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ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
ATP + (R)-ibuprofen + CoA
AMP + diphosphate + (R)-ibuprofenoyl-CoA
ATP + 1,12-dodecanedioic acid + CoA
AMP + diphosphate + ?
-
-
-
?
ATP + 20:3(n-6) fatty acid + CoA
?
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
ATP + elaidate + CoA
AMP + diphosphate + elaiodyl-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 + laurate + CoA
AMP + diphosphate + lauroyl-CoA
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
ATP + linolenate + CoA
AMP + diphosphate + linolenoyl-CoA
-
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
ATP + palmitoleate + CoA
AMP + diphosphate + palmitoleoyl-CoA
-
-
-
-
?
ATP + pristanic acid + CoA
AMP + diphosphate + pristanoyl-CoA
-
-
-
?
ATP + stearate + CoA
AMP + diphosphate + stearoyl-CoA
-
-
-
-
?
dATP + fatty acid + CoA
dAMP + diphosphate + acyl-CoA
-
-
-
-
?
additional information
?
-
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-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
-
-
-
?
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 + laurate + CoA
AMP + diphosphate + lauroyl-CoA
-
-
-
-
?
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
-
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-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 + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
-
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
20% of the activity with palmitate
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
?
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
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-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
-
-
?
additional information
?
-
no activity for lignoceric acid
-
-
?
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Triacsin C
IC50: 0.0055 mM
(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
Brij 58
-
maximal inhibition at 4% detergent
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
docosahexaenoate
-
unlabeled, inhibition of docosahexaenoate activation
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
eicosapentaenoate
-
inhibition of palmitoyl-CoA synthesis
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
Ketoprofen
-
non-competitive inhibition of the high affinity isoform
linoleate
-
inhibition of palmitoyl-CoA synthesis
linolenate
-
inhibition of palmitoyl-CoA synthesis
naproxen
-
non-competitive inhibition of the high affinity isoform
oleate
-
inhibition of palmitoyl-CoA synthesis
palmitate
-
linolenic acid activation
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
R-Fenoprofen
-
mixed inhibition of the high affinity isoform
R-Ibuprofen
-
mixed inhibition of the high affinity isoform
sodium cholate
-
maximal inhibition at 1% detergent
thiazolidinediones
-
specific inhibitors of ACS4
triacsin
-
competitive inhibitor of both ACS1 and ACS4
Triacsin A
-
non-competitive with respect to ATP and coenzyme A
Tween 80
-
maximal inhibition at 4% detergent
Zwittergent 3-12
-
inhibition below the critical micellar concentration, 0.12%. below this concentrations no inhibition
arachidonate
-
-
arachidonate
-
inhibition of palmitoyl-CoA synthesis
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
NEM
-
ACS4
NEM
-
strongly inhibits ACS5 and weakly inhibits ACS1, no effect on ACS5
rosiglitazone
-
rosiglitazone
-
IC50: 0.0005 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
Triacsin C
-
-
Triacsin C
-
strongly inhibits ACS1 and ACS4, no effect on ACS5
Triton X-100
-
Triton X-100
-
maximal inhibition at 4% detergent
Triton X-100
-
slight inhibition when incubated with microsomes at 0°C for 30 min
troglitazone
-
ACS4
troglitazone
-
IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
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
-
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
-
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
Tomoda, H.; Igarashi, K.; Omura, S.
Inhibition of acyl-CoA synthetase by triacsins
Biochim. Biophys. Acta
921
595-598
1987
Pseudomonas aeruginosa, Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
Noy, N.; Zakim, D.
Substrate specificity of fatty-acyl-CoA ligase in liver microsomes
Biochim. Biophys. Acta
833
239-244
1985
Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
Tanaka, T.; Hosaka, K.; Numa, S.
Long-chain acyl-CoA synthetase from rat liver
Methods Enzymol.
71
334-341
1981
Rattus norvegicus
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda