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Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase
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EC Tree
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 enzyme appears in 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACS
ACS1
ACS2
ACS3
ACS4
AcsA
ACSL
ACSL1
ACSL3
ACSL4
ACSL5
ACSL6
ACSL6_v1
ACSL6_v2
Acyl coenzyme A synthetase
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Acyl-CoA ligase
-
-
-
-
Acyl-CoA synthetase
Acyl-CoA synthetase 3
-
-
-
-
acyl-CoA synthetase 4
acyl-CoA synthetase 5
acyl-CoA synthetase-1
Acyl-coenzyme A ligase
-
-
-
-
BGR
bubblegum-related protein
FAA1
-
-
-
-
Faa1p
Facl1
Facl2
FACS
FAdD
FadD2
FATP
FATP4
Fatty acid CoA ligase
-
-
-
-
fatty acid CoA synthetase, AMP forming
Fatty acid thiokinase (long chain)
-
-
-
-
fatty acid transport protein
fatty acyl-CoA synthetase
Fatty acyl-coenzyme A synthetase
-
-
-
-
Fatty-acyl-CoA ligase
-
-
-
-
GR-LACS
LACS
LACS1
LACS2
LC-FACS
LCFA synthetase
-
-
-
-
lipidosin
long chain acyl-CoA synthetase
long chain acyl-CoA synthetase 1
long chain acyl-CoA synthetase 3
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 coenzyme A synthetase 1
long-chain acyl-CoA synthetase
long-chain acyl-CoA synthetase 4
long-chain acyl-CoA synthetase 6
Long-chain acyl-CoA synthetase I
-
-
-
-
Long-chain acyl-CoA synthetase II
-
-
-
-
Long-chain acyl-coenzyme A synthetase
long-chain fatty acid CoA ligase
long-chain fatty acyl coenzyme A ligase
Long-chain fatty acyl coenzyme A synthetase
-
-
-
-
long-chain polyunsaturated fatty acid acyl-coenzyme A synthetase
-
-
luciferase-like protein
mACS4
-
-
-
-
Oleoyl-CoA synthetase
-
-
-
-
Palmitoyl coenzyme A synthetase
-
-
-
-
Palmitoyl-CoA ligase
-
-
-
-
Palmityl-coenzyme A synthetase
-
-
-
-
Pristanoyl-CoA synthetase
-
-
-
-
Stearoyl-CoA synthetase
-
-
-
-
TbACS3
Thiokinase
-
-
-
-
additional information
ACS3
-
-
-
-
ACSL3
specifically required for incorporation of fatty acids into phosphatidylcholine
ACSL4
prefers longer chain polyunsaturated fatty acids as substrates
Acyl-CoA synthetase
-
-
-
-
FATP4
-
bifunctional enzyme, exhibiting both fatty acid transport and acyl-CoA synthetase activities
fatty acid transport protein
-
bifunctional enzyme, exhibiting both fatty acid transport and acyl-CoA synthetase activities
LACS
-
-
-
-
Long-chain acyl CoA synthetase
-
-
-
-
Long-chain acyl-coenzyme A synthetase
-
-
-
-
additional information
-
the enzyme belongs to a fatty acyl-CoA synthetase family, which is distinct from the known long-chain fatty acyl-CoA synthetase, LACS, and the 4-coumarate:CoA ligase, 4CL, families, overview
additional information
-
the enzyme is a member of the ACSL gene family that catalyzes the activation of long-chain fatty acids for lipid biosynthesis
additional information
the enzyme is a part of a larger AMP-forming superfamily
additional information
acyl-CoA synthetase belongs to the superfamily of adenylate-forming enzymes, whose three-dimensional structures are analogous to one another
additional information
acyl-CoA synthetase belongs to the superfamily of adenylate-forming enzymes, whose three-dimensional structures are analogous to one another
-
additional information
-
the enzyme is a part of a larger AMP-forming superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + a long-chain fatty 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
-
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + a long-chain fatty acyl-CoA
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
Phosphorylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, , , arachidonate biosynthesis, arachidonate biosynthesis, ceramide biosynthesis, ceramide biosynthesis, Fatty acid degradation, Fatty acid degradation, Fatty acid degradation, Fatty acid degradation, Fatty acid degradation, lipid metabolism, lipid metabolism, lipid metabolism, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation, octane oxidation
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9013-18-7
-
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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
ATP + (11Z)-eicosenoate + CoA
AMP + diphosphate + (11Z)-eicosenoyl-CoA
-
-
?
ATP + (15Z)-tetracosenoate + CoA
AMP + diphosphate + (15Z)-tetracosenoyl-CoA
-
-
?
ATP + (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + CoA
AMP + diphosphate + (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA
-
-
?
ATP + (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA
AMP + diphosphate + (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA
-
-
?
ATP + (6Z)-octadecenoate + CoA
AMP + diphosphate + (6Z)-octadecenoyl-CoA
-
-
?
ATP + (6Z,12Z, 15Z)-octadecatrienoate + CoA
AMP + diphosphate + (6Z,12Z,15Z)-octadecatrienoyl-CoA
-
-
?
ATP + (6Z,9Z,12Z)-octadecatrienoate + CoA
AMP + diphosphate + (6Z,9Z,12Z)-octadecatrienoyl-CoA
-
-
?
ATP + (9E)-octadecenoate + CoA
AMP + diphosphate + (9E)-octadecenoyl-CoA
-
-
?
ATP + (9Z)-hexadecenoate + CoA
AMP + diphosphate + (9Z)-hexadecenoyl-CoA
-
-
?
ATP + (9Z)-octadecenoate + CoA
AMP + diphosphate + (9Z)-octadecenoyl-CoA
-
-
?
ATP + (9Z)-tetradecenoate + CoA
AMP + diphosphate + (9Z)-tetradecenoyl-CoA
-
-
?
ATP + (9Z,12Z)-octadecadienoate + CoA
AMP + diphosphate + (9Z,12Z)-octadecadienoyl-CoA
-
-
?
ATP + 12-oxo-phytodienoic acid + CoA
AMP + diphosphate + 12-oxo-phytodienoyl-CoA
-
-
-
-
?
ATP + 16-hydroxypalmitic acid + CoA
AMP + diphosphate + 16-hydroxypalmitoyl-CoA
-
isoenzyme LACS2
-
-
?
ATP + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-hexanoic acid + CoA
AMP + diphosphate + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-hexanoyl-CoA
-
-
-
-
?
ATP + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-octanoic acid + CoA
AMP + diphosphate + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-octanoyl-CoA
-
preferred substrate
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain fatty acyl-CoA
-
-
-
-
?
ATP + alpha-linoleate + CoA
AMP + diphosphate + alpha-linoleoyl-CoA
-
best substrate
-
-
?
ATP + behenoate + CoA
AMP + diphosphate + behenoyl-CoA
-
isoform Facl1 exhibits about 20% activity and isoform Facl2 exhibits about 65% activity
-
-
?
ATP + caproate + CoA
AMP + diphosphate + caproyl-CoA
-
most preferred substrate for isoform Facl1 (100% activity)
-
-
?
ATP + capryloate + CoA
AMP + diphosphate + capryloyl-CoA
-
isoform Facl1 exhibits about 50% activity and isoform Facl2 exhibits about 45% activity
-
-
?
ATP + dihomo-gamma-linolenate + CoA
AMP + diphosphate + dihomo-gamma-linolenoyl-CoA
-
-
-
?
ATP + dinor-12-oxo-phytodienoic acid + CoA
AMP + diphosphate + dinor-12-oxo-phytodienoyl-CoA
-
-
-
-
?
ATP + eicosadienoate + CoA
AMP + diphosphate + eicosadienoyl-CoA
-
-
-
?
ATP + eicosanoate + CoA
AMP + diphosphate + eicosanoyl-CoA
preferred substrate of isoform ACSL4
-
-
?
ATP + fatty acid + N6-etheno-CoA
AMP + diphosphate + acyl-N6-etheno-CoA
-
-
-
-
?
ATP + hexacosanoate + CoA
AMP + diphosphate + hexacosanoyl-CoA
-
isoform Facl1 exhibits about 8% activity and isoform Facl2 exhibits about 23% activity
-
-
?
ATP + hexadecatrienoate + CoA
AMP + diphosphate + hexadecatrienoyl-CoA
-
-
-
-
?
ATP + laurate + CoA
AMP + diphosphate + lauryl-CoA
-
isoform Facl1 exhibits about 90% activity and isoform Facl2 exhibits about 55% activity
-
-
?
ATP + lignocerate + CoA
AMP + diphosphate + lignoceryl-CoA
-
isoform Facl1 exhibits about 20% activity and isoform Facl2 exhibits about 30% activity
-
-
?
ATP + linoleic acid + CoA
AMP + diphosphate + linoleoyl-CoA
-
-
-
?
ATP + melissoate + CoA
AMP + diphosphate + melissoyl-CoA
-
isoform Facl1 exhibits about 3% activity and isoform Facl2 exhibits about 1% activity
-
-
?
ATP + n-tetracosanoic acid + CoA
AMP + diphosphate + n-tetracosanoyl-CoA
-
-
-
-
?
ATP + octacosanoate + CoA
AMP + diphosphate + octacosanoyl-CoA
-
isoform Facl1 exhibits about 5% activity and isoform Facl2 exhibits about 3% activity
-
-
?
ATP + stearate + CoA
AMP + diphosphate + stearyl-CoA
-
isoform Facl1 exhibits about 45% activity and isoform Facl2 exhibits about 75% activity
-
-
?
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 carboxylate + CoA
AMP + diphosphate + an acyl-CoA
-
-
-
-
?
ATP + a long-chain carboxylate + CoA
AMP + diphosphate + an acyl-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 + 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 + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
the enzyme can elongate and desaturate fatty acids up to 22:6
-
-
?
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 + a long-chain fatty acid + CoA
AMP + diphosphate + an acyl-CoA
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + an acyl-CoA
-
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
isoform Facl1 exhibits less than 10% activity and isoform Facl2 exhibits about 20% activity
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
isoform Facl1 exhibits less than 10% activity and isoform Facl2 exhibits about 20% activity
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
isoform Facl1 exhibits about 40% activity and isoform Facl2 exhibits about 60% activity
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
isoform Facl1 exhibits about 40% activity and isoform Facl2 exhibits about 60% activity
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
preferred substrate
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
preferred substrate of isoform ACSL4
-
-
?
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
-
-
?
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 + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
isoform Facl1 exhibits about 20% activity and isoform Facl2 exhibits about 40% activity
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
-
isoform Facl1 exhibits about 20% activity and isoform Facl2 exhibits about 40% activity
-
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
-
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
preferred substrate of isoform ACSL6
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
second best substrate
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
-
?
ATP + docosahexaenoate + CoA
AMP + diphosphate + docosahexaenoyl-CoA
-
-
-
?
ATP + dodecanoate + CoA
AMP + diphosphate + dodecanoyl-CoA
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
best substrate
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
best substrate
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
-
?
ATP + eicosapentaenoate + CoA
AMP + diphosphate + eicosapentaenoyl-CoA
-
-
-
?
ATP + fatty acid + 4'-phosphopantetheine
AMP + diphosphate + acyl-4'-phosphopantetheine
-
-
-
-
?
ATP + fatty acid + 4'-phosphopantetheine
AMP + diphosphate + acyl-4'-phosphopantetheine
-
-
-
-
?
ATP + fatty acid + dephospho-CoA
AMP + diphosphate + acyl-dephospho-CoA
-
-
-
?
ATP + fatty acid + dephospho-CoA
AMP + diphosphate + acyl-dephospho-CoA
-
-
-
-
?
ATP + fatty acid + dephospho-CoA
AMP + diphosphate + acyl-dephospho-CoA
-
-
-
-
?
ATP + fatty acid + pantetheine
AMP + diphosphate + acyl-pantetheine
-
-
-
-
?
ATP + fatty acid + pantetheine
AMP + diphosphate + acyl-pantetheine
-
-
-
-
?
ATP + heptadecanoate + CoA
AMP + diphosphate + heptadecanoyl-CoA
-
-
-
?
ATP + hexadecanoate + CoA
AMP + diphosphate + hexadecanoyl-CoA
-
-
?
ATP + hexadecanoate + CoA
AMP + diphosphate + hexadecanoyl-CoA
-
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
4% of the activity with palmitate
-
?
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
-
-
-
?
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
-
high activity
-
-
?
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
-
high activity
-
-
?
ATP + lignocerate + CoA
AMP + diphosphate + lignoceroyl-CoA
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
-
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
enzyme plays a pivotal role in cellular homeostasis, particular in lipid metabolism
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
activates exogenous long-chain fatty acids concomitant with their transport across the inner membrane into metabolically active CoA thioesters
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
essential role in animal cell proliferation
-
-
?
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
?
-
at 36°C the enzyme is required for the utilization of exogenous myristate by the N-myristoyltransferase. This requirement is not apparent at 24°C or 30°C, suggesting that another acylCoA synthetase activity with differing chain length and/or temperature optima exists
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
acyl-CoA synthetase I is responsible for the production of long-chain acyl-CoA that is utilized solely for the synthesis of cellular lipids, while the acyl-CoA synthetase II provides long-chain acyl-CoA that is exclusively degraded via beta-oxidation
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
no activity with 18:1 and 22:1 fatty acid
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
active on fatty acids with chain length of 6 to 18 carbon atoms, and a maximum activity with laurate. Low affinity for the fatty acids C6 to C8
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
trans-DELTA9-18:1 fatty acid
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
trans-DELTA9-16:1 fatty acid
-
-
?
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 + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
Ulmus sp.
-
no activity with 18:1 and 22:1 fatty acid
-
-
?
ATP + long-chain carboxylic acid + CoA
AMP + diphosphate + long-chain acyl-CoA
-
utilizes straight-chain fatty acids with 14-18 carbon atoms regardless of the degree of unsaturation. Straight-chain fatty acids containing more than 18 or fewer than 14 carbon atoms, as well as 16-hydroxypalmitic acid and hexadecanedioic acid are ineffective. Acyl-CoA synthetase II has a broader fatty acid specificity than acyl-CoA synthetase I. The effective substrates include long-chain dicarboxylic acids
-
-
?
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
-
no activity with 18:1 and 22:1 fatty acid
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
isoform Facl1 exhibits about 65% activity and isoform Facl2 exhibits about 85% activity
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
-
-
?
ATP + o-succinyl-1-benzoate + CoA
AMP + diphosphate + o-succinyl-1-benzoyl-CoA
-
a step in the bacterial biosynthesis of menaquinone from chorismate, pathway overview
-
-
?
ATP + o-succinyl-1-benzoate + CoA
AMP + diphosphate + o-succinyl-1-benzoyl-CoA
-
a two-step reaction via o-succinyl-1-benzoyl-AMP intermediate
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-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
-
isoform LACS7 has a much higher ratio of oleoyl-CoA to octanoyl-CoA synthetase activity compared to isoform LCS6
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
preferred substrate of isoform ACSL3
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
high activity
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
high activity
-
-
?
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
-
most preferred substrate for isoform Facl2 (100% activity)
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
most preferred substrate for isoform Facl2 (100% activity)
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
highest activity on palmitate
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
highest activity on palmitate
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
highest activity
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
-
highest activity
-
-
?
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 + palmitoleate + CoA
AMP + diphosphate + palmitoleoyl-CoA
-
-
-
-
?
ATP + palmitoleate + CoA
AMP + diphosphate + palmitoleoyl-CoA
-
-
-
?
ATP + pentadecanoate + CoA
AMP + diphosphate + pentadecanoyl-CoA
-
-
-
?
ATP + stearate + CoA
AMP + diphosphate + stearoyl-CoA
-
-
-
?
ATP + tetradecanoate + CoA
AMP + diphosphate + tetradecanoyl-CoA
-
-
?
ATP + tetradecanoate + CoA
AMP + diphosphate + tetradecanoyl-CoA
-
-
-
?
ATP + tridecanoate + CoA
AMP + diphosphate + tridecanoyl-CoA
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
additional information
?
-
-
lacs2-1 mutation results in a defective cutin layer
-
-
?
additional information
?
-
-
peroxisomal acyl-CoA synthetase activity is essential for seedling development
-
-
?
additional information
?
-
-
the OPC-8:CoA ligase catalyses an essential step in jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of the carboxylic acid side chain of its precursors, and, in accordance with this function, the protein is localized in peroxisomes
-
-
?
additional information
?
-
-
enzyme family members display activity towards different biosynthetic precursors of jasmonic acid, including 12-oxo-phytodienoic acid, i.e. OPDA, dinor-OPDA, 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-octanoic acid, i.e. OPC-8, and OPC-6, substrate specificity of protein At1g20510 readily converting OPDA, dnOPDA, OPC-8, OPC-6, and myristic acid, OPC-8 is the preferred substrate, overview
-
-
?
additional information
?
-
-
Arabidopsis isoforms LACS1-3 display broad substrate specificities, ranging from saturated and monounsaturated C16, C18 and C20 fatty acids to saturated very-long-chain fatty acids
-
-
?
additional information
?
-
the enzyme ACS6 preferrs long-chain fatty acids that contain a cis-9 double bond
-
?
additional information
?
-
-
the enzyme plays a central role in intermediary metabolism by catalyzing the formation of acyl-CoA. The enzyme functions in the vectorial movement of exogenous fatty acids across the plasma membrane by acting as a metabolic trap, which results in the formation of acyl-CoA esters
-
?
additional information
?
-
-
fatty acyl-CoA synthetase facilitates long chain fatty acid permeation of the inner membrane by a vectorial thioesterification
-
-
?
additional information
?
-
-
unsaturated fatty acids such as 14:1, 16:1, 18:1, 22:1, 18:3(n-3), 20:3(n-6) fatty acids and arachidonic acid are no substrates of isoform Facl1 or Facl2
-
-
?
additional information
?
-
-
unsaturated fatty acids such as 14:1, 16:1, 18:1, 22:1, 18:3(n-3), 20:3(n-6) fatty acids and arachidonic acid are no substrates of isoform Facl1 or Facl2
-
-
?
additional information
?
-
-
the regulation of the FACL3/ACS3 expression by vitamin D3 is mediated by both androgen and androgen receptor, and suggests that increased FACL3/ACS3 expression by vitamin D3 is one of the components associated with antiproliferative effect of 1alpha,25(OH)2D3 in androgen receptor-positive prostate cancer LNCaP cells
-
-
?
additional information
?
-
-
octanoate and decanoate are ineffective substrates
-
-
?
additional information
?
-
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
?
additional information
?
-
-
lipidosin may mediate the link between adrenoleukodystrophy protein dysfunction and the impairment of fatty acid metabolism in Xlinked adrenoleukodystrophy
-
?
additional information
?
-
-
in vivo the loss of FATP4-mediated very long chain fatty acid uptake and/or esterification may underlie the null phenotype
-
-
?
additional information
?
-
-
inhibition of ACSL1 activity in adipocytes impairs fatty acid uptake, suggesting that esterification is essential for fatty acid transport. A constitutive interaction between the fatty acid transport protein FATP1 and ACSL1 contributes to efficient cellular uptake of long chain fatty acids in adipocytes through vectorial acylation
-
-
?
additional information
?
-
-
transcription of GR-LACS gene requires an Sp1/Sp3 binding element downstream of the transcriptional start sites which is essential for basal activity
-
-
?
additional information
?
-
-
the acyl-CoA synthetase is involved in bacterial menaquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme shows very low activity with acetate, propionate, butyrate, valerate, and caprylate
-
-
?
additional information
?
-
-
the enzyme shows very low activity with acetate, propionate, butyrate, valerate, and caprylate
-
-
?
additional information
?
-
low activity with caprate, laurate, myristate, eicosanoate, and docosanoate
-
-
?
additional information
?
-
low activity with caprate, laurate, myristate, eicosanoate, and docosanoate
-
-
?
additional information
?
-
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
?
additional information
?
-
firefly luciferase has two catalytic functions, it can act as a monooxygenase, luciferase, EC 1.13.12.7, but can also synthesize a long-chain fatty acyl-CoA from various long-chain fatty acids in the presence of ATP, CoA and Mg2+
-
-
?
additional information
?
-
FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids
-
-
?
additional information
?
-
FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids
-
-
?
additional information
?
-
-
FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids
-
-
?
additional information
?
-
the enzyme also forms a carbon-nitrogen bond, reaction of EC 6.3.1 acid-ammonia (or amide) ligase, i.e. amide synthase, and EC 6.3.2 acid-amino acid ligase, i.e. peptide synthase, comprising the amino group of the cysteine and the carboxyl group of the acid, overview
-
-
?
additional information
?
-
the enzyme also forms a carbon-nitrogen bond, reaction of EC 6.3.1 acid-ammonia (or amide) ligase, i.e. amide synthase, and EC 6.3.2 acid-amino acid ligase, i.e. peptide synthase, comprising the amino group of the cysteine and the carboxyl group of the acid, overview
-
-
?
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
?
-
-
luciferase shows beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea
-
-
?
additional information
?
-
-
TbACS1 prefers saturated fatty acids in the range undecanoate to tetradecanoate, TbACS3 and 4, which have 95% sequence identity, have similar specificities favouring fatty acids between tetradecanoate and heptadecanoate. In addition TbACS1, 3 and 4 function well with a variety of unsaturated fatty acids
-
?
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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
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 fatty acyl-CoA
-
-
-
-
?
ATP + o-succinyl-1-benzoate + CoA
AMP + diphosphate + o-succinyl-1-benzoyl-CoA
-
a step in the bacterial biosynthesis of menaquinone from chorismate, pathway overview
-
-
?
ATP + a long-chain carboxylate + CoA
AMP + diphosphate + an acyl-CoA
-
-
-
-
?
ATP + a long-chain carboxylate + CoA
AMP + diphosphate + an acyl-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 + 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 + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain acyl-CoA
the enzyme can elongate and desaturate fatty acids up to 22:6
-
-
?
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 + a long-chain fatty acid + CoA
AMP + diphosphate + an acyl-CoA
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + an acyl-CoA
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
preferred substrate
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
-
preferred substrate
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
enzyme plays a pivotal role in cellular homeostasis, particular in lipid metabolism
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
activates exogenous long-chain fatty acids concomitant with their transport across the inner membrane into metabolically active CoA thioesters
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
essential role in animal cell proliferation
-
-
?
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
?
-
at 36°C the enzyme is required for the utilization of exogenous myristate by the N-myristoyltransferase. This requirement is not apparent at 24°C or 30°C, suggesting that another acylCoA synthetase activity with differing chain length and/or temperature optima exists
-
-
?
ATP + long-chain carboxylic acid + CoA
?
-
acyl-CoA synthetase I is responsible for the production of long-chain acyl-CoA that is utilized solely for the synthesis of cellular lipids, while the acyl-CoA synthetase II provides long-chain acyl-CoA that is exclusively degraded via beta-oxidation
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
additional information
?
-
-
lacs2-1 mutation results in a defective cutin layer
-
-
?
additional information
?
-
-
peroxisomal acyl-CoA synthetase activity is essential for seedling development
-
-
?
additional information
?
-
-
the OPC-8:CoA ligase catalyses an essential step in jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of the carboxylic acid side chain of its precursors, and, in accordance with this function, the protein is localized in peroxisomes
-
-
?
additional information
?
-
-
the enzyme plays a central role in intermediary metabolism by catalyzing the formation of acyl-CoA. The enzyme functions in the vectorial movement of exogenous fatty acids across the plasma membrane by acting as a metabolic trap, which results in the formation of acyl-CoA esters
-
?
additional information
?
-
-
fatty acyl-CoA synthetase facilitates long chain fatty acid permeation of the inner membrane by a vectorial thioesterification
-
-
?
additional information
?
-
-
the regulation of the FACL3/ACS3 expression by vitamin D3 is mediated by both androgen and androgen receptor, and suggests that increased FACL3/ACS3 expression by vitamin D3 is one of the components associated with antiproliferative effect of 1alpha,25(OH)2D3 in androgen receptor-positive prostate cancer LNCaP cells
-
-
?
additional information
?
-
-
lipidosin may mediate the link between adrenoleukodystrophy protein dysfunction and the impairment of fatty acid metabolism in Xlinked adrenoleukodystrophy
-
?
additional information
?
-
-
in vivo the loss of FATP4-mediated very long chain fatty acid uptake and/or esterification may underlie the null phenotype
-
-
?
additional information
?
-
-
inhibition of ACSL1 activity in adipocytes impairs fatty acid uptake, suggesting that esterification is essential for fatty acid transport. A constitutive interaction between the fatty acid transport protein FATP1 and ACSL1 contributes to efficient cellular uptake of long chain fatty acids in adipocytes through vectorial acylation
-
-
?
additional information
?
-
-
transcription of GR-LACS gene requires an Sp1/Sp3 binding element downstream of the transcriptional start sites which is essential for basal activity
-
-
?
additional information
?
-
-
the acyl-CoA synthetase is involved in bacterial menaquinone biosynthesis
-
-
?
additional information
?
-
firefly luciferase has two catalytic functions, it can act as a monooxygenase, luciferase, EC 1.13.12.7, but can also synthesize a long-chain fatty acyl-CoA from various long-chain fatty acids in the presence of ATP, CoA and Mg2+
-
-
?
additional information
?
-
FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids
-
-
?
additional information
?
-
FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids
-
-
?
additional information
?
-
-
FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids
-
-
?
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
?
-
-
luciferase shows beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
isoform Facl1 shows 156% activity and isoform Facl2 shows 193% activity at 1 mM
Mg2+
salts
-
at low concentrations all salts, including the chaotropic salts, e.g. NaNO3, NaClO4 and KSCN, and thelyotropic salts, e.g. (NH4)2SO4 and potassium phosphate are equally effective in activation. At higher concentrations the chaotropic salts inhibit the enzyme activity. Activity can be recovered by dilution
additional information
-
K+, NH4+ and Na+ show no effects on the enzyme activity
Mg2+
-
high affinity triacsin C inhibition of both mitochondrial and microsomal enzyme form requires high concentrations of free Mg2+. Low affinity triacsin C inhibition is also enhanced by low Mg2+
Mg2+
-
maximal activity at 15-20 mM MgCl2, no inhibition at higher concentrations
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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
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
-
mechanism of covalent inhibition
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]hexa-1,5-dien-1-yl]sulfonyl)amino]adenosine
-
mechanism of covalent inhibition
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
-
mechanism of covalent inhibition
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)amino]adenosine
-
mechanism of covalent inhibition
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
-
mechanism of covalent inhibition
5'-O-([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)adenosine
-
mechanism of covalent inhibition
Ag+
-
isoform Facl1 shows 64% residual activity and isoform Facl2 shows 71% residual activity at 1 mM
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
Cu2+
-
isoform Facl1 shows 64% residual activity and isoform Facl2 shows 33% residual activity at 1 mM
EDTA
-
isoform Facl1 shows 12% residual activity and isoform Facl2 shows 26% residual activity at 1 mM
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
Fe2+
-
isoform Facl1 shows 57% residual activity and isoform Facl2 shows 36% residual activity at 1 mM
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
Mn2+
-
isoform Facl1 shows 28% residual activity and isoform Facl2 shows 40% residual activity at 1 mM
Ni2+
-
isoform Facl1 shows 1.3% residual activity and isoform Facl2 shows no activity at 1 mM
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
salts
-
at higher concentrations the chaotropic salts inhibit the enzyme activity, activity can be recovered by dilution. At low concentrations all salts, including the chaotropic salts and thelyotropic salts are equally effective in activation
-
Triacsins
-
hierarchy of inhibitory potency in decreasing order: triacsin C, triacsin A, triacsin D/ triacsin B
Zn2+
-
isoform Facl1 shows 13% residual activity and isoform Facl2 shows 0.36% residual activity at 1 mM
Zwittergent 3-12
-
inhibition below the critical micellar concentration, 0.12%. below this concentrations no inhibition
arachidonate
inhibits palmitoyl-CoA synthesis at high concentrations
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
fatty acids
-
palmitoleate, oleate and linoleate are competitive inhibitors of the activation of each other
rosiglitazone
-
IC50: 0.0005 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
SDS
-
isoform Facl1 shows 1.3% residual activity and isoform Facl2 shows 2.6% residual activity at 0.05% (w/v)
Triacsin A
-
isolated from the culture filtrate of Streptomyces sp. SK-1894, the anti-atherosclerotic agent acts as selective enzyme inhibitor, it inhibits the synthesis of cholesteryl ester and triacylglycerol in peritoneal macrophages
Triacsin C
-
competitive inhibitor of palmitate binding for microsomal and mitochondrial enzyme, uncompetitive inhibitor versus CoA. Biphasic Dixon plot, a high-affinity site with a Ki of 0.0001 mM accounts for a maximum of 70% of the inhibition. A low affinity site with a Ki of 0.006 mM accounts for a maximum of 30% inhibition
Triacsin C
-
i.e. 1-hydroxy-3-(E,E,E-2',4',7'-undecatrienylidine)triazene, potent competitive inhibitor
Triacsin C
-
in intact cultured cells the inhibition of arachidonoyl-CoA synthetase, EC 6.2.1.15, is much greater than the inhibition of nonspecific acyl-CoA synthetase
Triacsin C
-
no effect on FATP4 acyl-CoA synthetase activity towards n-tetracosanoic acid, inhibits activity with palmitate with IC50 of 0.03 mM
Triacsin C
-
isolated from the culture filtrate of Streptomyces sp. SK-1894, the anti-atherosclerotic agent acts as selective enzyme inhibitor, it inhibits the synthesis of cholesteryl ester and triacylglycerol in peritoneal macrophages
Triton X-100
-
Inhibition of acyl-CoA formation, inhibits ACSL6 isoform 2 (F-Gate) and its N-terminus truncated version, DELTAN-(F-Gate)
Triton X-100
-
slight inhibition when incubated with microsomes at 0°C for 30 min
troglitazone
-
no effect on FATP4 acyl-CoA synthetase activity towards n-tetracosanoic acid up to 0.05 mM, inhibits activity with palmitate with IC50 of 0.02 mM
troglitazone
-
IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein
additional information
-
not inhibited by 4,4,10 beta-trimethyl-trans-decal-3 beta-ol
-
additional information
-
an ACSL6 construct with a tag at its C-terminus has a far lower activity than a construct with a tag fused to its N-terminus
-
additional information
not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C
-
additional information
not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C
-
additional information
not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C
-
additional information
not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C
-
additional information
not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C
-
additional information
-
not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C
-
additional information
-
design and construction of mechanism-based inhibitors of MenE
-
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; 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; 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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triacsin C
ACSL activity is 17fold higher in the presence of 0.02 mM triacsin C
Triton X-100
-
isoform Facl1 shows 1.3% activity and isoform Facl2 shows 232% activity at 1% (v/v)
additional information
-
specific Gate-domain residues are essential for activity, detailed overview
-
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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
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
biphasic Dixon plot with the inhibitor triacsin C. A high-affinity site with a Ki of 0.0001 mM accounts for a maximum of 70% of the inhibition. A low affinity site with a Ki of 0.006 mM accounts for a maximum of 30% inhibition
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0057
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine
Mycobacterium tuberculosis
-
-
0.2
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]hexa-1,5-dien-1-yl]sulfonyl)amino]adenosine
Mycobacterium tuberculosis
-
above
0.034
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine
Mycobacterium tuberculosis
-
-
0.2
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)amino]adenosine
Mycobacterium tuberculosis
-
above
0.038
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine
Mycobacterium tuberculosis
-
-
0.2
5'-O-([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)adenosine
Mycobacterium tuberculosis
-
above
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
0.03
Triacsin C
Mus musculus
-
no effect on FATP4 acyl-CoA synthetase activity towards n-tetracosanoic acid, inhibits activity with palmitate with IC50 of 0.03 mM
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
0.02
troglitazone
Mus musculus
-
no effect on FATP4 acyl-CoA synthetase activity towards n-tetracosanoic acid up to 0.05 mM, inhibits activity with palmitate with IC50 of 0.02 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.8
-
isoform Facl1, using caproate as substrate, at pH 7.5 and 60°C
8.7
-
isoform Facl2, using palmitate as substrate, at pH 7.5 and 60°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8.5
8.1
-
acyl-CoA synthetase-4.6 and acyl-CoA synthetase-5.6. Acyl-CoA synthetase-4.6 has a second optimum at pH 8.5-9.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9.8
-
pH 6: about 50% of maximal activity, pH 8.9: about 60% of maximal activity
6.5 - 8.8
-
6.5: about 50% of maximal activity, 8.8: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 enzyme forms: long-chain acyl-CoA synthetase I and long-chain acyl-CoA synthetase II
-
-
brenda
heat inactivation does not distinguish between arachidonoyl-CoA synthetase, EC 6.2.1.15, and palmitoyl-CoA synthetase
-
-
brenda
palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase, EC 6.2.1.5, are not separate enzymes
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highly expressed in vascular endothelium of heart and aorta
brenda
inguinal adipose tissue
brenda
-
aortic, levels of isozymes ACSL1, ACSL3, and ACSL5, overview
brenda
additional information
gonadal and inguinal adipose tissue
brenda
-
isozyme LACS8 shows the highest expression level in the embryo
brenda
-
of Macaca mulatta or Macaca fascicularis infected with Plasmodium knowlesi
brenda
-
expression is limited to cells of the adaxial and abaxial epidermal layers, isoenzyme LACS2
brenda
-
-
brenda
-
hepatic ACS-5 mRNA is poorly expressed during fasting and diabetes and strongly induced by carbohydrate refeeding and insulin treatment
brenda
-
FACL3/ACS3 is the dominant isoform of FACL/ACS expressed in LNCaP cells
brenda
-
FACL3 protein expression and its regulation by 1alpha,25(OH)2D3 and its synthetic analogues EB1089 and CB1093 in prostate cancer cells, overview
brenda
additional information
-
expressed in young, rapidly expanding tissues, isoenzyme LACS2
brenda
additional information
-
tissue distribution of isozyme expression, overview
brenda
additional information
ACSL5 is expressed predominantly in tissues with high rates of triacylglycerol synthesis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
only LACS9 resides in the plastid, the site of de novo fatty acid synthesis
brenda
additional information
isoform ACSL3
brenda
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
brenda
-
-
-
brenda
-
mitochondrial membrane, ACS5. ACS1 is not detected in mitochondria
brenda
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
brenda
-
fatty acyl-CoA synthetase facilitates long chain fatty acid permeation of the inner membrane by a vectorial thioesterification
brenda
additional information
-
subcellular localization of isozymes, overview
-
brenda
additional information
not localized in mitochondrion or plasma membrane
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
abdominal segmentation defects of dAcsl mutants resemble those of gap gene knirps. The central expression domain of Kni transcripts or proteins is reduced whereas the adjacent domains of another gap gene Hunchback are correspondingly expanded in these mutants. Consequently, the striped pattern of the pair-rule gene Even-skipped is disrupted, phenotype, overview
malfunction
-
lipid-induced up-regulation of acyl-CoA synthetase 5 promotes hepatocellular apoptosis. High ACSL5 activity results in enhanced caspase-3/7 activity, but is not accompanied by up-regulation of death receptors, DR4, DR5 or TNF-R1
malfunction
-
loss of ACS-3, a long-chain acyl-CoA synthase, causes enhanced intestinal lipid uptake, de novo fat synthesis, and accumulation of enlarged, neutral lipid-rich intestinal depots. Acs-3 mutant phenotypes require the nuclear hormone receptor NHR-25, a key regulator of Caenorhabditis elegans molting
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
when compared to the wild-type strain, the fadD2 mutant exhibits decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant shows only increased swarming motility. Growth analysis of the fadD mutants show noticeable deficiencies in utilizing fatty acids and phosphatidylcholine as the sole carbon source, altered swimming and swarming motility of fadD mutants
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
-
dAcsl mutants exhibit neuromuscular junction (NMJ) overgrowth that is suppressed by reducing the doses of the bone morphogenetic protein, BMP, pathway components, accompanied by increased levels of activated BMP receptor Thickveins (Tkv) and phosphorylated mothers against decapentaplegic (Mad), the effector of the BMP signaling at NMJ terminals. In addition, Rab11, a small GTPase involved in endosomal recycling, is mislocalized in dAcsl mutant NMJs, and the membrane association of Rab11 is reduced in dAcsl mutant brains. The staining pattern of Rab11 is markedly alteredin dAcsl mutant NMJs, the abnormal Rab11 localization is specifically caused by dAcsl mutations. Consistently, the BMP receptor Tkv accumulates in early endosomes but is reduced in recycling endosomes in dAcsl mutant NMJs. The level of activated BMP receptor Tkv is elevated in dAcsl mutants. Phenotype, overview. The extended presynaptic distribution of Rab11 is completely reversed by both presynaptic and ubiquitous expression of human ACSL4
malfunction
-
enzyme deletion results in enhanced susceptibility to pyrazinoic acid and rifampin but not to isoniazid or ethambutol
malfunction
insights into the pathogenesis of ACSL4-related mental retardation, overview
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
malfunction
-
enzyme deletion results in enhanced susceptibility to pyrazinoic acid and rifampin but not to isoniazid or ethambutol
-
metabolism
-
acyl-CoA synthetase 5 is involved in the activation of long-chain fatty acids for lipid biosynthesis, and it is the only ACSL isoform that is both, located on mitochondria and functionally involved in enterocyte apoptosis. Analysis of regulation of ACSL5 in hepatocellular fatty acid degeneration and its involvement in hepatocyte apoptosis using models of in vitro and in vivo steatosis as well as plasmid-mediated stable gene transfer and RNAi-mediated gene silencing
metabolism
-
acyl-CoA synthetase 5 plays a key role in fatty acid metabolism. Isoform ACSL5 plays a role in channelling fatty acids towards palmitoylation and other lipid functions with high relevance for cellular behaviour
metabolism
-
long chain acyl CoA synthetase 4 is a key enzyme in steroidogenesis. It participates in steroid synthesis through of arachidonic acid release and steroidogenic acute regulatory protein induction
metabolism
-
the expression of FATP2 slightly, but reproducibly, increases both C16:0-CoA and C20:4-CoA derived from exogenous fatty acids, the formation of acyl CoA from C18:3 and C22:6 is significant
physiological function
-
ACSL3 shRNA, but not ACSL1 shRNA, inhibits the induction of lipid accumulation
physiological function
ACSL5 may have an anabolic role in lipid metabolism
physiological function
-
ACSL5 plays a role in promoting fatty acid-induced lipoapoptosis in hepatocytes as important mechanism in fatty liver-related disorders
physiological function
-
dAcsl is the Drosophila homolog of human ACSL4 and their functions are highly conserved in the processes ranging from lipid metabolism to the establishment of visual wiring, both maternal and zygotic dAcsl are required for embryonic segmentation
physiological function
-
FACL3 is a critical enzyme for activation of long-chain fatty acids. FACL3-mediated 1alpha,25(OH)2D3 inhibition of fatty acid synthase is associated with many cancers, including prostate cancer
physiological function
-
isozyme LACS9 is the major LACS isoform involved in plastidial fatty acid export for triacylglycerol formation. Isozymes LACS1 and LACS9 have overlapping functions in triacylglycerol biosynthesis. LACS1 is localized in the endoplasmic reticulum and is involved in cuticular lipid synthesis
physiological function
-
regulation of Caenorhabditis elegans fat uptake and storage by acyl-CoA synthase-3 is dependent on NR5A family nuclear hormone receptor nhr-25, overview. ACS-3-derived long-chain fatty acyl-CoAs, perhaps incorporated into complex ligands such as phosphoinositides, modulate NHR-25 function, which in turn regulates an endocrine program of lipid uptake and synthesis
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
-
Arabidopsis long-chain acyl-CoA synthetase isoforms LACS1, LACS2, and LACS3 facilitate fatty acid uptake in yeast. Expression of each isoform in yeast results in uptake of the long-chain fatty acid analogue, C1-Bodipy-C12. Only expression of LACS1 results in uptake of the very-long-chain fatty acid analogue, Bodipy-C16
physiological function
-
isoform Acsl3 is required to support effective poliovirus replication
physiological function
-
the enzyme plays a dual role in the transport and activation of exogenous fatty acids
physiological function
ACSL4 regulates neural development, role of ACSL4 in endosomal trafficking in vivo. ACSL4 is highly expressed in the hippocampus, a structure critical for learning and memory. Recombinant expression of human ACSL4 rescues the endocytic trafficking and neuromuscular junction (NMJ) phenotypes of Drosophila melanogaster enzyme mutants of the homologue dAcsl. The extended presynaptic distribution of Rab11 is completely reversed by both presynaptic and ubiquitous expression of human ACSL4
physiological function
-
dAcsl, the Drosophila orthologue of ACSL4 and ACSL3, inhibits synaptic growth by attenuating bone morphogenetic protein, BMP, signaling, a major growth-promoting pathway at neuromuscular junction (NMJ) synapses. dAcsl is also required for the recycling of photoreceptor rhodopsin in the eyes, implying a general role for dAcsl in regulating endocytic recycling of membrane receptors, dAcsl promotes rhodopsin recycling in photoreceptors, dAcsl inhibits endocytosis of BMP receptors. dAcsl regulates the membrane distribution of Rab11 at NMJs. dAcsl genetically interacts with rab11 in attenuating BMP signaling at NMJ synapses through facilitating Rab11 dependent BMP receptor recycling
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
-
isoform ACSL2 takes part in fatty acid and lipid degradation
physiological function
isoform ACSL6 overexpression in human primary myotubes increases phospholipid species and decreases oxidative metabolism
physiological function
-
isoforms LACS4 and LACS9 are involved in fatty acid transfer between endoplasmic reticulum and plastid
physiological function
long-chain acyl-CoA synthetases induce apoptotic cell death via the c-Jun N-terminal kinase pathway
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
additional information
-
Aspergillus nidulans contains six possible fatty acyl-CoA synthetases with FaaB being the major synthetase for fatty acid degradation. Deletion of faaB leads to growth defects on fatty acids but does not affect the induction of genes involved in boxidation
additional information
-
FACL3 protein expression and its regulation by 1alpha,25(OH)2D3 and its synthetic analogues EB1089 and CB1093 in prostate cancer cells, overview
additional information
-
fatty acid uptake rates in the organism, overview
additional information
-
isozyme ACSL4, EC 6.2.1.15, overexpression does not affect levels of ACSL3, ACSL1, and ACSL5
additional information
-
lacs9 null mutant do not show any detectable phenotype. Disruption of LACS8 in the lacs8 mutant and lacs8 lacs9 double mutant, and over-expression of LACS8, do not affect the seed fatty acid content
additional information
-
long-chain acyl-CoA synthetase member 6, ASCL6, is a form present in the plasma membrane of cells. Splicing events affecting the N-terminus and alternative motifs near the ATP-binding site generate different isoforms of ACSL6. Alternative fatty acid Gate-domain motifs are essential determinants for the activity of the human ACSL6 isoforms, which appear to act as homodimeric enzyme as well as in complex with other spliced forms. The diversity of these enzyme species can produce the variety of acyl-CoA synthetase activities that are necessary to generate and repair the hundreds of lipid species present in membranes. Oligomeric complex fomations and interactions between isoforms, overview. The N-terminal domain is not essential for oligomer formation
additional information
-
mutation of nhr-25 suppresses the fatty acid uptake phenotypes of acs-3(ft5) animals, overview
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
250000
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aggregates quite readily to form species with MW of over 1 million, gel filtration
47000
64000
75000
76000
79000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
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SDS-PAGE results in 4 protein components with MW 135000, 115000, 65000 and 55000
additional information
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fatty acid transport protein FATP1 and ACSL1 participate in an oligomeric complex in 3T3-L1 adipocytes. The interaction between ACSL1 and FATP1 is constitutive
additional information
FadDs contain ATP/AMP signature and FA-binding motifs
additional information
FadDs contain ATP/AMP signature and FA-binding motifs
additional information
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FadDs contain ATP/AMP signature and FA-binding motifs
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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the phosphorylation of the enzyme by protein kinase A and protein kinase C is hormone-dependent. Phosphorylation occurs after active dimer formation
additional information
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enzyme does not contain carbohydrate, phospholipid and fatty acid
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystallization of apoenzyme, enzyme in complex with adenosine 5'-(beta,gamma-imido)triphosphate and enzyme in complex with myristoyl-AMP
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K294E
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naturally occuring mutant of dAcs1, K294E is located in the AMP-binding domain
W685stop
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naturally occuring mutant of dAcs1, W685stop removes the last 33 amino acids
G216A
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the ratio of turnover number to Km-value for the reaction with oleate is 32.7% of the wild-type ratio
G219A
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the ratio of turnover number to Km-value for the reaction with oleate is 1.3fold higher than the wild-type ratio
K222A
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the ratio of turnover number to Km-value for the reaction with oleate is 8% of the wild-type ratio
N431A
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18 site-directed mutantions within the fatty acyl-CoA synthetase structural gene fadD corresponding to the FACS signature. Only one substitution results in wild-type fatty acyl-CoA synthetase activity profiles, 10 substitutions with abolished or greatly diminished enzyme activity, and seven substitutions with altered fatty acid chain length specificity. Of these seven, five also have reduced activity compared with the wild-type enzyme
T214A
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the ratio of turnover number to Km-value for the reaction with oleate is 10.3% of the wild-type ratio
T217A
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the ratio of turnover number to Km-value for the reaction with oleate is 6.7% of the wild-type ratio
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
additional information
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construction of opcl1 mutant, At1g20510-KO-1, plants, which show no induction of jasmonate by wounding in contrast to the wild-type plants, jasmonate profiles in leaves, overview
additional information
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generation of fatA, fatB, fatC and fatD deletion strains. Deletion of faaB leads to growth defects on fatty acids but does not affect the induction of genes involved in beta-oxidation, phenotype, overview
additional information
chimeric protein with firefly luciferase, EC 1.13.12.7, 4% of luminescence activity from Photinus pyralis luciferase activity
additional information
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recombinant expression of human gene ACSL4 in Drosophila melanogaster dAcsl mutant and complementation of reversed distribution of Rab11
additional information
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mutants of full-length ACSL6 isoform 2 (F-Gate) and DELTAN-truncated version of isoform 1 (DELTAN-(Y-Gate)) are obtained by site-directed mutagenesis of the H/L residue pair at position 316 and of the F/Y residue pair at position 319. An ACSL6 construct with a tag at its C-terminus has a far lower activity than a construct with a tag fused to its N-terminus
additional information
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overexpression of ACSL1 results in a less marked increase in arachidonoyl-CoA synthesis
additional information
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overexpression of ACSL5 decreases HepG2 cell viability and increases susceptibility to TRAIL- and TNFalpha-, but not FAS- induced apoptosis, whereas knockdown of ACSL5 reduces apoptosis susceptibility
additional information
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specific knockout of ACSL1 in mice leads to 30% increased fat mass when fed a low-fat diet, and normal fat mass with high-fat diet. The mutants incorporate oleate into fatty acids normally, but show 50-90% reduced fatty acid oxidation rates compared to the wild-type. The mutant mice are cold-intolerant and insensitive to beta3-adrenergic agonist activation, phenotype, overview
additional information
construction of fadD1 mutants, phenotype, overview
additional information
construction of fadD1 mutants, phenotype, overview
additional information
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construction of fadD1 mutants, phenotype, overview
additional information
siRNA knockdown of ACSL5 in rat primary hepatocytes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
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at pH levels from 5.0 to 11.0, isoform Facl activity increases along with an increase of pH, with the maximum activity obtained at pH 7.5, and about 40% of the highest activity still remains at pH 10.0 for isoform Facl1, and about 40% of the highest activity still remains at pH 9.5 for isoform Facl2
728248
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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2.5 min: 17-20% loss of activity, 5 min: 33-37% loss of activity, 15 min: 58-59% loss of activity
43
45
46
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5 min: 22% loss of acyl-CoA synthetase-4.6 activity, 38% loss of acyl-CoA synthetase-5.6 activity, 80% loss of acyl-CoA synthetase 5.0 activity
60
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about 40% of the highest activity of isoform Facl1 still remains after incubation at 60°C for 16 h, and above 50% of the highest isoform Facl2 activity still remains after incubation at 60°C for 8 h
additional information
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heat inactivation does not distinguish between arachidonoyl-CoA synthetase, EC 6.2.1.15, and palmitoyl-CoA synthetase
43
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half-life: about 10 min for ACS1, shorter thah 1 min fpr ACS4 and about 4 min for ACS5
45
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half-life of palmitoyl-CoA synthetase activity: 18 min, half-life of oleoyl-CoA synthetase activity: 4 min, half-life of arachidonyl-CoA synthetase activity: 49 min
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM potassium phosphate, 12 h, 70% loss of activity. 100 mM potassium phosphate or ATP stabilizes
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Sephacryl S-200 HR gel filtration
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partial
recombinant His-tagged AcsA by nickel affinity chromatography
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACS3, one of multiple forms of enzyme in brain, expression in COS cells
ACSL6 isoforms and truncated constructs, splicing variants, sequence organization, overview, expression of His-tagged full-length ACSL6 isoform 2 (F-Gate) and DELTAN-truncated version of isoform 1 (DELTAN-(Y-Gate)) in Escherichia coli strain BL21(DE3) membranes
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DNA and amino acid sequence determination and analysis, phylogenetic analysis, luciferase-like paralogues are located in close proximity on a chromosome, overview
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DNA and amino acid sequence determination and analysis, phylogenetic analysis, overview
ectopical overexpression of ACSL5 in rat hepatoma McArdle-RH7777 cells
expressed in a yeast fat1DELTA mutant which is deficient in both very-long-chain acyl-CoA synthetase activity and exogenous fatty acid uptake
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expressed in COS cells
expressed in COS-7 cells
expressed in Escherichia coli
expression in Escherichia coli
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
gene ACSL4, recombinant expression in Drosophila melanogaster dAcsl mutant and complementation of reversed distribution of Rab11
gene faaB or AN8280.3, DNA and amino acid sequence determination and analysis. The faaBD strain is complemented by transformation with a plasmid containing the original gene and its flanking region as well as an Aspergillus fumigatus riboB marker gene, pKR7320, and riboflavin prototrophic transformants are selected. Expression of GFP-fusion proteins GFP-FaaA and GFPFaaB
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gene fadD1, DNA and amino acid sequence determination, genetic organization, complemention of Escherichia coli strain fadD-/fadR- strain E2011. SMART mapping of the transcriptional start site for fadD1
gene fadD2, DNA and amino acid sequence determination, genetic organization, complemention of Escherichia coli strain fadD-/fadR- strain E2011. SMART mapping of the transcriptional start site fadD1
heterologous expression of TplacsA in yeast fatty acid activation depletion strain faa4DELTA. TplacsA transformants are able to incorporate more docosahexaenoic acid in triacylglycerols than the control yeast
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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
menE, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
acute lipid ingestion increases the expression of isoform ACSL6
adenocarcinomas with an invasive phenotype and enhanced proliferation show decreased levels of isoform ACSL5
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enzyme transcription is up-regulated when treated by nitrogen and iron excess and at 15 and 35C
exercise and fasting decrease isoform ACSL6 mRNA
expression of ACSL3 is induced by ER stress in HuH-7 cells. shRNA that target GSK-3beta also inhibits the upregulation of ACSL3 and lipid accumulation in HuH-7 and HepG2 cells
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FaaB but not FaaA is induced in the presence of both sort-chain fatty acids and long-chain fatty acids
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FACL3 is upregulated by 1alpha, 25(OH)2D3 at an mRNA and enzyme activity levels in prostate cancer cells, overview
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GSK-3beta inhibitors attenuate ACSL3 expression and the lipid accumulation induced by ER stress in HuH-7 cells. shRNA that target GSK-3beta also inhibits the upregulation of ACSL3 and lipid accumulation in HuH-7 and HepG2 cells
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isoform ACSL2 is highly expressed in germinating seedling and strongly induced 1 day after imbibition
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lipid-induced up-regulation of acyl-CoA synthetase 5 promotes hepatocellular apoptosis. ACSL5 expression is enhanced in steatotic liver
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long chain acyl-CoA synthetase activity is upregulated in poliovirus-infected cells
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there is a 6.7fold increase and a 10.8fold increase in the mRNA levels of isoforms facl1 and facl2, respectively, when crude oil is used as a sole carbon source instead of sucrose
enzyme transcription is up-regulated when treated by nitrogen and iron excess and at 15 and 35C
enzyme transcription is up-regulated when treated by nitrogen and iron excess and at 15 and 35C
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there is a 6.7fold increase and a 10.8fold increase in the mRNA levels of isoforms facl1 and facl2, respectively, when crude oil is used as a sole carbon source instead of sucrose
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there is a 6.7fold increase and a 10.8fold increase in the mRNA levels of isoforms facl1 and facl2, respectively, when crude oil is used as a sole carbon source instead of sucrose
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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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Release 2023.1 (January 2023)
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