show all | hide all No of entries

Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase and Organism(s) Homo sapiens and UniProt Accession P33121

for references in articles please use BRENDA:EC6.2.1.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.3 long-chain-fatty-acid-CoA ligase
IUBMB 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.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P33121
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
Abll, ACS, ACS-3, ACS-5, ACS1, ACS2, ACS3, ACS4, ACS5, ACS6, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACS
247
-
ACS3
-
-
-
-
ACSL
247
-
ACSL1
ACSL3
ACSL4
281640
-
ACSL6
ACSL6 protein
281637
-
ACSL6_v1
247
-
ACSL6_v2
281637
-
ACSL6_v3
281637
-
ACSL6_v5
247
-
ACSL6_v6
247
-
Acsvl1
247
-
Acyl coenzyme A synthetase
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Acyl-CoA ligase
-
-
-
-
Acyl-CoA synthetase
Acyl-CoA synthetase 3
-
-
-
-
acyl-CoA synthetase 5
247
-
acyl-CoA synthetase long-chain family member 4
281640
-
acyl-CoA synthetase-1
281625
-
Acyl-coenzyme A ligase
-
-
-
-
BGR
247
-
bubblegum-related protein
247
-
FAA1
-
-
-
-
FACL3
247
-
FACL3/ACS3
247
-
FACL4
281640
-
FATP
247
-
FATP2
247
-
FATP4
281643
-
Fatty acid CoA ligase
-
-
-
-
Fatty acid thiokinase (long chain)
-
-
-
-
fatty acid transport protein 2
247
-
fatty acid-CoA ligase 4
281640
-
Fatty acyl-coenzyme A synthetase
-
-
-
-
Fatty-acyl-CoA ligase
-
-
-
-
LCFA synthetase
-
-
-
-
long chain acyl-CoA synthetase
247
-
long chain acyl-CoA synthetase 3
Long chain fatty acyl CoA ligase
-
-
-
-
Long chain fatty acyl-CoA synthetase
-
-
-
-
Long-chain acyl CoA synthetase
-
-
-
-
long-chain acyl-CoA synthetase
247
-
long-chain acyl-CoA synthetase 6
281637
-
Long-chain acyl-CoA synthetase I
-
-
-
-
Long-chain acyl-CoA synthetase II
-
-
-
-
long-chain acyl-CoA synthetases
247, 281637
-
Long-chain acyl-coenzyme A synthetase
-
-
-
-
long-chain fatty acid:CoA ligase
247
-
Long-chain fatty acyl coenzyme A synthetase
-
-
-
-
long-chain fatty acyl-CoA synthetase
247
-
long-chain fatty-acid-CoA ligase 3
247
-
mACS4
-
-
-
-
Oleoyl-CoA synthetase
-
-
-
-
Palmitoyl coenzyme A synthetase
-
-
-
-
Palmitoyl-CoA ligase
-
-
-
-
Palmityl-coenzyme A synthetase
-
-
-
-
Pristanoyl-CoA synthetase
-
-
-
-
Stearoyl-CoA synthetase
-
-
-
-
Thiokinase
-
-
-
-
very long chain acyl-CoA synthetase 1
247
-
additional information
247
the ezyme is a member of the ACSL gene family that catalyzes the activation of long-chain fatty acids for lipid biosynthesis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
Phosphorylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
long-chain fatty acid:CoA ligase (AMP-forming)
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-18-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + fatty acid + dephospho-CoA
AMP + diphosphate + acyl-dephospho-CoA
show the reaction diagram
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
show the reaction diagram
-
-
-
?
ATP + a long-chain carboxylate + CoA
AMP + diphosphate + an acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain fatty acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + an acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acylate + CoA
AMP + diphosphate + acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
ATP + Bodipy 500/510 C4-C9 + CoA
?
show the reaction diagram
-
-
-
-
?
ATP + hexadecanoate + CoA
AMP + diphosphate + hexadecanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + lignocerate + CoA
AMP + diphosphate + lignoceroyl-CoA
show the reaction diagram
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + lineoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
show the reaction diagram
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
show the reaction diagram
-
essential role in animal cell proliferation
-
-
-
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
show the reaction diagram
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
show the reaction diagram
ATP + stearate + CoA
AMP + diphosphate + stearoyl-CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a long-chain carboxylate + CoA
AMP + diphosphate + an acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + a long-chain fatty acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + a long-chain fatty acid + CoA
AMP + diphosphate + an acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acylate + CoA
AMP + diphosphate + acyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + hexadecanoate + CoA
AMP + diphosphate + hexadecanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
show the reaction diagram
-
essential role in animal cell proliferation
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triacsin C
Triacsins
-
hierarchy of inhibitory potency in decreasing order: triacsin C, triacsin A, triacsin D/ triacsin B
Triton X-100
-
Inhibition of acyl-CoA formation, inhibits ACSL6 isoform 2 (F-Gate) and its N-terminus truncated version, DELTAN-(F-Gate)
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
specific Gate-domain residues are essential for activity, detailed overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low FACT3 expression level
Manually annotated by BRENDA team
-
highest expression level in enterocytes at the villus tip
Manually annotated by BRENDA team
-
high expression level of ACSL4
Manually annotated by BRENDA team
-
low FACT3 expression level
Manually annotated by BRENDA team
-
aortic, levels of isozymes ACSL1, ACSL3, and ACSL5, overview
Manually annotated by BRENDA team
exclusively found in testis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozyme ACSL6
Manually annotated by BRENDA team
additional information
not found at the plasma membrane
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ACSL1_HUMAN
698
1
77943
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
predicted molecular mass
75000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F319A
-
site-directed mutagenesis
F319W
-
site-directed mutagenesis
F319Y
-
site-directed mutagenesis
H316L
-
site-directed mutagenesis
L316H
-
site-directed mutagenesis
Y319A
-
site-directed mutagenesis
Y319F
-
site-directed mutagenesis
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
heat inactivation does not distinguish between arachidonoyl-CoA synthetase, EC 6.2.1.15, and palmitoyl-CoA synthetase
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partial
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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
-
expressed in COS-7 cells
expressed in Escherichia coli
-
expressed in Pt-K2 cells
FACL3, quantitative real-time quantitative PCR expression analysis
-
gene acs-3, quantitative reverse transcription PCR expression analysis
-
gene ACSL4, recombinant expression in Drosophila melanogaster dAcsl mutant and complementation of reversed distribution of Rab11
-
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
-
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
-
FACL3 is upregulated by 1alpha, 25(OH)2D3 at an mRNA and enzyme activity levels in prostate cancer cells, overview
-
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
-
lipid-induced up-regulation of acyl-CoA synthetase 5 promotes hepatocellular apoptosis. ACSL5 expression is enhanced in steatotic liver
-
long chain acyl-CoA synthetase activity is upregulated in poliovirus-infected cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bakken, A.M.; Farstad, M.
Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets
Biochem. J.
261
71-76
1989
Homo sapiens
Manually annotated by BRENDA team
Bakken, A.M.; Farstad, M.; Holmsen, H.
Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelets?
Biochem. J.
274
145-152
1991
Homo sapiens
Manually annotated by BRENDA team
Tomoda, H.; Igarashi, K.; Cyong, J.C.; Omura, S.
Evidence for an essential role of long chain acyl-CoA synthetase in animal cell proliferation. Inhibition of long chain acyl-CoA synthetase by triacsins caused inhibition of Raji cell proliferation
J. Biol. Chem.
266
4214-4219
1991
Homo sapiens
Manually annotated by BRENDA team
Qiao, S.; Tuohimaa, P.
The role of long-chain fatty-acid-CoA ligase 3 in vitamin D3 and androgen control of prostate cancer LNCaP cell growth
Biochem. Biophys. Res. Commun.
319
358-368
2004
Homo sapiens
Manually annotated by BRENDA team
Vessey, D.A.; Kelley, M.; Warren, R.S.
Characterization of triacsin C inhibition of short-, medium-, and long-chain fatty acid: CoA ligases of human liver
J. Biochem. Mol. Toxicol.
18
100-106
2004
Homo sapiens
Manually annotated by BRENDA team
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
Homo sapiens, Homo sapiens (P33121), Mus musculus, Mus musculus (P41216), Rattus norvegicus (P18163)
Manually annotated by BRENDA team
Fraisl, P.; Tanaka, H.; Forss-Petter, S.; Lassmann, H.; Nishimune, Y.; Berger, J.
A novel mammalian bubblegum-related acyl-CoA synthetase restricted to testes and possibly involved in spermatogenesis
Arch. Biochem. Biophys.
451
23-33
2006
Homo sapiens, Homo sapiens (Q5FVE4), Mus musculus
Manually annotated by BRENDA team
Fujimoto, Y.; Onoduka, J.; Homma, K.J.; Yamaguchi, S.; Mori, M.; Higashi, Y.; Makita, M.; Kinoshita, T.; Noda, J.; Itabe, H.; Takanoa, T.
Long-chain fatty acids induce lipid droplet formation in a cultured human hepatocyte in a manner dependent of acyl-CoA synthetase
Biol. Pharm. Bull.
29
2174-2180
2006
Homo sapiens
Manually annotated by BRENDA team
Soupene, E.; Kuypers, F.A.
Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains
BMC Mol. Biol.
7
21
2006
Homo sapiens, Homo sapiens (Q9UKU0)
Manually annotated by BRENDA team
Sung, Y.K.; Park, M.K.; Hong, S.H.; Hwang, S.Y.; Kwack, M.H.; Kim, J.C.; Kim, M.K.
Regulation of cell growth by fatty acid-CoA ligase 4 in human hepatocellular carcinoma cells
Exp. Mol. Med.
39
477-482
2007
Homo sapiens, Homo sapiens (O60488)
Manually annotated by BRENDA team
Yao, H.; Ye, J.
Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells
J. Biol. Chem.
283
849-854
2007
Homo sapiens, Homo sapiens (O60488), Homo sapiens (O95573), Homo sapiens (P33121)
Manually annotated by BRENDA team
Milger, K.; Herrmann, T.; Becker, C.; Gotthardt, D.; Zickwolf, J.; Ehehalt, R.; Watkins, P.A.; Stremmel, W.; Fuellekrug, J.
Cellular uptake of fatty acids driven by the ER-localized acyl-CoA synthetase FATP4
J. Cell Sci.
119
4678-4688
2006
Homo sapiens (Q6P1M0), Mus musculus (Q91VE0)
Manually annotated by BRENDA team
Reinartz, A.; Ehling, J.; Leue, A.; Liedtke, C.; Schneider, U.; Kopitz, J.; Weiss, T.; Hellerbrand, C.; Weiskirchen, R.; Knuechel, R.; Gassler, N.
Lipid-induced up-regulation of human acyl-CoA synthetase 5 promotes hepatocellular apoptosis
Biochim. Biophys. Acta
1801
1025-1035
2010
Homo sapiens
Manually annotated by BRENDA team
Soupene, E.; Dinh, N.P.; Siliakus, M.; Kuypers, F.A.
Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains
BMC Biochem.
11
18
2010
Homo sapiens
Manually annotated by BRENDA team
Chang, Y.S.; Tsai, C.T.; Huangfu, C.A.; Huang, W.Y.; Lei, H.Y.; Lin, C.F.; Su, I.J.; Chang, W.T.; Wu, P.H.; Chen, Y.T.; Hung, J.H.; Young, K.C.; Lai, M.D.
ACSL3 and GSK-3beta are essential for lipid upregulation induced by endoplasmic reticulum stress in liver cells
J. Cell. Biochem.
112
881-893
2011
Homo sapiens
Manually annotated by BRENDA team
Golej, D.L.; Askari, B.; Kramer, F.; Barnhart, S.; Vivekanandan-Giri, A.; Pennathur, S.; Bornfeldt, K.E.
Long-chain acyl-CoA synthetase 4 modulates prostaglandin E2 release from human arterial smooth muscle cells
J. Lipid Res.
52
782-793
2011
Homo sapiens
Manually annotated by BRENDA team
Qiao, S.; Tuohimaa, P.
Expression and vitamin D3 regulation of long-chain fatty-acid-CoA ligase 3 in human prostate cancer cells
Prostaglandins Leukot. Essent. Fatty Acids
84
19-23
2011
Homo sapiens
Manually annotated by BRENDA team
Melton, E.M.; Cerny, R.L.; DiRusso, C.C.; Black, P.N.
Overexpression of human fatty acid transport protein 2/very long chain acyl-CoA synthetase 1 (FATP2/Acsvl1) reveals distinct patterns of trafficking of exogenous fatty acids
Biochem. Biophys. Res. Commun.
440
743-748
2013
Homo sapiens
Manually annotated by BRENDA team
Nchoutmboube, J.A.; Viktorova, E.G.; Scott, A.J.; Ford, L.A.; Pei, Z.; Watkins, P.A.; Ernst, R.K.; Belov, G.A.
Increased long chain acyl-CoA synthetase activity and fatty acid import is linked to membrane synthesis for development of picornavirus replication organelles
PLoS Pathog.
9
e1003401
2013
Homo sapiens
Manually annotated by BRENDA team
Klaus, C.; Jeon, M.K.; Kaemmerer, E.; Gassler, N.
Intestinal acyl-CoA synthetase 5: activation of long chain fatty acids and behind
World J. Gastroenterol.
19
7369-7373
2013
Homo sapiens
Manually annotated by BRENDA team
Liu, Z.; Huang, Y.; Hu, W.; Huang, S.; Wang, Q.; Han, J.; Zhang, Y.Q.
dAcsl, the Drosophila ortholog of acyl-CoA synthetase long-chain family member 3 and 4, inhibits synapse growth by attenuating bone morphogenetic protein signaling via endocytic recycling
J. Neurosci.
34
2785-2796
2014
Drosophila melanogaster, Homo sapiens, Homo sapiens (O60488)
Manually annotated by BRENDA team
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
Homo sapiens, Homo sapiens (Q9UKU0), Rattus norvegicus
Manually annotated by BRENDA team
Select items on the left to see more content.