-9,10-methylene octadecanoic acid
-
IC50: 0.025 mM for ACS1-Flag fusion protein, 0.03-0.04 mM for ACS4-Flag fusion protein, no effect on ACS5-Flag fusion protein
Eicosa-11,14,17-trienoic acid
-
competitive inhibitor of palmitoleic acid activation
eicosa-8,11,14-trienoic acid
-
competitive inhibitor of palmitoleic acid activation
Eicosa-8,14-dienoic acid
-
competitive inhibitor of palmitoleic acid activation
GW1929
-
IC50: above 0.05 mM for ACS1-Flag fusion protein, 0.05 mM for ACS4-Flag fusion protein, no effect on ACS5-Flag fusion protein
Perfluorodecanoic acid
-
no inhibition by short-chain perfluorinated fatty acids
Perfluorononanoic acid
-
no inhibition by short-chain perfluorinated fatty acids
Perfluorooctanoic acid
-
no inhibition by short-chain perfluorinated fatty acids
pioglitazone
-
IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
Zwittergent 3-12
-
inhibition below the critical micellar concentration, 0.12%. below this concentrations no inhibition
fatty acids
-
palmitoleate, oleate and linoleate are competitive inhibitors of the activation of each other
fatty acids
-
saturated fatty acids do not inhibit activation of docosahexaenoate or palmitate. Unsaturated fatty acids, except nervonic acid, inhibit the activation of docosahexaenoate acid. Moderate inhibition by oleate, linoleate, eicosapentanoate, and palmitate
rosiglitazone
-
IC50: 0.0005 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
Triton X-100
-
slight inhibition when incubated with microsomes at 0°C for 30 min
troglitazone
-
IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
additional information
-
3-phenoxybenzoic acid, p-coumaric acid, ibuprofen, ferulic acid and firefly luciferin, at concentrations up to 0.05 mM have no effect on three ACS isoenzymes
-
additional information
isoenzyme ACSL3 maintains activity in presence of 2-3 mM Triton X-100. Isoenzyme ACSL6_v1 is insensitive to rosiglitazone
-
additional information
isoenzyme ACSL6_v1 maintains activity in presence of 2-3 mM Triton X-100. Isoenzyme ACSL6_v1 is insensitive to rosiglitazone and is not affected by triacsin C up to concentrations of 0.05 mM
-
additional information
isoenzyme ACSL6_v2 maintains optimal activity up to 4 mM Triton X-100. Isoenzyme ACSL6_v2 is insensitive to rosiglitazone and is not affected by triacsin C up to concentrations of 0.05 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triacsin C
ACSL activity is 17fold higher in the presence of 0.02 mM triacsin C
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0211
palmitate
mutant S291Y, at 37°C, in 175 mM Tris-HCl at pH 7.4
0.0238
palmitate
mutant L399M, at 37°C, in 175 mM Tris-HCl at pH 7.4
0.0281
palmitate
wild type enzyme, at 37°C, in 175 mM Tris-HCl at pH 7.4
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
cis-9,10-methylene octadecanoic acid
Rattus norvegicus
-
IC50: 0.025 mM for ACS1-Flag fusion protein, 0.03-0.04 mM for ACS4-Flag fusion protein, no effect on ACS5-Flag fusion protein
0.05
GW1929
Rattus norvegicus
-
IC50: above 0.05 mM for ACS1-Flag fusion protein, 0.05 mM for ACS4-Flag fusion protein, no effect on ACS5-Flag fusion protein
0.0015
pioglitazone
Rattus norvegicus
-
IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
0.0005
rosiglitazone
Rattus norvegicus
-
IC50: 0.0005 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
0.0015
troglitazone
Rattus norvegicus
-
IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9.8
-
pH 6: about 50% of maximal activity, pH 8.9: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
inguinal adipose tissue
additional information
gonadal and inguinal adipose tissue
-
-
-
hepatic ACS-5 mRNA is poorly expressed during fasting and diabetes and strongly induced by carbohydrate refeeding and insulin treatment
additional information
ACSL5 is expressed predominantly in tissues with high rates of triacylglycerol synthesis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
additional information
not localized in mitochondrion or plasma membrane
-
Ad-ACSL-5, long chain acyl-CoA synthetase 5 overexpressed in rat hepatoma McRrdle-RG7777 cells mediated by adenovirus colocalizes to both mitochondria and endoplasmic reticulum
-
mitochondrial membrane, ACS5. ACS1 is not detected in mitochondria
ACSl5 is the only isoform of long chain acyl-CoA synthetase partly located on mitochondria. Ad-ACSL-5, long chain acyl-CoA synthetase 5 overexpressed in rat hepatoma McRrdle-RG7777 cells mediated by adenovirus colocalizes to both mitochondria and endoplasmic reticulum
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
suppression of ACSL5 expression significantly decreases fatty acid-induced lipid droplet formation. ACSL5 knockdown results in decreased oleic acid or acetic acid incorporation into intracellular triacylglycerol, phospholipids, and cholesterol esters without altering fatty acid uptake or lipogenic gene expression. ACSL5 knockdown also decreases hepatic TAG secretion proportionate to the observed decrease in neutral lipid synthesis. ACSL5 knockdown does not alter lipid turnover or mediate the effects of insulin on lipid metabolism, phenotype, detailed overview
malfunction
-
knockdown of endogenous Acsl4 expression increases significantly the release of arachidonate metabolites, including prostaglandin E2, prostaglandin D2, and prostaglandin F2alpha, compared with replicated control cells, whereas knockdown of Acsl1 expression reduces the interleukin-1beta-induced release of arachidonate metabolites
malfunction
-
isoform ACSL6 genic inhibition in rat primary myotubes decreases lipid accumulation, as well as activates the higher mitochondrial oxidative capacity programme and fatty acid oxidation through the AMP-activated protein kinase/ peroxisome proliferator-activated receptor gamma coactivator 1-alpha pathway
physiological function
ACSL5 may have an anabolic role in lipid metabolism
physiological function
-
Acsl isozymes play distinct roles in the control of arachidonate remodeling in rat fibroblasts: isoform Acsl4 acts as the first step of enzyme for arachidonate remodeling following interleukin-1beta stimulation, and isoform Acsl1 is involved in the maintenance of some arachidonate-containing phosphatidylcholine species
physiological function
isoform Acsl1 overexpression prevents oxidative stress (nitrotyrosine, hydroxyoctadecadienoic acids) and attenuates cellular injury in Schwann cells following 12 h exposure to long chain fatty acids
physiological function
upregulation of isoform ACSL4 is responsible for the increase in polyunsaturated fatty acid-triacylglycerol species during activation of hepatic stellate cells, which may serve to protect cells against a shortage of polyunsaturated fatty acids required for eicosanoid secretion
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). ACBG1_RAT
721
0
80519
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
250000
-
aggregates quite readily to form species with MW of over 1 million, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
SDS-PAGE results in 4 protein components with MW 135000, 115000, 65000 and 55000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L399M
no significant alteration of activity compared to the wild type enzyme
S291Y
mutant prefers 20:5 and 22:6 substrates and has an increased Km for ATP
additional information
siRNA knockdown of ACSL5 in rat primary hepatocytes
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
2.5 min: 17-20% loss of activity, 5 min: 33-37% loss of activity, 15 min: 58-59% loss of activity
43
45
43
-
half-life: about 10 min for ACS1, shorter thah 1 min fpr ACS4 and about 4 min for ACS5
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to 24 h dialysis at 0EC, against 50 mM potassium phosphate buffer, pH 7.4, containing 2 mM Triton X-100, 2 mM DTT, 1 mM EDTA
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACS3, one of multiple forms of enzyme in brain, expression in COS cells
ectopical overexpression of ACSL5 in rat hepatoma McArdle-RH7777 cells
expression of isoenzyme ACS1 in PC12 cells. Overexpression of ACS1 increases the rate of oleic acid internalization by 55%, and arachidonic acid and docosahexaenoic acid uptake is increased by 25%, but there is no significant change in neurite outgrowth
expression of isoenzyme ACS2 in PC12 cells. Overexpression of ACS2 increases the rate of oleic acid internalization by 90%, arachidonic acid by 115%, docosahexaenoic acid by 70%. ACS2 enhances neurote outgrowth by promoting polyunsaturated fatty acid internalization
isoforms 1-5 of Rattus norvegicus long chain acyl-CoA synthetase are expressed in Escherichia coli. Specific activities are 1.6-20fold higher than wild-type control strain expressing FadD. Only ACS5 restores growth on oleate as the sole carbon source in Escherichia coli
isoforms 1-5 of Rattus norvegicus long chain acyl-CoA synthetase are expressed in Escherichia coli. Specific activities are 1.6-20fold higher than wild-type control strain expressing FadD. Only ACS5 restores growth on oleate as the sole carbon source in Escherichia coli fad
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coleman, R.A.; Rao, P.; Fogelsong, R.J.; Bardes, E.S.G.
2-Bromopalmitoyl-CoA and 2-bromopalmitate: promiscuous inhibitors of membrane-bound enzymes
Biochim. Biophys. Acta
1125
203-209
1992
Rattus norvegicus
Suzuki, H.; Kawarabayashi, Y.; Kondo, J.; Abe, T.; Hishikawa, K.; Kimura, S.; Hashimoto, T.; Yamamoto, T.
Structure and regulation of rat long-chain acyl-CoA synthetase
J. Biol. Chem.
265
8681-8685
1990
Rattus norvegicus
Hurtado del Catalfo, G.E.; De Gomez Dumm, I.N.T.; Mandon, E.C.
Long chain acyl-CoA synthetase of rat testis microsomes. Substrate specificity and hormonal regulation
Biochem. Mol. Biol. Int.
31
643-649
1993
Rattus norvegicus
Vanden Heuvel, J.P.; Kuslikis, B.I.; Shrago, E.; Peterson, R.E.
Inhibition of long-chain acyl-CoA synthetase by the peroxisome proliferator perfluorodecanoic acid in rat hepatocytes
Biochem. Pharmacol.
42
295-302
1991
Rattus norvegicus
Knights, K.M.; Jones, M.E.
Inhibition kinetics of hepatic microsomal long chain fatty acid-CoA ligase by 2-arylpropionic acid non-steroidal anti-inflammatory drugs
Biochem. Pharmacol.
43
1465-1471
1992
Rattus norvegicus
Wanders, R.J.A.; Denis, S.; Roermund, C.W.T.; Jakobs, C.; ten Brink, H.J.
Characteristics and subcellular localization of pristanoyl-CoA synthetase in rat liver
Biochim. Biophys. Acta
1125
274-279
1992
Rattus norvegicus
Fujino, T.; Kang, M.J.; Suzuki, H.; Iijima, H.; Yamamoto, T.
Molecular characterization and expression of rat acyl-CoA synthetase 3
J. Biol. Chem.
271
16748-16752
1996
Rattus norvegicus (Q63151)
Tomoda, H.; Igarashi, K.; Omura, S.
Inhibition of acyl-CoA synthetase by triacsins
Biochim. Biophys. Acta
921
595-598
1987
Pseudomonas aeruginosa, Rattus norvegicus
Haq, R.U.; Tsao, F.; Shrago, E.
Activity of long chain acyl-CoA synthetase in isolated alveolar type II cells
Biochim. Biophys. Acta
918
36-39
1987
Rattus norvegicus
Morisaki, N.; Kanzaki, T.; Saito, Y.; Yoshida, S.
Fatty acid specificity of acyl-CoA synthetase in rat glomeruli
Biochim. Biophys. Acta
875
311-315
1986
Rattus norvegicus
Miyazawa, S.; Hashimoto, T.; Yokota, S.
Identity of long-chain acyl-coenzyme A synthetase of microsomes, mitochondria, and peroxisomes in rat liver
J. Biochem.
98
723-733
1985
Rattus norvegicus
Noy, N.; Zakim, D.
Substrate specificity of fatty-acyl-CoA ligase in liver microsomes
Biochim. Biophys. Acta
833
239-244
1985
Rattus norvegicus
Reddy, T.S.; Sprecher, H.; Bazan, N.G.
Long-chain acyl-coenzyme A synthetase from rat liver brain microsomes. Kinetic studies using [1-14C]docosahexaenoic acid substrate
Eur. J. Biochem.
145
21-29
1984
Rattus norvegicus
Normann, P.T.; Norseth, J.; Flatmark, T.
Acyl-CoA synthetase activity of rat heart mitochondria. Substrate specificity with special reference to very-long-chain and isomeric fatty acids
Biochim. Biophys. Acta
752
474-481
1983
Rattus norvegicus
Mannaerts, G.P.; Van Veldhoven, P.; Van Broekhoven, A.; Vanderbroek, C.; Debeer, L.J.
Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane
Biochem. J.
204
17-23
1982
Rattus norvegicus
Tanaka, T.; Hosaka, K.; Numa, S.
Long-chain acyl-CoA synthetase from rat liver
Methods Enzymol.
71
334-341
1981
Rattus norvegicus
Normann, P.T.; Thomassen, M.S.; Christiansen, E.N.; Flatmark, T.
Acyl-CoA synthetase activity of rat liver microsomes. Substrate specificity with special reference to very-long-chain and isomeric fatty acids
Biochim. Biophys. Acta
664
416-427
1981
Rattus norvegicus
Philipp, D.P.; Parsons, P.
Kinetic characterization of long chain fatty acyl coenzyme A ligase from rat liver mitochondria
J. Biol. Chem.
254
10785-10790
1979
Rattus norvegicus
-
Philipp, D.P.; Parsons, P.
Isolation and purification of long chain fatty acyl coenzyme A ligase from rat liver mitochondria
J. Biol. Chem.
254
10776-10784
1979
Rattus norvegicus
Tanaka, T.; Hosaka, M.; Hoshimaru, M.; Numa, S.
Purification and properties of long-chain acyl-coenzyme -A synthetase from rat liver
Eur. J. Biochem.
98
165-172
1979
Rattus norvegicus
Marcel, Y.L.; Suzue, G.
Kinetic studies on the specificity of long chain acyl coenzyme A synthetase from rat liver microsomes
J. Biol. Chem.
247
4433-4436
1972
Rattus norvegicus
Brugger, R.; Reichel, C.; Garcia Alia, B.; Brune, K.; Yamamoto, T.; Tegeder, I.; Geissinger, G.
Expression of rat liver long-chain acyl-CoA synthetase and characterization of its role in the metabolism of R-ibuprofen and other fatty acid-like xenobiotics
Biochem. Pharmacol.
61
651-656
2001
Rattus norvegicus
Kim, J.H.; Lewin, T.M.; Coleman, R.A.
Expression and characterization of recombinant rat acyl-CoA synthetases 1, 4, and 5: selective inhibition by triacsin C and thiazolidinediones
J. Biol. Chem.
276
24667-24673
2001
Rattus norvegicus
Lewin, T.M.; Kim, J.H.; Granger, D.A.; Vance, J.E.; Coleman, R.A.
Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently
J. Biol. Chem.
276
24674-24679
2001
Rattus norvegicus
Tang, P.Z.; Tsai-Morris, C.H.; Dufau, M.L.
Cloning and characterization of a hormonally regulated rat long chain acyl-CoA synthetase
Proc. Natl. Acad. Sci. USA
98
6581-6586
2001
Rattus norvegicus (Q924N5)
Van Horn, C.G.; Caviglia, J.M.; Li, L.O.; Wang, S.; Granger, D.A.; Coleman, R.A.
Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6
Biochemistry
44
1635-1642
2005
Rattus norvegicus (P33124)
Achouri, Y.; Hegarty, B.D.; Allanic, D.; Becard, D.; Hainault, I.; Ferre, P.; Foufelle, F.
Long chain fatty acyl-CoA synthetase 5 expression is induced by insulin and glucose: involvement of sterol regulatory element-binding protein-1c
Biochimie
87
1149-1155
2005
Rattus norvegicus
Caviglia, J.M.; Li, L.O.; Wang, S.; DiRusso, C.C.; Coleman, R.A.; Lewin, T.M.
Rat long chain acyl-CoA synthetase 5, but not 1, 2, 3, or 4, complements Escherichia coli fadD
J. Biol. Chem.
279
11163-11169
2004
Rattus norvegicus, Rattus norvegicus (Q63151)
Marszalek, J.R.; Kitidis, C.; Dararutana, A.; Lodish, H.F.
Acyl-CoA synthetase 2 overexpression enhances fatty acid internalization and neurite outgrowth
J. Biol. Chem.
279
23882-23891
2004
Rattus norvegicus (P33124)
Marszalek, J.R.; Kitidis, C.; Dirusso, C.C.; Lodish, H.F.
Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism
J. Biol. Chem.
280
10817-10826
2005
Rattus norvegicus
Mashek, D.G.; McKenzie, M.A.; Van Horn, C.G.; Coleman, R.A.
Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglcyerol in McArdle-RH7777 cells
J. Biol. Chem.
281
945-950
2005
Rattus norvegicus, Rattus norvegicus (O88813)
Wang, Y.L.; Guo, W.; Zang, Y.; Yaney, G.C.; Vallega, G.; Getty-Kaushik, L.; Pilch, P.; Kandror, K.; Corkey, B.E.
Acyl coenzyme a synthetase regulation: putative role in long-chain acyl coenzyme a partitioning
Obes. Res.
12
1781-1788
2004
Rattus norvegicus
Parkes, H.A.; Preston, E.; Wilks, D.; Ballesteros, M.; Carpenter, L.; Wood, L.; Kraegen, E.W.; Furler, S.M.; Cooney, G.J.
Overexpression of acyl-CoA synthetase-1 increases lipid deposition in hepatic (HepG2) cells and rodent liver in vivo
Am. J. Physiol. Endocrinol. Metab.
291
E737-E744
2006
Rattus norvegicus (P18163), Homo sapiens (P33121), Homo sapiens, Mus musculus (P41216), Mus musculus
Durgan, D.J.; Smith, J.K.; Hotze, M.A.; Egbejimi, O.; Cuthbert, K.D.; Zaha, V.G.; Dyck, J.R.; Abel, E.D.; Young, M.E.
Distinct transcriptional regulation of long-chain acyl-CoA synthetase isoforms and cytosolic thioesterase 1 in the rodent heart by fatty acids and insulin
Am. J. Physiol. Heart Circ. Physiol.
290
H2480-H2497
2006
Mus musculus, Rattus norvegicus
Stinnett, L.; Lewin, T.M.; Coleman, R.A.
Mutagenesis of rat acyl-CoA synthetase 4 indicates amino acids that contribute to fatty acid binding
Biochim. Biophys. Acta
1771
119-125
2007
Rattus norvegicus (O35547)
Black, P.N.; DiRusso, C.C.
Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation
Biochim. Biophys. Acta
1771
286-298
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38137), Saccharomyces cerevisiae (P38225), Saccharomyces cerevisiae (P39518), Rattus norvegicus (O35547), Rattus norvegicus (O88813)
Li, L.O.; Mashek, D.G.; An, J.; Doughman, S.D.; Newgard, C.B.; Coleman, R.A.
Overexpression of rat long chain acyl-coa synthetase 1 alters fatty acid metabolism in rat primary hepatocytes
J. Biol. Chem.
281
37246-37255
2006
Rattus norvegicus (P18163)
Mashek, D.G.; Li, L.O.; Coleman, R.A.
Rat long-chain acyl-CoA synthetase mRNA, protein, and activity vary in tissue distribution and in response to diet
J. Lipid Res.
47
2004-2010
2006
Rattus norvegicus (O35547), Rattus norvegicus (O88813), Rattus norvegicus (P18163), Rattus norvegicus (P33124), Rattus norvegicus (Q63151)
Song, S.Y.; Kato, C.; Adachi, E.; Moriya-Sato, A.; Inagawa-Ogashiwa, M.; Umeda, R.; Hashimoto, N.
Expression of an acyl-CoA synthetase, lipidosin, in astrocytes of the murine brain and its up-regulation during remyelination following cuprizone-induced demyelination
J. Neurosci. Res.
85
3586-3597
2007
Rattus norvegicus
Li, J.; Sheng, Y.; Tang, P.Z.; Tsai-Morris, C.H.; Dufau, M.L.
Tissue-cell- and species-specific expression of gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain. Identification of novel forms in the brain
J. Steroid Biochem. Mol. Biol.
98
207-217
2006
Rattus norvegicus (Q63151), Mus musculus (Q99PU5), Mus musculus
Bu, S.Y.; Mashek, D.G.
Hepatic long-chain acyl-CoA synthetase 5 mediates fatty acid channeling between anabolic and catabolic pathways
J. Lipid Res.
51
3270-3280
2010
Rattus norvegicus (O88813)
Kuwata, H.; Yoshimura, M.; Sasaki, Y.; Yoda, E.; Nakatani, Y.; Kudo, I.; Hara, S.
Role of long-chain acyl-coenzyme A synthetases in the regulation of arachidonic acid metabolism in interleukin 1beta-stimulated rat fibroblasts
Biochim. Biophys. Acta
1841
44-53
2014
Rattus norvegicus
Hinder, L.; Figueroa-Romero, C.; Pacut, C.; Hong, Y.; Vivekanandan-Giri, A.; Pennathur, S.; Feldman, E.
Long-chain acyl coenzyme a synthetase 1 overexpression in primary cultured Schwann cells prevents long chain fatty acid-induced oxidative stress and mitochondrial dysfunction
Antioxid. Redox Signal.
21
588-600
2014
Rattus norvegicus (P18163)
Tuohetahuntila, M.; Spee, B.; Kruitwagen, H.S.; Wubbolts, R.; Brouwers, J.F.; van de Lest, C.H.; Molenaar, M.R.; Houweling, M.; Helms, J.B.; Vaandrager, A.B.
Role of long-chain acyl-CoA synthetase 4 in formation of polyunsaturated lipid species in hepatic stellate cells
Biochim. Biophys. Acta
1851
220-230
2015
Rattus norvegicus (O35547)
Teodoro, B.G.; Sampaio, I.H.; Bomfim, L.H.; Queiroz, A.L.; Silveira, L.R.; Souza, A.O.; Fernandes, A.M.; Eberlin, M.N.; Huang, T.Y.; Zheng, D.; Neufer, P.D.; Cortright, R.N.; Alberici, L.C.
Long-chain acyl-CoA synthetase 6 regulates lipid synthesis and mitochondrial oxidative capacity in human and rat skeletal muscle
J. Physiol.
595
677-693
2017
Rattus norvegicus, Homo sapiens (Q9UKU0), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 6.2.1.3)
Transporter Classification Database (TCDB): 4.C.1.1.4, 4.C.1.1.15, 4.C.1.1.9, 4.C.1.1.5, 4.C.1.1.12, 4.C.1.1.10, 4.C.1.1.1, 4.C.1.1.13, 4.C.1.1.8, 4.C.1.1.11, 4.C.1.1.3, 4.C.1.1.14
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