Information on EC 6.2.1.3 -

Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase:

Please wait a moment until all data are loaded. This message will disappear when all data are loaded.

Mark a special word or phrase in this record:
Select one or more organisms in this record:

Show additional data Do not include text mining results
Include

(text mining) results (more...)
Include

results (AMENDA + additional results, but less precise; more...)

Please login to have access to the AMENDA and FRENDA data

EC NUMBER	COMMENTARY
6.2.1.3	-

RECOMMENDED NAME	GeneOntology No.
long-chain-fatty-acid-CoA ligase	GO:0031957

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA		mitochondrial long chain fatty acyl-CoA ligase, unlike short chain ligases and medium chain ligases, does not utilize an adenylate as an intermediate in the formation of fatty acyl-CoA	Rattus norvegicus	-	762
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA		-	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Acid-thiol ligation	-	-	-	-
Phosphorylation	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
(Z)-9-tricosene biosynthesis	-	PWY-7035
6-gingerol analog biosynthesis	-	PWY-6920
alkane biosynthesis II	-	PWY-7033
androstenedione degradation	-	PWY-6944
arachidonate biosynthesis	-	PWY-5353
cholesterol degradation to androstenedione I (cholesterol oxidase)	-	PWY-6945
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)	-	PWY-6946
docosahexanoate biosynthesis I	-	PWY-7053
docosahexanoate biosynthesis II	-	PWY-6951
eicosapentaenoate biosynthesis II (metazoa)	-	PWY-7049
fatty acid activation	-	PWY-5143
fatty acid alpha-oxidation II	-	PWY66-387
fatty acid beta-oxidation I	-	FAO-PWY
fatty acid beta-oxidation II (peroxisome)	-	PWY-5136
fatty acid salvage	-	PWY-7094
gamma-linolenate biosynthesis II (animals)	-	PWY-6000
linoleate biosynthesis I (plants)	-	PWY-5995
linoleate biosynthesis II (animals)	-	PWY-6001
long chain fatty acid ester synthesis for microdiesel production	-	PWY-6873
octane oxidation	-	P221-PWY
phosphatidylcholine acyl editing	-	PWY-6803
stearate biosynthesis I (animals)	-	PWY-5972
wax esters biosynthesis II	-	PWY-5885

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.

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Abll	Agrypnus binodulus	-	-	697221
ACS	Mus musculus	-	-	671606, 672182, 692792
ACS	Homo sapiens	Q5FVE4	-	671606
ACS	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
ACS	Rattus norvegicus	-	-	674710
ACS	Plasmodium falciparum	-	-	675872
ACS-3	Caenorhabditis elegans	-	-	714677
ACS-5	Rattus norvegicus	-	-	661284
ACS1	Rattus norvegicus	-	-	652138, 652139, 662185, 662225
ACS1	Babesia bovis	Q6QLU3	-	675867
ACS2	Rattus norvegicus	-	-	662185, 662225
ACS3	-	-	-	-
ACS3	Rattus norvegicus	Q63151	-	662185
ACS4	Rattus norvegicus	-	-	652138, 652139, 662185
ACS4	Mus musculus	Q61193	-	675690
ACS5	Rattus norvegicus	-	-	652138, 652139, 662185
ACS6	Brassica napus	Q9FNT6	-	653493
AcsA	Pseudomonas chlororaphis	Q5CD72	-	693035
ACSL	Mus musculus	-	-	662593, 671244
ACSL	Rattus norvegicus	-	-	662994, 671244
ACSL	Saccharomyces cerevisiae	-	-	672418
ACSL	Drosophila melanogaster	-	-	714799
ACSL	Homo sapiens	-	-	715715
ACSL1	Mus musculus	-	-	662593, 671234, 672421, 714678
ACSL1	Rattus norvegicus	P18163	-	671234, 674710, 675267
ACSL1	Homo sapiens	-	-	671234, 674910, 715838
ACSL3	Rattus norvegicus	-	-	661181, 675267
ACSL3	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421
ACSL3	Homo sapiens	O95573	specifically required for incorporation of fatty acids into phosphatidylcholine	674910
ACSL3	Homo sapiens	-	-	715715, 715838
ACSL4	Sus scrofa	-	-	671335
ACSL4	Rattus norvegicus	-	prefers longer chain polyunsaturated fatty acids as substrates	672417
ACSL4	Rattus norvegicus	-	-	672419, 675267
ACSL4	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421
ACSL4	Homo sapiens	O95573	-	674910
ACSL5	Rattus norvegicus	-	;	662463
ACSL5	Rattus norvegicus	-	-	672419, 675267, 715835
ACSL5	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421
ACSL5	Homo sapiens	-	-	714313, 715838
ACSL6	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421
ACSL6	Rattus norvegicus	P33124	-	675267
ACSL6	Homo sapiens	-	-	714605
ACSL6 protein	Homo sapiens	Q9UKU0	-	672807
ACSL6_v1	Rattus norvegicus	P33124	-	661181
ACSL6_v1	Homo sapiens	Q9UKU0	-	672807
ACSL6_v2	Rattus norvegicus	P33124	-	661181
ACSL6_v2	Homo sapiens	Q9UKU0	-	672807
ACSL6_v3	Homo sapiens	Q9UKU0	-	672807
ACSL6_v5	Homo sapiens	Q9UKU0	-	672807
ACSL6_v6	Homo sapiens	Q9UKU0	-	672807
Acyl coenzyme A synthetase	-	-	-	-
Acyl-activating enzyme	-	-	-	-
Acyl-CoA ligase	-	-	-	-
acyl-CoA synthase-3	Caenorhabditis elegans	-	-	714677
Acyl-CoA synthetase	-	-	-	-
Acyl-CoA synthetase	Mus musculus	-	-	671606, 675015, 692792
Acyl-CoA synthetase	Homo sapiens	-	-	671606, 675015, 714605
Acyl-CoA synthetase	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
Acyl-CoA synthetase	Rattus norvegicus	-	-	675554
Acyl-CoA synthetase	Plasmodium falciparum	-	-	675872
Acyl-CoA synthetase	Mycobacterium tuberculosis	-	-	691308
Acyl-CoA synthetase	Pseudomonas chlororaphis	Q5CD72	-	693035
Acyl-CoA synthetase	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	;	716680
Acyl-CoA synthetase 3	-	-	-	-
acyl-CoA synthetase 4	Rattus norvegicus	-	-	672419
acyl-CoA synthetase 4	Mus musculus	Q61193	-	675690
acyl-CoA synthetase 5	Rattus norvegicus	-	-	672419
acyl-CoA synthetase 5	Homo sapiens	-	-	714313
acyl-CoA synthetase-1	Mus musculus	-	-	671234, 714678
acyl-CoA synthetase-1	Homo sapiens, Rattus norvegicus	-	-	671234
Acyl-coenzyme A ligase	-	-	-	-
BGR	Homo sapiens	Q5FVE4	-	671606
BGR	Mus musculus	-	-	671606
bubblegum-related protein	Homo sapiens	Q5FVE4	-	671606
bubblegum-related protein	Mus musculus	-	-	671606
CG6178	Drosophila melanogaster	-	-	672684
dAcsl	Drosophila melanogaster	-	-	714799
FAA1	-	-	-	-
Faa1p	Saccharomyces cerevisiae	-	-	672418
Faa1p	Saccharomyces cerevisiae	P38137, P38225, P39518	in the peroxisome	672419
Faa2p	Saccharomyces cerevisiae	P38137, P38225, P39518	;	672419
Faa3p	Saccharomyces cerevisiae	P38137, P38225, P39518	in the membrane	672419
Faa4p	Saccharomyces cerevisiae	P38137, P38225, P39518	in membrane and cytosol	672419
FaaA	Emericella nidulans	-	-	713991
FaaB	Emericella nidulans	-	-	713991
FACL3	Homo sapiens	-	-	716813
FACL3/ACS3	Homo sapiens	-	-	660874
FACL4	Homo sapiens	-	-	673484
FACS	Escherichia coli	-	-	652285, 662226
FACS	Mus musculus	Q924N5	-	675688
FACS	Rattus norvegicus	-	-	675688
FAdD	Rattus norvegicus	Q63151	;	662185
FAdD	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	gene name; gene name	716680
Fat1p	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
Fat2p	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
FatA	Emericella nidulans	-	-	713991
FatB	Emericella nidulans	-	-	713991
FatC	Emericella nidulans	-	-	713991
FatD	Emericella nidulans	-	-	713991
FATP4	Mus musculus	-	bifunctional enzyme, exhibiting both fatty acid transport and acyl-CoA synthetase activities	662341
FATP4	Mus musculus	-	-	674830, 675015
FATP4	Homo sapiens	Q6P1M0	-	675015
Fatty acid CoA ligase	-	-	-	-
fatty acid CoA ligase: AMP forming	Saccharomyces cerevisiae	-	-	672418
fatty acid thiokinase	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
Fatty acid thiokinase (long chain)	-	-	-	-
fatty acid transport protein	Mus musculus	-	bifunctional enzyme, exhibiting both fatty acid transport and acyl-CoA synthetase activities	662341
fatty acid transport protein 4	Mus musculus	O88561	-	674830
fatty acid-CoA ligase 4	Homo sapiens	-	-	673484
fatty acid:CoA ligase, AMP-forming	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
fatty acyl-CoA synthetase	Escherichia coli	-	-	662226
fatty acyl-CoA synthetase	Trypanosoma brucei	-	-	662797
fatty acyl-CoA synthetase	Drosophila melanogaster	-	-	672684
fatty acyl-CoA synthetase	Babesia bovis	Q6QLU3	-	675867
fatty acyl-CoA synthetase	Arabidopsis thaliana	-	-	693420
fatty acyl-CoA synthetase	Photinus pyralis	P08659	-	694271
fatty acyl-CoA synthetase	Tribolium castaneum	-	-	694271
fatty acyl-CoA synthetase	Emericella nidulans	-	-	713991
Fatty acyl-coenzyme A synthetase	-	-	-	-
Fatty-acyl-CoA ligase	-	-	-	-
gonadotropin-regulated long chain acyl-CoA synthetase	Rattus norvegicus	Q924N5	-	653671
gonadotropin-regulated long-chain acyl CoA synthetase	Mus musculus	-	-	661822
GR-LACS	Rattus norvegicus	Q924N5	-	653671
GR-LACS	Mus musculus	-	-	661822
LACS	-	-	-	-
LACS	Rattus norvegicus	-	-	649789, 675688
LACS	Homo sapiens	-	-	662072
LACS	Mus musculus	Q924N5	-	675688
LACS1	Arabidopsis thaliana	-	-	716538
LACS2	Arabidopsis thaliana	-	-	663058
LC-FACS	Thermus thermophilus	-	-	662243
LCFA synthetase	-	-	-	-
LCFACoAS	Oryctolagus cuniculus	-	-	650399
lipidosin	Mus musculus	-	-	649559
lipidosin	Rattus norvegicus	-	-	675554
long chain acyl-CoA synthetase	Saccharomyces cerevisiae	-	-	672418
long chain acyl-CoA synthetase	Homo sapiens	-	-	672490
long chain acyl-CoA synthetase	Mus musculus	-	-	674830, 675688
long chain acyl-CoA synthetase	Rattus norvegicus	P33124	-	675267
long chain acyl-CoA synthetase	Rattus norvegicus	-	-	675688
long chain acyl-CoA synthetase 1	Rattus norvegicus	-	-	662185, 674710
long chain acyl-CoA synthetase 2	Rattus norvegicus	Q63151	-	662185
long chain acyl-CoA synthetase 3	Rattus norvegicus	Q63151	-	662185
long chain acyl-CoA synthetase 3	Homo sapiens	O95573	-	674910
long chain acyl-CoA synthetase 4	Rattus norvegicus	-	-	662185, 672417
long chain acyl-CoA synthetase 5	Rattus norvegicus	Q63151	-	662185
long chain acyl-CoA synthetase 5	Rattus norvegicus	-	;	662463
Long chain fatty acyl CoA ligase	-	-	-	-
Long chain fatty acyl-CoA synthetase	-	-	-	-
long chain fatty acyl-CoA synthetase 5	Rattus norvegicus	-	-	661284
long fatty acyl-CoA synthetase	Drosophila melanogaster	-	-	697221
Long-chain acyl CoA synthetase	-	-	-	-
Long-chain acyl CoA synthetase	Caulobacter vibrioides	-	-	713994
long-chain acyl coenzyme A synthetase 1	Mus musculus	-	-	662593
long-chain acyl-CoA synthetase	Mus musculus	-	-	671244, 672182
long-chain acyl-CoA synthetase	Rattus norvegicus	-	-	671244
long-chain acyl-CoA synthetase	Sus scrofa	-	-	671335
long-chain acyl-CoA synthetase	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421
long-chain acyl-CoA synthetase	Drosophila melanogaster	-	-	714799
long-chain acyl-CoA synthetase	Homo sapiens	-	-	715715
long-chain acyl-CoA synthetase 1	Arabidopsis thaliana	-	-	716538
long-chain acyl-CoA synthetase 5	Rattus norvegicus	O88813	-	715835
long-chain acyl-CoA synthetase 6	Rattus norvegicus	-	-	662330
Long-chain acyl-CoA synthetase I	-	-	-	-
Long-chain acyl-CoA synthetase II	-	-	-	-
long-chain acyl-CoA synthetase-1	Mus musculus	-	-	714678
long-chain acyl-CoA synthetases	Homo sapiens	Q9UKU0	;	672807
Long-chain acyl-coenzyme A synthetase	-	-	-	-
long-chain fatty acid:CoA ligase	Homo sapiens	-	-	662072
Long-chain fatty acyl coenzyme A synthetase	-	-	-	-
long-chain fatty acyl-CoA synthetase	Homo sapiens	-	-	662072
long-chain fatty-acid-CoA ligase 3	Homo sapiens	-	-	660874, 716813
long-chain polyunsaturated fatty acid acyl-coenzyme A synthetase	Thalassiosira pseudonana	-	-	663142
luciferase-like gene	Agrypnus binodulus	-	-	697221
luciferase-like protein	Photinus pyralis	P08659	-	694271
luciferase-like protein	Tribolium castaneum	-	-	694271
mACS4	-	-	-	-
MALCE1	Mortierella alpina	C8KHM6	-	701851
Oleoyl-CoA synthetase	-	-	-	-
OPC-8:CoA ligase	Arabidopsis thaliana	-	-	693420
OPCL1	Arabidopsis thaliana	-	-	693420
Palmitoyl coenzyme A synthetase	-	-	-	-
Palmitoyl-CoA ligase	-	-	-	-
Palmityl-coenzyme A synthetase	-	-	-	-
PhpLL1	Photinus pyralis	P08659	-	694271
Pristanoyl-CoA synthetase	-	-	-	-
protein At1g20510	Arabidopsis thaliana	-	-	693420
putative long-chain acyl-CoA synthetase	Babesia bovis	Q6QLU3	-	675867
R-ibuprofenoyl-CoA synthetase	Rattus norvegicus	-	-	649789
Stearoyl-CoA synthetase	-	-	-	-
TbACS1	Trypanosoma brucei	-	-	649717
TbACS3	Trypanosoma brucei	-	-	649717, 662797
TbACS4	Trypanosoma brucei	-	-	649717
Thiokinase	-	-	-	-
YBR041W	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
YBR222C	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
YER015W	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419
MenE	Mycobacterium tuberculosis	-	-	691308
additional information	Pseudomonas chlororaphis	Q5CD72	acyl-CoA synthetase belongs to the superfamily of adenylate-forming enzymes, whose three-dimensional structures are analogous to one another	693035
additional information	Arabidopsis thaliana	-	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	693420
additional information	Photinus pyralis	P08659	the enzyme is a part of a larger AMP-forming superfamily	694271
additional information	Tribolium castaneum	-	the enzyme is a part of a larger AMP-forming superfamily	694271
additional information	Homo sapiens	-	the ezyme is a member of the ACSL gene family that catalyzes the activation of long-chain fatty acids for lipid biosynthesis	714313

CAS REGISTRY NUMBER	COMMENTARY
9013-18-7	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Agrypnus binodulus	-	697221	-	-
Arabidopsis thaliana	-	663057	-	-
Arabidopsis thaliana	Col-0, Ws-0, gene OPCL1	693420	-	-
Arabidopsis thaliana	isoenzyme LACS2	663058	-	-
Arabidopsis thaliana	isozymes LACS1-LACS9	716538	-	-
Babesia bovis	-	675867	Q6QLU3	TrEMBL
Brassica napus	-	653493	Q9FNT6	SwissProt
Brassica napus	-	745	-	-
Caenorhabditis elegans	isozyme ACS-3, gene acs-3	714677	-	-
Caulobacter vibrioides	-	713994	-	-
Chaenocephalus aceratus	-	661519	-	-
Drosophila melanogaster	-	672684, 697221	Q9VCC6	UniProt
Drosophila melanogaster	isozyme dAcsl	714799	-	-
Emericella nidulans	gene faaB or AN8280.3 encoding isozyme FaaB	713991	-	-
Escherichia coli	-	652285, 662226, 743, 753, 761	-	-
Escherichia coli	multiple charge isoforms: 4.6, 5.0 and 5.6	751	-	-
Escherichia coli	wild-type and mutant forms	739	-	-
Homo sapiens	-	660874, 662072, 672490, 672807, 715715, 716813, 741	-	-
Homo sapiens	-	671234, 674910	P33121	UniProt
Homo sapiens	-	671606	Q5FVE4	Uniprot
Homo sapiens	-	672807	Q9UKU0	SwissProt
Homo sapiens	-	673484, 674910	O60488	UniProt
Homo sapiens	-	674910	O95573	SwissProt
Homo sapiens	-	675015	Q6P1M0	SwissProt
Homo sapiens	heat inactivation does not distinguish between arachidonoyl-CoA synthetase, EC 6.2.1.15, and palmitoyl-CoA synthetase	637	-	-
Homo sapiens	isozyme ACSL5	714313	-	-
Homo sapiens	isozyme ACSL6	714605	-	-
Homo sapiens	isozymes ACSL1, ACSL3, and ACSL5	715838	-	-
Homo sapiens	palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase, EC 6.2.1.5, are not separate enzymes	638	-	-
Luciola cruciata	-	658314, 658709	-	-
Mortierella alpina	strain 1S-4	701851	C8KHM6	UniProt
Mortierella alpina 1S-4	strain 1S-4	701851	C8KHM6	UniProt
Mus musculus	-	634, 649559, 661822, 662341, 662593, 671244, 671606, 672182, 692792, 714678	-	-
Mus musculus	-	671234, 672421	P41216	UniProt
Mus musculus	-	672421	Q8JZR0, Q91WC3	UniProt
Mus musculus	-	672421	Q9CZW4	Uniprot
Mus musculus	-	672421	Q9QUJ7	SwissProt
Mus musculus	-	674830	O88561	UniProt
Mus musculus	-	675015	Q91VE0	UniProt
Mus musculus	-	675688	Q924N5	UniProt
Mus musculus	-	675690	Q61193	UniProt
Mycobacterium tuberculosis	-	691308	-	-
Notothenia coriiceps	-	661519	-	-
Oryctolagus cuniculus	-	636, 650399	-	-
Photinus pyralis	-	658314, 658709	-	-
Photinus pyralis	North American firefly	694271	P08659	UniProt
Pichia pastoris	-	742	-	-
Pisum sativum	-	746	-	-
Plasmodium falciparum	-	675872	-	-
Plasmodium knowlesi	-	747	-	-
Pseudomonas aeruginosa	-	748	-	-
Pseudomonas aeruginosa	FadD1; gene FadD1	716680	Q9HYU4	UniProt
Pseudomonas aeruginosa	FadD2; gene FadD2	716680	Q9HYU3	UniProt
Pseudomonas chlororaphis	strain B23, gene acsA	693035	Q5CD72	UniProt
Pseudomonas chlororaphis B23	strain B23, gene acsA	693035	Q5CD72	UniProt
Rattus norvegicus	-	649789, 652138, 652139, 661284, 662330, 662463, 662994, 671244, 675554, 732, 733, 734, 736, 737, 738, 748, 749, 750, 752, 754, 755, 756, 757, 758, 760, 762, 763, 764, 765	-	-
Rattus norvegicus	-	653671	Q924N5	Uniprot
Rattus norvegicus	-	662463, 672419, 675267	O88813	UniProt
Rattus norvegicus	-	671234, 674710, 675267	P18163	UniProt
Rattus norvegicus	-	672417, 672419, 675267	O35547	SwissProt
Rattus norvegicus	-	675267	P33124	UniProt
Rattus norvegicus	-	675267, 675688	Q63151	SwissProt
Rattus norvegicus	ACS3, one of multiple form of the enzyme in brain	740	Q63151	SwissProt
Rattus norvegicus	isoenzyme ACS1; isoenzyme ACS2	662225	P33124	UniProt
Rattus norvegicus	isoenzyme ACSL3; isoenzyme ACSL6_v1; isoenzyme ACSL6_v2	661181	P33124	UniProt
Rattus norvegicus	isozyme ACSL5	715835	O88813	UniProt
Rattus norvegicus	long chain acyl-CoA synthetase 1; long chain acyl-CoA synthetase 2; long chain acyl-CoA synthetase 4; long chain acyl-CoA synthetase 5	662185	-	-
Rattus norvegicus	long chain acyl-CoA synthetase 3	662185	Q63151	SwissProt
Saccharomyces cerevisiae	-	672418, 672419, 744	-	-
Saccharomyces cerevisiae	-	672419	P38137, P38225, P39518	UniProt
Sus scrofa	Iberian Guadyerbas x Landrace cross breed	671335	-	-
Thalassiosira pseudonana	-	663142	-	-
Thermus thermophilus	strain HB8	662243	-	-
Tribolium castaneum	red flour beetle	694271	-	-
Trypanosoma brucei	-	649717	-	-
Trypanosoma brucei	strain 427	662797	-	-
Trypanosoma brucei 427	strain 427	662797	-	-
Ulmus sp.	elm	745	-	-
Yarrowia lipolytica	2 enzyme forms: long-chain acyl-CoA synthetase I and long-chain acyl-CoA synthetase II	759	-	-
Zea mays	-	745	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
malfunction	Homo sapiens	-	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	714313
malfunction	Caenorhabditis elegans	-	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	714677
malfunction	Drosophila melanogaster	-	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	714799
malfunction	Rattus norvegicus	O88813	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	715835
malfunction	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	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; 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	716680
physiological function	Mortierella alpina	C8KHM6	a MALCE1 gene-silenced strain exhibits a low content of octadecanoic acid and a high content of hexadecanoic acid	701851
physiological function	Homo sapiens	-	ACSL5 plays a role in promoting fatty acid-induced lipoapoptosis in hepatocytes as important mechanism in fatty liver-related disorders	714313
physiological function	Caenorhabditis elegans	-	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	714677
physiological function	Drosophila melanogaster	-	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	714799
physiological function	Homo sapiens	-	ACSL3 shRNA, but not ACSL1 shRNA, inhibits the induction of lipid accumulation	715715
physiological function	Rattus norvegicus	O88813	ACSL5 may have an anabolic role in lipid metabolism	715835
physiological function	Arabidopsis thaliana	-	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	716538
physiological function	Homo sapiens	-	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	716813
metabolism	Homo sapiens	-	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	714313
additional information	Emericella nidulans	-	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	713991
additional information	Caulobacter vibrioides	-	fatty acid uptake rates in the organism, overview	713994
additional information	Homo sapiens	-	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	714605
additional information	Caenorhabditis elegans	-	mutation of nhr-25 suppresses the fatty acid uptake phenotypes of acs-3(ft5) animals, overview	714677
additional information	Homo sapiens	-	isozyme ACSL4, EC 6.2.1.15, overexpression does not affect levels of ACSL3, ACSL1, and ACSL5	715838
additional information	Arabidopsis thaliana	-	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	716538
additional information	Homo sapiens	-	FACL3 protein expression and its regulation by 1alpha,25(OH)2D3 and its synthetic analogues EB1089 and CB1093 in prostate cancer cells, overview	716813

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
arachidonic acid + ATP + CoA	arachidonoyl-CoA + AMP + diphosphate		Luciola cruciata	-	-	658709	-	-	?
ATP + (11Z)-eicosenoate + CoA	AMP + diphosphate + (11Z)-eicosenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (15Z)-tetracosenoate + CoA	AMP + diphosphate + (15Z)-tetracosenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + CoA	AMP + diphosphate + (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA	AMP + diphosphate + (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (6Z)-octadecenoate + CoA	AMP + diphosphate + (6Z)-octadecenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (6Z,12Z, 15Z)-octadecatrienoate + CoA	AMP + diphosphate + (6Z,12Z,15Z)-octadecatrienoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (6Z,9Z,12Z)-octadecatrienoate + CoA	AMP + diphosphate + (6Z,9Z,12Z)-octadecatrienoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (9E)-octadecenoate + CoA	AMP + diphosphate + (9E)-octadecenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (9Z)-hexadecenoate + CoA	AMP + diphosphate + (9Z)-hexadecenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (9Z)-hexadecenoate + CoA	AMP + diphosphate + (9Z)-hexadecenoyl-CoA		Mortierella alpina	C8KHM6	-	701851	-	-	?
ATP + (9Z)-octadecenoate + CoA	AMP + diphosphate + (9Z)-octadecenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (9Z)-tetradecenoate + CoA	AMP + diphosphate + (9Z)-tetradecenoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (9Z,12Z)-octadecadienoate + CoA	AMP + diphosphate + (9Z,12Z)-octadecadienoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + (9Z,12Z)-octadecadienoate + CoA	AMP + diphosphate + (9Z,12Z)-octadecadienoyl-CoA		Mortierella alpina	C8KHM6	-	701851	-	-	?
ATP + (9Z,12Z,15Z)-octadecatrienoate + CoA	AMP + diphosphate + (9Z,12Z,15Z)-octadecatrienoyl-CoA		Mortierella alpina	C8KHM6	-	701851	-	-	?
ATP + (R)-ibuprofen + CoA	AMP + diphosphate + (R)-ibuprofenoyl-CoA		Rattus norvegicus	-	9% of the activity with palmitate, (R)-ibuprofenoyl-CoA synthetase and long-chain acyl-CoA synthetase are identical enzymes that are involved in the metabolism of various xenobiotics	649789	-	649789	?
ATP + 1,12-dodecanedioic acid + CoA	AMP + diphosphate + ?		Rattus norvegicus	-	-	738	-	738	-
ATP + 12-oxo-phytodienoic acid + CoA	AMP + diphosphate + 12-oxo-phytodienoyl-CoA		Arabidopsis thaliana	-	-	693420	-	-	?
ATP + 16-hydroxypalmitic acid + CoA	AMP + diphosphate + 16-hydroxypalmitoyl-CoA		Arabidopsis thaliana	-	isoenzyme LACS2	663058	-	-	?
ATP + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-hexanoic acid + CoA	AMP + diphosphate + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-hexanoyl-CoA		Arabidopsis thaliana	-	-	693420	-	-	?
ATP + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-octanoic acid + CoA	AMP + diphosphate + 3-oxo-2(2'-[Z]-pentenyl)cyclopentane-1-octanoyl-CoA		Arabidopsis thaliana	-	preferred substrate	693420	-	-	?
ATP + acylate + CoA	AMP + diphosphate + acyl-CoA		Homo sapiens	-	-	714605	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Mus musculus	-	-	671606, 672182	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Homo sapiens	Q5FVE4	-	671606	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Homo sapiens	Q9UKU0	-	672807	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Rattus norvegicus	Q63151	-	740	-	-	-
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Rattus norvegicus	-	-	750	-	-	-
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Rattus norvegicus	Q924N5	-	653671	-	653671	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Rattus norvegicus	P33124	-	661181	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Plasmodium knowlesi	-	-	747	-	-	-
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Drosophila melanogaster	Q9VCC6	-	672684	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Homo sapiens	O60488	-	673484	-	-	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Rattus norvegicus	-	85% of the activity with palmitate	649789	-	649789	?
ATP + arachidonate + CoA	AMP + diphosphate + arachidonoyl-CoA		Rattus norvegicus	O35547	the activity with arachidonate is twice as high as with palmitate	672417	-	-	?
ATP + decanoate + CoA	AMP + diphosphate + decanoyl-CoA		Escherichia coli	-	-	739, 751, 761	-	-	-
ATP + decanoate + CoA	AMP + diphosphate + decanoyl-CoA		Escherichia coli	-	-	652285	-	652285	?
ATP + decanoate + CoA	AMP + diphosphate + decanoyl-CoA		Zea mays, Ulmus sp., Brassica napus	-	-	745	-	-	-
ATP + decanoate + CoA	AMP + diphosphate + decanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + decanoate + CoA	AMP + diphosphate + decanoyl-CoA		Drosophila melanogaster	Q9VCC6	-	672684	-	-	?
ATP + decanoate + CoA	AMP + diphosphate + decanoyl-CoA		Yarrowia lipolytica	-	ineffective	759	-	-	-
ATP + decenoate + CoA	AMP + diphosphate + decenoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + dinor-12-oxo-phytodienoic acid + CoA	AMP + diphosphate + dinor-12-oxo-phytodienoyl-CoA		Arabidopsis thaliana	-	-	693420	-	-	?
ATP + docosahexaenoate + CoA	AMP + diphosphate + docosahexaenoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + docosahexaneoate + CoA	AMP + diphosphate + docosahexaenoyl-CoA		Rattus norvegicus	-	-	755	-	-	-
ATP + docosahexaneoate + CoA	AMP + diphosphate + docosahexaenoyl-CoA		Thalassiosira pseudonana	-	-	663142	-	-	?
ATP + docosahexaneoate + CoA	AMP + diphosphate + docosahexaenoyl-CoA		Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519	-	-	?
ATP + docosenoate + CoA	AMP + diphosphate + docosenoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + dodecanoate + CoA	AMP + diphosphate + dodecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + dodecanoate + CoA	AMP + diphosphate + dodecanoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + eicosapentaenoate + CoA	AMP + diphosphate + eicosapentaenoyl-CoA		Rattus norvegicus	Q63151	-	740	-	-	-
ATP + eicosapentaenoate + CoA	AMP + diphosphate + eicosapentaenoyl-CoA		Rattus norvegicus	-	-	750	-	-	-
ATP + eicosapentaenoate + CoA	AMP + diphosphate + eicosapentaenoyl-CoA		Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519	-	-	?
ATP + eicosapentaenoate + CoA	AMP + diphosphate + eicosapentaenoyl-CoA		Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421	-	-	?
ATP + elaidate + CoA	AMP + diphosphate + elaiodyl-CoA		Rattus norvegicus	-	-	754	-	-	-
ATP + fatty acid + 4'-phosphopantetheine	AMP + diphosphate + acyl-4'-phosphopantetheine		Rattus norvegicus	-	-	758, 764	-	-	-
ATP + fatty acid + 4'-phosphopantetheine	AMP + diphosphate + acyl-4'-phosphopantetheine		Yarrowia lipolytica	-	-	759	-	-	-
ATP + fatty acid + dephospho-CoA	AMP + diphosphate + acyl-dephospho-CoA		Rattus norvegicus	-	-	758, 764	-	-	-
ATP + fatty acid + dephospho-CoA	AMP + diphosphate + acyl-dephospho-CoA		Sus scrofa	-	-	671335	-	-	?
ATP + fatty acid + dephospho-CoA	AMP + diphosphate + acyl-dephospho-CoA		Yarrowia lipolytica	-	-	759	-	-	-
ATP + fatty acid + dephospho-CoA	AMP + diphosphate + acyl-dephospho-CoA		Homo sapiens	P33121	-	671234	-	-	?
ATP + fatty acid + N6-etheno-CoA	AMP + diphosphate + acyl-N6-etheno-CoA		Yarrowia lipolytica	-	-	759	-	-	-
ATP + fatty acid + pantetheine	AMP + diphosphate + acyl-pantetheine		Rattus norvegicus	-	-	758, 764	-	-	-
ATP + fatty acid + pantetheine	AMP + diphosphate + acyl-pantetheine		Yarrowia lipolytica	-	-	759	-	-	-
ATP + heptadecanoate + CoA	AMP + diphosphate + heptadecanoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + heptadecanoate + CoA	AMP + diphosphate + heptadecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + hexadecanoate + CoA	AMP + diphosphate + hexadecanoyl-CoA		Mus musculus	-	-	714678	-	-	?
ATP + hexadecanoate + CoA	AMP + diphosphate + hexadecanoyl-CoA		Homo sapiens	-	-	714313	-	-	?
ATP + hexadecanoate + CoA	AMP + diphosphate + hexadecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + hexadecanoate + CoA	AMP + diphosphate + hexadecanoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + hexanoate + CoA	AMP + diphosphate + hexanoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + hexanoate + CoA	AMP + diphosphate + hexanoyl-CoA		Rattus norvegicus	-	4% of the activity with palmitate	649789	-	649789	?
ATP + jasmonic acid + CoA	AMP + diphosphate + jasmonyl-CoA		Arabidopsis thaliana	-	-	693420	-	-	?
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Escherichia coli	-	-	751, 761	-	-	-
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Homo sapiens	-	-	672490	-	-	?
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Rattus norvegicus	Q63151	-	740	-	-	-
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Rattus norvegicus	-	-	754, 756	-	-	-
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Zea mays, Ulmus sp., Brassica napus	-	-	745	-	-	-
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421	-	-	?
ATP + laurate + CoA	AMP + diphosphate + lauroyl-CoA		Drosophila melanogaster	Q9VCC6	-	672684	-	-	?
ATP + lignocerate + CoA	AMP + diphosphate + lignoceroyl-CoA		Mus musculus	-	-	671606	-	-	?
ATP + lignocerate + CoA	AMP + diphosphate + lignoceroyl-CoA		Homo sapiens	Q5FVE4	-	671606	-	-	?
ATP + lignocerate + CoA	AMP + diphosphate + lignoceroyl-CoA		Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419	-	-	?
ATP + lignocerate + CoA	AMP + diphosphate + lignoceroyl-CoA		Mus musculus	O88561	-	674830	-	-	?
ATP + linoleate + CoA	AMP + diphosphate + linoleoyl-CoA		Mus musculus	-	-	671606	-	-	?
ATP + linoleate + CoA	AMP + diphosphate + linoleoyl-CoA		Homo sapiens	Q5FVE4	-	671606	-	-	?
ATP + linoleate + CoA	AMP + diphosphate + linoleoyl-CoA		Rattus norvegicus	-	-	750, 765	-	-	-
ATP + linoleate + CoA	AMP + diphosphate + linoleoyl-CoA		Plasmodium knowlesi	-	-	747	-	-	-
ATP + linoleate + CoA	AMP + diphosphate + linoleoyl-CoA		Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519	-	-	?
ATP + linoleate + CoA	AMP + diphosphate + lineoyl-CoA		Homo sapiens	-	-	672490	-	-	?
ATP + linoleate + CoA	AMP + diphosphate + lineoyl-CoA		Drosophila melanogaster	Q9VCC6	-	672684	-	-	?
ATP + linoleic acid + CoA	AMP + diphosphate + linoleoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + linolenate + CoA	AMP + diphosphate + linolenoyl-CoA		Rattus norvegicus	-	-	750, 765	-	-	-
ATP + linolenate + CoA	AMP + diphosphate + linolenoyl-CoA		Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519	-	-	?
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	-	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	760	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	-	18:3(n-3)	734	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Escherichia coli	-	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	761	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	-	18:1	756	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Zea mays	-	18:1	745	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Yarrowia lipolytica	-	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	759	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Escherichia coli	-	trans-DELTA9-18:1 fatty acid	753	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	-	substrate specificity of microsomal and mitochondrial enzyme are indistinguishable	764	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Zea mays, Ulmus sp., Brassica napus	-	no activity with 18:1 and 22:1 fatty acid	745	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Escherichia coli	-	trans-DELTA9-16:1 fatty acid	753	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	-	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	756	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	Q63151	utilizes laurate and myristate most efficientyl among C8-C22 saturated fatty acids and arachidonate and eicosapentaenoate among the C16-C20 unsaturated fatty acids	740	-	-	-
ATP + long-chain carboxylic acid + CoA	AMP + diphosphate + acyl-CoA		Rattus norvegicus	-	20:3(n-6)	734	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Saccharomyces cerevisiae	-	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	744	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Homo sapiens	-	essential role in animal cell proliferation	741	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Yarrowia lipolytica	-	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	759	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Rattus norvegicus	-	physiological significance of enzyme in fatty acid metabolism	733	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Rattus norvegicus	-	enzyme is essential for both oxidation and esterification of fatty acids	736	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Escherichia coli	-	enzyme plays a pivotal role in cellular homeostasis, particular in lipid metabolism	739	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Escherichia coli	-	activates exogenous long-chain fatty acids concomitant with their transport across the inner membrane into metabolically active CoA thioesters	743	-	-	-
ATP + long-chain carboxylic acid + CoA	?		Rattus norvegicus	Q63151	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	740	-	-	-
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Escherichia coli	-	-	739, 751, 761	-	-	-
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Homo sapiens	-	-	672490	-	-	?
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Rattus norvegicus	Q63151	-	740	-	-	-
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Rattus norvegicus	-	-	749, 754	-	-	-
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Rattus norvegicus	Q924N5	-	653671	-	653671	?
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Saccharomyces cerevisiae	-	-	744	-	-	-
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Zea mays, Ulmus sp., Brassica napus	-	-	745	-	-	-
ATP + myristate + CoA	AMP + diphosphate + myristoyl-CoA		Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421	-	-	?
ATP + myristic acid + CoA	AMP + diphosphate + myristoyl-CoA		Arabidopsis thaliana	-	-	693420	-	-	?
ATP + n-tetracosanoic acid + CoA	AMP + diphosphate + n-tetracosanoyl-CoA		Mus musculus	-	-	662341	-	-	?
ATP + nonanoate + CoA	AMP + diphosphate + nonanoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + o-succinyl-1-benzoate + CoA	AMP + diphosphate + o-succinyl-1-benzoyl-CoA		Mycobacterium tuberculosis	-	a step in the bacterial biosynthesis of menaquinone from chorismate, pathway overview, a two-step reaction via o-succinyl-1-benzoyl-AMP intermediate	691308	-	-	?
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Mus musculus	-	-	714678	-	-	?
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Caulobacter vibrioides	-	-	713994	-	-	?
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Rattus norvegicus	O88813	-	715835	-	-	?
ATP + octanoate + CoA	AMP + diphosphate + octanoyl-CoA		Escherichia coli	-	-	751, 761	-	-	-
ATP + octanoate + CoA	AMP + diphosphate + octanoyl-CoA		Rattus norvegicus	-	-	754	-	-	-
ATP + octanoate + CoA	AMP + diphosphate + octanoyl-CoA		Drosophila melanogaster	Q9VCC6	-	672684	-	-	?
ATP + octanoate + CoA	AMP + diphosphate + octanoyl-CoA		Yarrowia lipolytica	-	ineffective	759	-	-	-
ATP + octanoate + CoA	AMP + diphosphate + octanoyl-CoA		Rattus norvegicus	-	20% of the activity with palmitate	649789	-	649789	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Mus musculus	-	-	662593, 671606	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Escherichia coli	-	-	739, 761	-	-	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Escherichia coli	-	-	652285	-	652285	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Homo sapiens	Q5FVE4	-	671606	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Homo sapiens	-	-	672490	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	-	-	748	-	748	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	-	-	749, 750, 754, 765	-	-	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	Q924N5	-	653671	-	653671	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	P33124	-	661181	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	Q63151	-	662185	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Saccharomyces cerevisiae	-	-	672418	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Oryctolagus cuniculus	-	-	636	-	-	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Pseudomonas aeruginosa	-	-	748	-	748	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Plasmodium knowlesi	-	-	747	-	747	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Yarrowia lipolytica	-	-	759	-	-	-
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Chaenocephalus aceratus	-	-	661519	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	-	-	675688	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Notothenia coriiceps	-	-	661519	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Homo sapiens	O95573	-	674910	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	O88813	-	662463	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Drosophila melanogaster	Q9VCC6	-	672684	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Rattus norvegicus	-	-	674710	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Homo sapiens	Q6P1M0	-	675015	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Mus musculus	Q91VE0	-	675015	-	-	?
ATP + oleate + CoA	AMP + diphosphate + oleoyl-CoA		Mus musculus	Q924N5	-	675688	-	-	?
ATP + oleic acid + CoA	AMP + diphosphate + oleoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Mus musculus	-	-	662341	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Escherichia coli	-	-	751, 761	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Homo sapiens	-	-	662072, 672490	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	732, 736	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	737	-	737	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	738	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	Q63151	-	740	-	740	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	749, 750	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	752	-	752	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	754, 755, 756, 757	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	762	-	762	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	763	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	764	-	764	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	765	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	649789	-	649789	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	652138	-	652138	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	652139	-	652139	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	Q924N5	-	653671	-	653671	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	P33124	-	661181	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Pisum sativum	-	-	746	-	746	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Zea mays	-	-	745	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Arabidopsis thaliana	-	-	663058	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Ulmus sp., Brassica napus	-	-	745	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Plasmodium knowlesi	-	-	747	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Yarrowia lipolytica	-	-	759	-	-	-
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Chaenocephalus aceratus	-	-	661519	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	P33124, Q63151	-	675267	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	675688	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Notothenia coriiceps	-	-	661519	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	O35547	-	672417	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Rattus norvegicus	-	-	674710	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Mus musculus	O88561	-	674830	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Mus musculus	Q924N5	-	675688	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Mus musculus	-	highest activity on palmitate	671606	-	-	?
ATP + palmitate + CoA	AMP + diphosphate + palmitoyl-CoA		Homo sapiens	Q5FVE4	highest activity on palmitate	671606	-	-	?
ATP + palmitoleate + CoA	AMP + diphosphate + palmitolenoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + palmitoleate + CoA	AMP + diphosphate + palmitolenoyl-CoA		Rattus norvegicus	-	-	765	-	-	-
ATP + palmitoleate + CoA	AMP + diphosphate + palmitolenoyl-CoA		Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519	-	-	?
ATP + pentadecanoate + CoA	AMP + diphosphate + pentadecanoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + pentadecanoate + CoA	AMP + diphosphate + pentadecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + pristanic acid + CoA	AMP + diphosphate + pristanoyl-CoA		Rattus norvegicus	-	-	738	-	738	-
ATP + stearate + CoA	AMP + diphosphate + stearoyl-CoA		Escherichia coli	-	-	751, 761	-	-	-
ATP + stearate + CoA	AMP + diphosphate + stearoyl-CoA		Homo sapiens	-	-	672490	-	-	?
ATP + stearate + CoA	AMP + diphosphate + stearoyl-CoA		Rattus norvegicus	-	-	734, 749, 754, 756	-	-	-
ATP + stearate + CoA	AMP + diphosphate + stearoyl-CoA		Plasmodium knowlesi	-	-	747	-	-	-
ATP + tetradecanoate + CoA	AMP + diphosphate + tetradecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + tetradecanoate + CoA	AMP + diphosphate + tetradecanoyl-CoA		Brassica napus	Q9FNT6	-	653493	-	653493	?
ATP + tridecanoate + CoA	AMP + diphosphate + tridecanoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + tridecanoate + CoA	AMP + diphosphate + tridecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
ATP + undecanoate + CoA	AMP + diphosphate + undecanoyl-CoA		Escherichia coli	-	-	761	-	-	-
ATP + undecanoate + CoA	AMP + diphosphate + undecanoyl-CoA		Trypanosoma brucei	-	-	649717	-	649717	?
dATP + fatty acid + CoA	dAMP + diphosphate + acyl-CoA		Rattus norvegicus	-	-	758, 764	-	-	-
dATP + fatty acid + CoA	dAMP + diphosphate + acyl-CoA		Yarrowia lipolytica	-	-	759	-	-	-
decanoic acid + ATP + CoA	decanoyl-CoA + AMP + diphosphate		Photinus pyralis, Luciola cruciata	-	-	658314	-	-	?
lauric acid	?		Drosophila melanogaster	-	-	697221	-	-	?
lauric acid + ATP + CoA	lauroyl-CoA + AMP + diphosphate		Photinus pyralis, Luciola cruciata	-	-	658314	-	-	?
linoleic acid + ATP + CoA	linoleoyl-CoA + AMP + diphosphate		Luciola cruciata	-	-	658709	-	-	?
linoleic acid + ATP + CoA	linoleoyl-CoA + AMP + diphosphate		Drosophila melanogaster	-	-	697221	-	-	?
linolenic acid + ATP + CoA	linolenoyl-CoA + AMP + diphosphate		Luciola cruciata	-	-	658709	-	-	?
luciferin + O2 + ATP	oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv		Photinus pyralis, Luciola cruciata	-	-	658709	-	-	?
myristic acid + ATP + CoA	myristoyl-CoA + AMP + diphosphate		Photinus pyralis, Luciola cruciata	-	-	658314	-	-	?
oleic acid + ATP + CoA	oleoyl-CoA + AMP + diphosphate		Luciola cruciata	-	-	658709	-	-	?
luciferin + O2 + ATP	oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv		Photinus pyralis, Luciola cruciata	-	the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism	658709	-	-	?
additional information	?	-	Rattus norvegicus	Q924N5	no activity for the very long chain fatty acid, lignoceric acid, and a medium chain fatty acid, decanoic acid	653671	-	653671	?
additional information	?	-	Trypanosoma brucei	-	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	649717	-	649717	?
additional information	?	-	Brassica napus	Q9FNT6	the enzyme ACS6 preferrs long-chain fatty acids that contain a cis-9 double bond	653493	-	653493	?
additional information	?	-	Rattus norvegicus	-	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	652139	-	652139	?
additional information	?	-	Mus musculus	-	lipidosin may mediate the link between adrenoleukodystrophy protein dysfunction and the impairment of fatty acid metabolism in X�linked adrenoleukodystrophy	649559	-	649559	?
additional information	?	-	Escherichia coli	-	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	652285	-	652285	?
additional information	?	-	Photinus pyralis, Luciola cruciata	-	no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid	658314	-	-	-
additional information	?	-	Rattus norvegicus	-	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	662330	-	-	-
additional information	?	-	Escherichia coli	-	fatty acyl-CoA synthetase facilitates long chain fatty acid permeation of the inner membrane by a vectorial thioesterification	662226	-	-	-
additional information	?	-	Rattus norvegicus	-	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	661284	-	-	-
additional information	?	-	Mus musculus	-	in vivo the loss of FATP4-mediated very long chain fatty acid uptake and/or esterification may underlie the null phenotype	662341	-	-	-
additional information	?	-	Mus musculus	-	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	662593	-	-	-
additional information	?	-	Rattus norvegicus	-	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	662994	-	-	-
additional information	?	-	Arabidopsis thaliana	-	lacs2-1 mutation results in a defective cutin layer	663058	-	-	-
additional information	?	-	Arabidopsis thaliana	-	peroxisomal acyl-CoA synthetase activity is essential for seedling development	663057	-	-	-
additional information	?	-	Homo sapiens	-	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	660874	-	-	-
additional information	?	-	Mus musculus	-	transcription of GR-LACS gene requires an Sp1/Sp3 binding element downstream of the transcriptional start sites which is essential for basal activity	661822	-	-	-
additional information	?	-	Rattus norvegicus	-	no activity for lignoceric acid	675688	-	-	-
additional information	?	-	Mus musculus	Q924N5	no activity for lignoceric acid	675688	-	-	-
additional information	?	-	Homo sapiens	-	octanoate and decanoate are ineffective substrates	672490	-	-	-
additional information	?	-	Photinus pyralis	P08659	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+	694271	-	-	-
additional information	?	-	Tribolium castaneum	-	luciferase shows beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea	694271	-	-	-
additional information	?	-	Mycobacterium tuberculosis	-	the acyl-CoA synthetase is involved in bacterial menaquinone biosynthesis	691308	-	-	-
additional information	?	-	Arabidopsis thaliana	-	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, 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	693420	-	-	-
additional information	?	-	Pseudomonas chlororaphis	Q5CD72	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	693035	-	-	-
additional information	?	-	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids	716680	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
ATP + (R)-ibuprofen + CoA	AMP + diphosphate + (R)-ibuprofenoyl-CoA		Rattus norvegicus	-	(R)-ibuprofenoyl-CoA synthetase and long-chain acyl-CoA synthetase are identical enzymes that are involved in the metabolism of various xenobiotics	649789	-	649789
ATP + acylate + CoA	AMP + diphosphate + acyl-CoA		Homo sapiens	-	-	714605	-	-
ATP + hexadecanoate + CoA	AMP + diphosphate + hexadecanoyl-CoA		Mus musculus	-	-	714678	-	-
ATP + hexadecanoate + CoA	AMP + diphosphate + hexadecanoyl-CoA		Homo sapiens	-	-	714313	-	-
ATP + long-chain carboxylic acid + CoA	?		Saccharomyces cerevisiae	-	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	744	-	-
ATP + long-chain carboxylic acid + CoA	?		Homo sapiens	-	essential role in animal cell proliferation	741	-	-
ATP + long-chain carboxylic acid + CoA	?		Yarrowia lipolytica	-	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	759	-	-
ATP + long-chain carboxylic acid + CoA	?		Rattus norvegicus	-	physiological significance of enzyme in fatty acid metabolism	733	-	-
ATP + long-chain carboxylic acid + CoA	?		Rattus norvegicus	-	enzyme is essential for both oxidation and esterification of fatty acids	736	-	-
ATP + long-chain carboxylic acid + CoA	?		Escherichia coli	-	enzyme plays a pivotal role in cellular homeostasis, particular in lipid metabolism	739	-	-
ATP + long-chain carboxylic acid + CoA	?		Escherichia coli	-	activates exogenous long-chain fatty acids concomitant with their transport across the inner membrane into metabolically active CoA thioesters	743	-	-
ATP + long-chain carboxylic acid + CoA	?		Rattus norvegicus	Q63151	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	740	-	-
ATP + o-succinyl-1-benzoate + CoA	AMP + diphosphate + o-succinyl-1-benzoyl-CoA		Mycobacterium tuberculosis	-	a step in the bacterial biosynthesis of menaquinone from chorismate, pathway overview	691308	-	-
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Mus musculus	-	-	714678	-	-
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Caulobacter vibrioides	-	-	713994	-	-
ATP + octadecanoate + CoA	AMP + diphosphate + octadecanoyl-CoA		Rattus norvegicus	O88813	-	715835	-	-
luciferin + O2 + ATP	oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv		Photinus pyralis, Luciola cruciata	-	the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism	658709	-	-
additional information	?	-	Rattus norvegicus	-	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	652139	-	652139
additional information	?	-	Mus musculus	-	lipidosin may mediate the link between adrenoleukodystrophy protein dysfunction and the impairment of fatty acid metabolism in X�linked adrenoleukodystrophy	649559	-	649559
additional information	?	-	Escherichia coli	-	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	652285	-	652285
additional information	?	-	Rattus norvegicus	-	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	662330	-	-
additional information	?	-	Escherichia coli	-	fatty acyl-CoA synthetase facilitates long chain fatty acid permeation of the inner membrane by a vectorial thioesterification	662226	-	-
additional information	?	-	Rattus norvegicus	-	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	661284	-	-
additional information	?	-	Mus musculus	-	in vivo the loss of FATP4-mediated very long chain fatty acid uptake and/or esterification may underlie the null phenotype	662341	-	-
additional information	?	-	Mus musculus	-	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	662593	-	-
additional information	?	-	Rattus norvegicus	-	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	662994	-	-
additional information	?	-	Arabidopsis thaliana	-	lacs2-1 mutation results in a defective cutin layer	663058	-	-
additional information	?	-	Arabidopsis thaliana	-	peroxisomal acyl-CoA synthetase activity is essential for seedling development	663057	-	-
additional information	?	-	Homo sapiens	-	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	660874	-	-
additional information	?	-	Mus musculus	-	transcription of GR-LACS gene requires an Sp1/Sp3 binding element downstream of the transcriptional start sites which is essential for basal activity	661822	-	-
additional information	?	-	Photinus pyralis	P08659	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+	694271	-	-
additional information	?	-	Tribolium castaneum	-	luciferase shows beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea	694271	-	-
additional information	?	-	Mycobacterium tuberculosis	-	the acyl-CoA synthetase is involved in bacterial menaquinone biosynthesis	691308	-	-
additional information	?	-	Arabidopsis thaliana	-	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	693420	-	-
additional information	?	-	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	FadD1 has a substrate preference for long-chain fatty acids, while FadD2 prefers shorter-chain fatty acids	716680	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Rattus norvegicus	-	-	662463, 672417, 674710, 675688, 715835	2D-image
ATP	Mus musculus	-	-	662593, 671606, 672182, 674830, 675015, 675688, 714678	2D-image
ATP	Homo sapiens	-	-	671234, 671606, 672490, 673484, 675015, 714313, 714605	2D-image
ATP	Sus scrofa	-	-	671335	2D-image
ATP	Saccharomyces cerevisiae	-	-	672418, 672419	2D-image
ATP	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	; ; ; ;	672421	2D-image
ATP	Drosophila melanogaster	-	-	672684	2D-image
ATP	Homo sapiens	Q9UKU0	;	672807	2D-image
ATP	Homo sapiens	O95573	; ;	674910	2D-image
ATP	Rattus norvegicus	P33124	; ; ; ;	675267	2D-image
ATP	Mycobacterium tuberculosis	-	-	691308	2D-image
ATP	Pseudomonas chlororaphis	Q5CD72	-	693035	2D-image
ATP	Arabidopsis thaliana	-	-	693420	2D-image
ATP	Caulobacter vibrioides	-	-	713994	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Mg2+	Luciola cruciata, Photinus pyralis	-	required	658709
Mg2+	Homo sapiens	-	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+	662072
Mg2+	Saccharomyces cerevisiae	-	required, 10 mM	672418
Mg2+	Mycobacterium tuberculosis	-	-	691308
Mg2+	Pseudomonas chlororaphis	Q5CD72	-	693035
Mg2+	Arabidopsis thaliana	-	-	693420
Mg2+	Caulobacter vibrioides	-	required	713994
Mg2+	Homo sapiens	-	required	714313, 714605
Mg2+	Pisum sativum	-	required	746
Mg2+	Plasmodium knowlesi	-	Km: 1.554; required	747
Mg2+	Rattus norvegicus	-	Km: 0.555 mM; required	755
Mg2+	Rattus norvegicus	-	most effective activator of all cations	756
Mg2+	Rattus norvegicus	-	maximal activity at 15-20 mM MgCl2, no inhibition at higher concentrations; required	762
Mg2+	Rattus norvegicus	-	required	764, 765
Mn2+	Rattus norvegicus	-	divalent cation required, Mn2+ can replace Mg2+ in activation	762
Salts	Escherichia coli	-	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	753

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2-Bromopalmitate	Rattus norvegicus	-	inhibition can be overcome by addition of phospholipid vesicles	732	2D-image
2-Bromopalmitoyl-CoA	Rattus norvegicus	-	inhibition can be overcome by addition of phospholipid vesicles	732	2D-image
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine	Mycobacterium tuberculosis	-	mechanism of covalent inhibition	691308	2D-image
5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]hexa-1,5-dien-1-yl]sulfonyl)amino]adenosine	Mycobacterium tuberculosis	-	mechanism of covalent inhibition	691308	2D-image
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine	Mycobacterium tuberculosis	-	mechanism of covalent inhibition	691308	2D-image
5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)amino]adenosine	Mycobacterium tuberculosis	-	mechanism of covalent inhibition	691308	2D-image
5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine	Mycobacterium tuberculosis	-	mechanism of covalent inhibition	691308	2D-image
5'-O-([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)adenosine	Mycobacterium tuberculosis	-	mechanism of covalent inhibition	691308	2D-image
AMP	Rattus norvegicus	-	-	762	2D-image
arachidonate	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	inhibits palmitoyl-CoA synthesis at high concentrations	672421	2D-image
arachidonate	Rattus norvegicus	-	inhibition of palmitoyl-CoA synthesis	750	2D-image
arachidonate	Rattus norvegicus	-	-	755	2D-image
arachidonic acid	Drosophila melanogaster	-	concentration above 10 microM	697221	2D-image
ATP	Plasmodium knowlesi	-	above 13.3 mM	747	2D-image
ATP	Rattus norvegicus	-	above 15 mM	762	2D-image
Brij 58	Rattus norvegicus	-	maximal inhibition at 4% detergent	762	2D-image
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	652138	2D-image
diphosphate	Plasmodium knowlesi	-	low inhibition of oleoyl-CoA synthesis	747	2D-image
diphosphate	Rattus norvegicus	-	-	762	2D-image
Docosahexaenoate	Rattus norvegicus	-	unlabeled, inhibition of docosahexaenoate activation	755	2D-image
Eicosa-11,14,17-trienoic acid	Rattus norvegicus	-	competitive inhibitor of palmitoleic acid activation	765	2D-image
Eicosa-5,8,11,14-tetraenoic acid	Rattus norvegicus	-	competitive inhibitor of palmitoleic acid activation	765	2D-image
Eicosa-8,11,14-trienoic acid	Rattus norvegicus	-	competitive inhibitor of palmitoleic acid activation	765	2D-image
Eicosa-8,14-dienoic acid	Rattus norvegicus	-	competitive inhibitor of palmitoleic acid activation	765	2D-image
eicosapentanoate	Rattus norvegicus	-	inhibition of palmitoyl-CoA synthesis	750	-
fatty acids	Rattus norvegicus	-	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	755	2D-image
fatty acids	Rattus norvegicus	-	palmitoleate, oleate and linoleate are competitive inhibitors of the activation of each other	764	2D-image
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	652138	2D-image
Hg2+	Rattus norvegicus	-	-	755	2D-image
Ketoprofen	Rattus norvegicus	-	non-competitive inhibition of the high affinity isoform	737	2D-image
linoleate	Rattus norvegicus	-	inhibition of palmitoyl-CoA synthesis	750	2D-image
linoleic acid	Drosophila melanogaster	-	concentration above 10 microM	697221	2D-image
Naproxen	Rattus norvegicus	-	non-competitive inhibition of the high affinity isoform	737	2D-image
NEM	Rattus norvegicus	-	strongly inhibits ACS5 and weakly inhibits ACS1, no effect on ACS5	652138	2D-image
NEM	Rattus norvegicus	-	ACS4	652139	2D-image
oleate	Rattus norvegicus	-	inhibition of palmitoyl-CoA synthesis	750	2D-image
oleic acid	Drosophila melanogaster	-	concentration above 10 microM	697221	2D-image
oleoyl-CoA	Plasmodium knowlesi	-	inhibition of oleoyl-CoA synthesis	747	2D-image
palmitate	Rattus norvegicus	-	linolenic acid activation	765	2D-image
Pb2+	Rattus norvegicus	-	-	755	2D-image
Perfluorodecanoic acid	Rattus norvegicus	-	no inhibition by short-chain perfluorinated fatty acids	736	2D-image
Perfluorononanoic acid	Rattus norvegicus	-	no inhibition by short-chain perfluorinated fatty acids	736	2D-image
Perfluorooctanoic acid	Rattus norvegicus	-	no inhibition by short-chain perfluorinated fatty acids	736	2D-image
pioglitazone	Rattus norvegicus	-	IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein	652138	2D-image
R-Fenoprofen	Rattus norvegicus	-	mixed inhibition of the high affinity isoform	737	2D-image
R-Ibuprofen	Rattus norvegicus	-	mixed inhibition of the high affinity isoform	737	2D-image
rosiglitazone	Rattus norvegicus	-	IC50: 0.0005 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein	652138	2D-image
Salts	Escherichia coli	-	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	753	-
SDS	Rattus norvegicus	-	-	755	2D-image
Sodium cholate	Rattus norvegicus	-	maximal inhibition at 1% detergent	762	2D-image
Sodium deoxycholate	Rattus norvegicus	-	-	755	2D-image
thiazolidinediones	Rattus norvegicus	-	specific inhibitors of ACS4	652138	2D-image
thiazolidinediones	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	-	672421	2D-image
triacsin	Rattus norvegicus	-	competitive inhibitor of both ACS1 and ACS4	652139	2D-image
Triacsin A	Mus musculus	-	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	692792	2D-image
Triacsin A	Pseudomonas aeruginosa, Rattus norvegicus	-	non-competitive with respect to ATP and coenzyme A	748	2D-image
Triacsin C	Mus musculus	-	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	634	2D-image
Triacsin C	Rattus norvegicus	-	strongly inhibits ACS1 and ACS4, no effect on ACS5	652138	2D-image
Triacsin C	Rattus norvegicus	P33124	IC50: 0.0055 mM	661181	2D-image
Triacsin C	Homo sapiens	-	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	662072	2D-image
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	662341	2D-image
Triacsin C	Mus musculus	-	90% inhibition at 0.02 mM	662593	2D-image
Triacsin C	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	;	672421	2D-image
Triacsin C	Homo sapiens	-	significant inhibiton	672490	2D-image
Triacsin C	Homo sapiens	-	0.02 mM	673484	2D-image
Triacsin C	Homo sapiens	O95573	95% inhibition at 0.005 mM	674910	2D-image
Triacsin C	Mus musculus	-	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	692792	2D-image
Triacsin C	Homo sapiens	-	-	715715	2D-image
Triacsin C	Rattus norvegicus	-	-	748	2D-image
Triacsins	Homo sapiens	-	hierarchy of inhibitory potency in decreasing order: triacsin C, triacsin A, triacsin D/ triacsin B	741	2D-image
Triton X-100	Rattus norvegicus	-	-	672419	2D-image
Triton X-100	Homo sapiens	-	Inhibition of acyl-CoA formation, inhibits ACSL6 isoform 2 (F-Gate) and its N-terminus truncated version, DELTAN-(F-Gate)	714605	2D-image
Triton X-100	Rattus norvegicus	-	slight inhibition when incubated with microsomes at 0�C for 30 min	755	2D-image
Triton X-100	Rattus norvegicus	-	maximal inhibition at 4% detergent	762	2D-image
troglitazone	Rattus norvegicus	-	IC50: 0.0015 mM for ACS1-Flag fusion protein, no effect on ACS4-Flag fusion protein and ACS5-Flag fusion protein	652138	2D-image
troglitazone	Rattus norvegicus	-	ACS4	652139	2D-image
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	662341	2D-image
troglitazone	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	; ; 0.05 mM, 5% inhibition	672421	2D-image
Tween 80	Rattus norvegicus	-	maximal inhibition at 4% detergent	762	2D-image
Zwittergent 3-12	Rattus norvegicus	-	inhibition below the critical micellar concentration, 0.12%. below this concentrations no inhibition	755	2D-image
linolenate	Rattus norvegicus	-	inhibition of palmitoyl-CoA synthesis	750	2D-image
additional information	Rattus norvegicus	-	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	652138	-
additional information	Rattus norvegicus	P33124	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	661181	-
additional information	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	not inhibited by thiazolidinediones; not inhibited by thiazolidinediones; not inhibited by triacsin C; not inhibited by triacsin C; not inhibited by triacsin C	672421	-
additional information	Homo sapiens	-	not inhibited by 4,4,10 beta-trimethyl-trans-decal-3 beta-ol	672490	-
additional information	Mycobacterium tuberculosis	-	design and construction of mechanism-based inhibitors of MenE	691308	-
additional information	Homo sapiens	-	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	714605	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
phosphatidylcholine	Yarrowia lipolytica	-	absolute requirement, acyl-CoA synthetase II	759	2D-image
phosphatidylethanolamine	Yarrowia lipolytica	-	slight stimulation, acyl-CoA synthetase II	759	2D-image
phosphatidylserine	Yarrowia lipolytica	-	slight stimulation, acyl-CoA synthetase II	759	2D-image
Triacsin C	Rattus norvegicus	-	ACSL activity is 17fold higher in the presence of 0.02 mM triacsin C	662463	2D-image
Triton X-100	Rattus norvegicus	-	-	672419	2D-image
Triton X-100	Saccharomyces cerevisiae	P38137, P38225, P39518	-	672419	2D-image
Triton X-100	Rattus norvegicus	-	enhances activity	755	2D-image
alpha-synuclein	Mus musculus	-	0.0063-0.634 mM	672182	-
additional information	Arabidopsis thaliana	-	the enzyme is inducible by wounding	693420	-
additional information	Homo sapiens	-	specific Gate-domain residues are essential for activity, detailed overview	714605	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.167	-	(11Z)-eicosenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.253	-	(15Z)-tetracosenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.222	-	(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.017	-	(5Z,8Z,11Z,14Z)-eicosatetraenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.048	-	(6Z)-octadecenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.02	-	(6Z,12Z, 15Z)-octadecatrienoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.009	-	(6Z,9Z,12Z)-octadecatrienoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.109	-	(9E)-octadecenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.009	-	(9Z)-hexadecenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.024	-	(9Z)-octadecenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.009	-	(9Z)-tetradecenoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.021	-	(9Z,12Z)-octadecadienoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.0314	-	16-hydroxypalmitic acid	Arabidopsis thaliana	-	isoenzyme LACS2	663058	2D-image
0.0375	-	18:3(n-3) fatty acid	Rattus norvegicus	-	-	734	-
0.06	-	20:3(n-6) fatty acid	Rattus norvegicus	-	-	734	-
0.41	0.43	4'-phosphopantetheine	Rattus norvegicus	-	-	758, 764	2D-image
3.3	-	4'-phosphopantetheine	Yarrowia lipolytica	-	-	759	2D-image
0.0065	-	arachidonate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v2	661181	2D-image
0.0089	-	arachidonate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL3	661181	2D-image
0.0193	-	arachidonate	Rattus norvegicus	-	-	750	2D-image
0.0337	-	arachidonate	Mus musculus	-	-	672182	2D-image
0.059	-	arachidonate	Plasmodium knowlesi	-	-	747	2D-image
9.7	-	arachidonate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v1	661181	2D-image
0.025	-	ATP	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.033	-	ATP	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.033	-	ATP	Escherichia coli	-	nonanoate	761	2D-image
0.034	-	ATP	Rattus norvegicus	-	pH 7.5, 37�C, ACS4	652138	2D-image
0.05	-	ATP	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.05	-	ATP	Rattus norvegicus	-	CoA	762	2D-image
0.0516	-	ATP	Saccharomyces cerevisiae	-	in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30�C	672418	2D-image
0.06	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme G219A	652285	2D-image
0.087	-	ATP	Rattus norvegicus	-	wild type enzyme, at 37�C, in 175 mM Tris-HCl, at pH 7.4	672417	2D-image
0.11	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme G216A	652285	2D-image
0.125	-	ATP	Rattus norvegicus	-	mutant L399M, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.13	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme T214A; pH 7.5, 37�C, wild-type enzyme	652285	2D-image
0.185	-	ATP	Rattus norvegicus	-	-	755	2D-image
0.242	-	ATP	Rattus norvegicus	-	mutant Q525K, at 37�C, in 175 mM Tris-HCl, at pH 7.4	672417	2D-image
0.402	-	ATP	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL3	661181	2D-image
0.44	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme K222A	652285	2D-image
0.5	-	ATP	Rattus norvegicus	Q63151	-	740	2D-image
0.5	-	ATP	Yarrowia lipolytica	-	N6-etheno-CoA	759	2D-image
0.502	-	ATP	Rattus norvegicus	-	mutant S291Y, at 37�C, in 175 mM Tris-HCl, at pH 7.4	672417	2D-image
0.53	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme T217A	652285	2D-image
0.649	-	ATP	Rattus norvegicus	-	pH 7.5, 37�C, ACS1	652138	2D-image
0.666	-	ATP	Rattus norvegicus	-	pH 7.5, 37�C, ACS5	652138	2D-image
0.73	-	ATP	Plasmodium knowlesi	-	-	747	2D-image
1.4	-	ATP	Mus musculus	-	-	662341	2D-image
1.48	-	ATP	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v2	661181	2D-image
2.3	2.4	ATP	Rattus norvegicus	-	-	758, 764	2D-image
4.1	-	ATP	Rattus norvegicus	-	at 20 mM MgCl2	762	2D-image
12.21	-	ATP	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v1	661181	2D-image
0.00053	-	CoA	Rattus norvegicus	Q63151	-	740	2D-image
0.0024	-	CoA	Rattus norvegicus	-	pH 7.5, 37�C, ACS5	652138	2D-image
0.0024	-	CoA	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v2	661181	2D-image
0.003	-	CoA	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL3	661181	2D-image
0.0041	-	CoA	Rattus norvegicus	-	pH 7.5, 37�C, ACS4	652138	2D-image
0.00488	-	CoA	Rattus norvegicus	-	-	755	2D-image
0.0064	-	CoA	Rattus norvegicus	-	pH 7.5, 37�C, ACS1	652138	2D-image
0.0064	-	CoA	Rattus norvegicus	-	mutant S291Y, at 37�C, in 175 mM Tris-HCl, at pH 7.4	672417	2D-image
0.0067	-	CoA	Rattus norvegicus	-	wild type enzyme, at 37�C, in 175 mM Tris-HCl, at pH 7.4	672417	2D-image
0.0068	-	CoA	Rattus norvegicus	-	mutant Q525K, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.0072	-	CoA	Rattus norvegicus	-	activation of palmitic acid	765	2D-image
0.0088	-	CoA	Rattus norvegicus	-	mutant L399M, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.0094	-	CoA	Rattus norvegicus	-	activation of oleic acid	765	2D-image
0.0183	-	CoA	Saccharomyces cerevisiae	-	in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30�C	672418	2D-image
0.026	0.028	CoA	Rattus norvegicus	-	-	758, 764	2D-image
0.034	-	CoA	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.035	-	CoA	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.042	-	CoA	Yarrowia lipolytica	-	-	759	2D-image
0.047	-	CoA	Mus musculus	-	-	662341	2D-image
0.048	-	CoA	Plasmodium knowlesi	-	-	747	2D-image
0.053	-	CoA	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
4.7	-	CoA	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v1	661181	2D-image
1.93	-	coenzyme A	Pseudomonas aeruginosa	-	oleate activation	748	2D-image
12.5	13.3	dATP	Rattus norvegicus	-	-	758, 764	2D-image
0.004	-	Decanoate	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.0043	-	Decanoate	Escherichia coli	-	-	761	2D-image
0.0063	-	Decanoate	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.0083	-	Decanoate	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.11	-	dephospho-CoA	Yarrowia lipolytica	-	-	759	2D-image
0.23	0.29	dephospho-CoA	Rattus norvegicus	-	-	758, 764	2D-image
0.1	-	dodecanoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.0155	-	eicosapentaenoate	Rattus norvegicus	-	-	750	2D-image
0.0102	-	heptadecanoate	Escherichia coli	-	-	761	2D-image
0.026	-	Heptanoate	Escherichia coli	-	-	761	2D-image
0.014	-	hexadecanoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.0112	-	Hexanoate	Escherichia coli	-	-	761	2D-image
0.00051	-	laurate	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.0016	-	laurate	Escherichia coli	-	-	761	2D-image
0.0019	-	laurate	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.002	-	laurate	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.00168	-	lauric acid	Drosophila melanogaster	-	-	697221	2D-image
0.00741	-	lauric acid	Photinus pyralis	-	-	658314	2D-image
0.0163	-	lauric acid	Luciola cruciata	-	-	658314	2D-image
0.00222	-	linoleate	Rattus norvegicus	-	-	765	2D-image
0.0128	-	linoleate	Rattus norvegicus	-	-	750	2D-image
0.041	-	linoleate	Plasmodium knowlesi	-	-	747	2D-image
0.041	-	linoleate	Pseudomonas aeruginosa	-	ATP, , oleate activation	748	2D-image
0.00188	-	linoleic acid	Drosophila melanogaster	-	-	697221	2D-image
0.00164	-	linolenate	Rattus norvegicus	-	-	765	2D-image
0.0002	-	myristate	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.0012	-	myristate	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.0021	-	myristate	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.0024	-	myristate	Escherichia coli	-	palmitate	761	2D-image
0.0048	-	n-tetracosanoic acid	Mus musculus	-	-	662341	2D-image
0.061	-	octadecanoate	Caulobacter vibrioides	-	pH 7.5, 30�C	713994	2D-image
0.072	-	octadecanoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.00072	-	Octanoate	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.0059	-	Octanoate	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.0125	-	Octanoate	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.0408	-	Octanoate	Escherichia coli	-	-	761	2D-image
0.00139	-	oleate	Rattus norvegicus	-	-	765	2D-image
0.0051	-	oleate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL3	661181	2D-image
0.0053	-	oleate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v2	661181	2D-image
0.0085	-	oleate	Escherichia coli	-	-	761	2D-image
0.0229	-	oleate	Rattus norvegicus	-	-	750	2D-image
0.03	-	oleate	Plasmodium knowlesi	-	-	747	2D-image
0.0711	-	oleate	Saccharomyces cerevisiae	-	in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30�C	672418	2D-image
3	-	oleate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v1	661181	2D-image
0.101	-	oleic acid	Pseudomonas aeruginosa	-	-	748	2D-image
0.00021	-	palmitate	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.00278	-	palmitate	Rattus norvegicus	-	-	765	2D-image
0.0029	-	palmitate	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.0036	-	palmitate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v2	661181	2D-image
0.0043	-	palmitate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL3	661181	2D-image
0.005	-	palmitate	Rattus norvegicus	-	pH 7.5, 37�C, ACS1	652138	2D-image
0.0054	-	palmitate	Rattus norvegicus	-	pH 7.5, 37�C, ACS4	652138	2D-image
0.0086	-	palmitate	Rattus norvegicus	-	pH 7.5, 37�C, ACS5	652138	2D-image
0.011	-	palmitate	Plasmodium knowlesi	-	-	747	2D-image
0.013	-	palmitate	Mus musculus	-	-	662341	2D-image
0.0143	-	palmitate	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.02	-	palmitate	Rattus norvegicus	-	mutant Q525K, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.0211	-	palmitate	Rattus norvegicus	-	mutant S291Y, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.0238	-	palmitate	Rattus norvegicus	-	mutant L399M, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.0281	-	palmitate	Rattus norvegicus	-	wild type enzyme, at 37�C, in 175 mM Tris-HCl at pH 7.4	672417	2D-image
0.0455	-	palmitate	Rattus norvegicus	-	-	750	2D-image
0.0814	-	palmitate	Arabidopsis thaliana	-	isoenzyme LACS2	663058	2D-image
6	-	palmitate	Rattus norvegicus	P33124	pH 7.4, isoenzyme ACSL6_v1	661181	2D-image
0.0015	-	palmitoleate	Escherichia coli	-	-	761	2D-image
0.00204	-	palmitoleate	Rattus norvegicus	-	-	765	2D-image
1.1	1.2	pantetheine	Rattus norvegicus	-	-	758, 764	2D-image
2.5	-	pantetheine	Yarrowia lipolytica	-	-	759	2D-image
0.0022	-	Pentadecanoate	Escherichia coli	-	-	761	2D-image
0.00017	-	stearate	Escherichia coli	-	acyl-CoA synthetase-4.6	751	2D-image
0.00028	-	stearate	Escherichia coli	-	acyl-CoA synthetase-5.6	751	2D-image
0.0089	-	stearate	Escherichia coli	-	-	761	2D-image
0.0091	-	stearate	Escherichia coli	-	acyl-CoA synthetase-5.0	751	2D-image
0.028	-	stearate	Plasmodium knowlesi	-	-	747	2D-image
0.12	-	stearate	Rattus norvegicus	-	-	734	2D-image
0.01	-	tetradecanoate	Brassica napus	Q9FNT6	pH 8.5, 30�C	653493	2D-image
0.0034	-	tridecanoate	Escherichia coli	-	-	761	2D-image
0.0013	-	Undecanoate	Escherichia coli	-	-	761	2D-image
0.0073	-	linolenate	Rattus norvegicus	-	-	750	2D-image
additional information	-	additional information	Arabidopsis thaliana	-	Michaelis-Menten kinetics	693420	-
additional information	-	additional information	Rattus norvegicus	-	-	760	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.003	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme T214A	652285	2D-image
0.008	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme G216A; pH 7.5, 37�C, mutant enzyme K222A; pH 7.5, 37�C, mutant enzyme T217A	652285	2D-image
0.017	-	ATP	Escherichia coli	-	pH 7.5, 37�C, mutant enzyme G219A	652285	2D-image
0.029	-	ATP	Escherichia coli	-	pH 7.5, 37�C, wild-type enzyme	652285	2D-image
0.278	-	lauric acid	Photinus pyralis	-	-	658314	2D-image
0.651	-	lauric acid	Luciola cruciata	-	-	658314	2D-image
0.5	-	tetradecanoate	Trypanosoma brucei	-	enzyme TbACS1	649717	2D-image
1.1	-	tetradecanoate	Trypanosoma brucei	-	enzyme TbACS3	649717	2D-image
1.2	-	tetradecanoate	Trypanosoma brucei	-	enzyme TbACS4	649717	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
additional information	-	additional information	Homo sapiens	-	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	662072	-

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.0057	-	5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]-5-oxopent-1-en-1-yl]sulfonyl)amino]adenosine	Mycobacterium tuberculosis	-	-	691308	2D-image
0.2	-	5'-deoxy-5'-[([(1E)-5-[2-(methoxycarbonyl)phenyl]hexa-1,5-dien-1-yl]sulfonyl)amino]adenosine	Mycobacterium tuberculosis	-	above	691308	2D-image
0.034	-	5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)amino]adenosine	Mycobacterium tuberculosis	-	-	691308	2D-image
0.2	-	5'-deoxy-5'-[([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)amino]adenosine	Mycobacterium tuberculosis	-	above	691308	2D-image
0.038	-	5'-O-([4-[2-(methoxycarbonyl)phenyl]-4-oxobutanoyl]sulfamoyl)adenosine	Mycobacterium tuberculosis	-	-	691308	2D-image
0.2	-	5'-O-([4-[2-(methoxycarbonyl)phenyl]pent-4-enoyl]sulfamoyl)adenosine	Mycobacterium tuberculosis	-	above	691308	2D-image
0.025	-	cis-9,10-methylene octadecanoic acid	Rattus norvegicus	-	IC50: 0.025 mM for ACS1-Flag fusion protein, 0.03-0.04 mM for ACS4-Flag fusion protein, no effect on ACS5-Flag fusion protein	652138	2D-image
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	652138	2D-image
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	652138	2D-image
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	652138	2D-image
0.00016	-	Triacsin A	Mus musculus	-	inhibition of triacylglycerol synthesis	692792	2D-image
0.00018	-	Triacsin A	Mus musculus	-	inhibition of cholesteryl ester synthesis	692792	2D-image
0.0001	-	Triacsin C	Mus musculus	-	inhibition of triacylglycerol synthesis	692792	2D-image
0.00019	-	Triacsin C	Mus musculus	-	inhibition of cholesteryl ester synthesis	692792	2D-image
0.0055	-	Triacsin C	Rattus norvegicus	P33124	IC50: 0.0055 mM	661181	2D-image
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	662341	2D-image
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	652138	2D-image
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	662341	2D-image

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.00094	-	Caulobacter vibrioides	-	oleoyl-CoA formation, pH 7.5, 30�C	713994
0.017	-	Rattus norvegicus	-	formation of (R)-ibuprofenoyl-CoA	649789
0.121	-	Saccharomyces cerevisiae	-	in the presence of 10 mM MnCl2, at pH 8.0	672418
0.145	-	Saccharomyces cerevisiae	-	in the presence of 10 mM MgCl2, at pH 8.0	672418
0.24	-	Escherichia coli	-	-	761
0.28	-	Rattus norvegicus	-	formation of palmitoyl-CoA	649789
0.57	-	Rattus norvegicus	-	-	763
0.723	-	Mus musculus	-	-	662341
1.103	-	Escherichia coli	-	-	753
1.19	-	Oryctolagus cuniculus	-	-	650399
4.62	-	Rattus norvegicus	Q63151	-	740
10.8	-	Yarrowia lipolytica	-	-	759
26.2	-	Rattus norvegicus	-	mitochondrial enzyme	758, 764
28.7	-	Rattus norvegicus	-	microsomal enzyme	758, 764
additional information	-	Trypanosoma brucei	-	-	662797

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.1	9.6	Yarrowia lipolytica	-	-	759
7.4	9.1	Rattus norvegicus	-	-	758
7.5	8.3	Rattus norvegicus	-	-	762
7.5	8.5	Rattus norvegicus	Q63151	-	740
7.5	8.5	Plasmodium knowlesi	-	-	747
7.5	-	Mus musculus	-	substrate: palmitate	662341
7.5	-	Pseudomonas chlororaphis	Q5CD72	assay at	693035
7.5	-	Caulobacter vibrioides	-	assay at	713994
7.5	-	Homo sapiens	-	assay at	714313
7.8	8.9	Escherichia coli	-	acyl-CoA synthetase-5.0	751
8	-	Homo sapiens	-	assay at	714605
8	-	Rattus norvegicus	-	-	755
8.1	-	Escherichia coli	-	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	751
8.4	-	Rattus norvegicus	-	pristanoyl-CoA formation	738
8.5	9.4	Escherichia coli	-	acyl-CoA synthetase-4.6 has a second optimum at pH 8.1	751

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6	9	Mus musculus	-	about 60% of maximal activity at pH 6.0 and pH 9.0	662341
6	9.8	Rattus norvegicus	-	pH 6: about 50% of maximal activity, pH 8.9: about 60% of maximal activity	762
6.5	8.8	Plasmodium knowlesi	-	6.5: about 50% of maximal activity, 8.8: about 70% of maximal activity	747
7.5	8.5	Drosophila melanogaster	-	-	697221

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.4	8	Rattus norvegicus	-	ACS5	652138
7.4	9	Rattus norvegicus	-	ACS1 and ACS4	652138
20	-	Pseudomonas chlororaphis	Q5CD72	assay at	693035
30	-	Caulobacter vibrioides	-	-	713994
30	-	Homo sapiens	-	assay at	714313, 714605
45	-	Rattus norvegicus	-	-	755

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	-	Drosophila melanogaster	-	estimated from amino acid sequence	672684
7.58	-	Saccharomyces cerevisiae	P38137, P38225, P39518	calculated from amino acid sequence	672419

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
3T3-L1 cell	Mus musculus	-	-	662593
adipocyte	Mus musculus	-	-	662593, 714678
adipocyte	Rattus norvegicus	-	-	662994
adipose tissue	Rattus norvegicus	P33124	gonadal and inguinal adipose tissue	675267
adipose tissue	Rattus norvegicus	-	-	733
adrenal gland	Mus musculus	-	expressed exclusively in brain, adrenal gland and testis	649559
adrenal gland	Rattus norvegicus	-	-	675267, 675554
adrenal gland	Mus musculus	Q924N5	-	675688
adrenal gland	Rattus norvegicus	Q63151	low activity	740
adult	Caenorhabditis elegans	-	tissue expression patterns of acs-3, overview	714677
alveolar cell	Rattus norvegicus	-	type II cell	749
aorta	Oryctolagus cuniculus	-	highly expressed in vascular endothelium	650399
astrocyte	Rattus norvegicus	-	-	675554
backfat	Sus scrofa	-	-	671335
blood platelet	Homo sapiens	-	-	637, 638
blood vessel endothelium	Oryctolagus cuniculus	-	coronary microvessel, cell culture	636
brain	Mus musculus	-	expressed exclusively in brain, adrenal gland and testis	649559
brain	Rattus norvegicus	-	-	649789, 675554, 675688, 755
brain	Rattus norvegicus	P33124	ACSL3 and ACSL6 are the predominant isoforms in brain	661181
brain	Rattus norvegicus	-	;	662185, 675267
brain	Mus musculus	-	-	662341, 672182, 675688
brain	Sus scrofa	-	-	671335
brain	Homo sapiens	Q9UKU0	-	672807
brain	Rattus norvegicus	-	low activity	733
brain	Rattus norvegicus	Q63151	most abundant in	740
brown adipose tissue	Rattus norvegicus	P33124	-	675267
brown adipose tissue	Mus musculus	-	-	714678
CACO-2 cell	Homo sapiens	Q6P1M0	-	675015
COS cell	Homo sapiens	Q6P1M0	-	675015
DU-145 cell	Homo sapiens	-	low FACT3 expression level	716813
duodenal mucosa	Rattus norvegicus	P33124	;	675267
embryo	Brassica napus	Q9FNT6	strong enzyme expression	653493
embryo	Arabidopsis thaliana	-	isozyme LACS8 shows the highest expression level in the embryo	716538
endothelium	Oryctolagus cuniculus	-	highly expressed in vascular endothelium of heart and aorta	650399
epidermal cell	Caenorhabditis elegans	-	-	714677
epidermis	Arabidopsis thaliana	-	isoenzyme LACS2	663058
epididymis	Rattus norvegicus	-	-	733
erythrocyte	Homo sapiens	Q9UKU0	-	672807
erythrocyte	Plasmodium knowlesi	-	of Macaca mulatta or Macaca fascicularis infected with Plasmodium knowlesi	747
flower	Brassica napus	Q9FNT6	strong enzyme expression	653493
germ cell	Mus musculus	-	-	671606
gonad	Rattus norvegicus	P33124	gonadal adipose tissue	675267
gonad	Mus musculus	Q924N5	-	675688
gonad	Rattus norvegicus	-	-	675688
heart	Rattus norvegicus	-	-	649789, 671244, 733, 756
heart	Oryctolagus cuniculus	-	highly expressed in vascular endothelium	650399
heart	Mus musculus	-	-	671244
heart	Sus scrofa	-	-	671335
heart	Mus musculus	Q8JZR0, Q91WC3, Q9CZW4, Q9QUJ7	; ; ; ;	672421
HeLa cell	Homo sapiens	Q6P1M0	-	675015
Hep-3B cell	Homo sapiens	-	-	673484
Hep-G2 cell	Homo sapiens	-	-	671234, 673484, 714313
hepatocyte	Homo sapiens	-	-	672490
hepatocyte	Rattus norvegicus	-	-	674710, 736
hepatoma cell	Rattus norvegicus	-	-	662463
hepatoma cell	Homo sapiens	-	-	673484
hepatoma cell	Homo sapiens	O95573	; ;	674910
HSDM1C1 cell	Mus musculus	-	-	634
Huh-7 cell	Homo sapiens	-	-	672490, 715715
Huh-7 cell	Homo sapiens	O95573	; ;	674910
ileum	Rattus norvegicus	-	-	649789
inguinal canal	Rattus norvegicus	P33124	inguinal adipose tissue	675267
intestine	Mus musculus	-	-	662341
kidney	Rattus norvegicus	-	-	649789, 675267
kidney	Rattus norvegicus	Q63151	low activity	740
kidney	Rattus norvegicus	-	glomeruli	750
larva	Caenorhabditis elegans	-	tissue expression patterns of acs-3, overview	714677
leaf	Arabidopsis thaliana	-	expression is limited to cells of the adaxial and abaxial epidermal layers, isoenzyme LACS2	663058
leaf	Arabidopsis thaliana	-	expression levels of OPCL1	693420
Leydig cell	Rattus norvegicus	-	-	653671, 675688
Leydig cell	Mus musculus	-	-	661822, 671606
liver	Rattus norvegicus	-	high expression	649789
liver	Oryctolagus cuniculus	-	-	650399
liver	Rattus norvegicus	-	-	652139, 671234, 715835, 732, 733, 737, 738, 748, 752, 754, 757, 758, 760, 762, 763, 764, 765
liver	Rattus norvegicus	-	hepatic ACS-5 mRNA is poorly expressed during fasting and diabetes and strongly induced by carbohydrate refeeding and insulin treatment	661284
liver	Homo sapiens	-	-	662072, 714313, 715715
liver	Mus musculus	-	-	662341, 671234
liver	Sus scrofa	-	-	671335
liver	Rattus norvegicus	P33124	; ;	675267
LNCaP cell	Homo sapiens	-	FACL3/ACS3 is the dominant isoform of FACL/ACS expressed in LNCaP cells	660874
LNCaP cell	Homo sapiens	-	-	716813
lung	Rattus norvegicus	-	-	649789, 675267
lung	Mus musculus	-	-	662341
lung	Sus scrofa	-	-	671335
lung	Rattus norvegicus	-	low activity	733, 740
MA-10 cell	Mus musculus	Q61193	-	675690
macrophage	Mus musculus	-	peritoneal	692792
McA-RH7777 cell	Rattus norvegicus	-	-	662463
MDCK cell	Mus musculus	Q91VE0	-	675015
muscle	Rattus norvegicus	P33124	-	675267
myocardium	Mus musculus, Rattus norvegicus	-	-	671244
ovary	Sus scrofa	-	-	671335
ovary	Rattus norvegicus	-	-	675554
ovary	Mus musculus	Q924N5	-	675688
PC-3 cell	Homo sapiens	-	low FACT3 expression level	716813
prostate cancer cell	Homo sapiens	-	-	660874
prostate cancer cell	Homo sapiens	-	FACL3 protein expression and its regulation by 1alpha,25(OH)2D3 and its synthetic analogues EB1089 and CB1093 in prostate cancer cells, overview	716813
Pt-K2 cell	Homo sapiens	Q6P1M0	-	675015
RAJI cell	Homo sapiens	-	-	741
seam cell	Caenorhabditis elegans	-	-	714677
seed	Arabidopsis thaliana	-	LACS1, LACS2, LACS4, LACS8, and LACS9	716538
seed	Brassica napus, Ulmus sp., Zea mays	-	-	745
seed	Pisum sativum	-	-	746
seedling	Arabidopsis thaliana	-	-	663057
Sertoli cell	Mus musculus	-	-	671606
skeletal muscle	Chaenocephalus aceratus, Notothenia coriiceps	-	-	661519
skeletal muscle	Sus scrofa	-	-	671335
skin	Mus musculus	-	-	662341
skin fibroblast	Mus musculus	O88561	-	674830
small intestine	Rattus norvegicus	-	low activity	733, 740
smooth muscle cell	Homo sapiens	-	aortic, levels of isozymes ACSL1, ACSL3, and ACSL5, overview	715838
SNU-354 cell	Homo sapiens	-	-	673484
SNU-368 cell	Homo sapiens	-	-	673484
SNU-398 cell	Homo sapiens	-	-	673484
SNU-423 cell	Homo sapiens	-	-	673484
spleen	Sus scrofa	-	-	671335
stomach	Sus scrofa	-	-	671335
testis	Mus musculus	-	expressed exclusively in brain, adrenal gland and testis	649559
testis	Rattus norvegicus	-	-	653671, 675267, 675554, 734
testis	Mus musculus	-	adult	661822
testis	Sus scrofa	-	-	671335
testis	Homo sapiens	Q5FVE4	exclusively found in testis	671606
testis	Mus musculus	-	-	671606
uterus	Sus scrofa	-	-	671335
white adipose tissue	Rattus norvegicus	P33124	-	675267
merozoite	Babesia bovis	Q6QLU3	-	675867
additional information	Arabidopsis thaliana	-	expressed in young, rapidly expanding tissues, isoenzyme LACS2	663058
additional information	Rattus norvegicus	P33124	not detected in liver	675267
additional information	Rattus norvegicus	O88813	ACSL5 is expressed predominantly in tissues with high rates of triacylglycerol synthesis	715835
additional information	Arabidopsis thaliana	-	tissue distribution of isozyme expression, overview	716538

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
chloroplast	Arabidopsis thaliana	-	only LACS9 resides in the plastid, the site of de novo fatty acid synthesis	9507	716538
cytoplasm	Rattus norvegicus	Q924N5	-	5737	653671
cytosol	Rattus norvegicus	-	ACS1	5829	652139
cytosol	Saccharomyces cerevisiae	P38137, P38225, P39518	-	5829	672419
endoplasmic reticulum	Rattus norvegicus	-	ACS1	5783	652139
endoplasmic reticulum	Rattus norvegicus	-	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	5783	662463
endoplasmic reticulum	Mus musculus	-	-	5783	672182, 674830, 675015
endoplasmic reticulum	Rattus norvegicus	-	-	5783	674710, 738
endoplasmic reticulum	Homo sapiens	-	-	5783	675015, 715715
endoplasmic reticulum	Arabidopsis thaliana	-	isozymne LACS1	5783	716538
glyoxysome	Brassica napus, Ulmus sp., Zea mays	-	-	9514	745
membrane	Rattus norvegicus	-	mitochondria-associated membrane, ACS1, ACS4	16020	652139
membrane	Brassica napus	Q9FNT6	most highly active in light membrane fraction	16020	653493
membrane	Mus musculus	-	-	16020	671234, 671606, 674830
membrane	Homo sapiens	-	-	16020	671234, 671606
membrane	Rattus norvegicus	-	-	16020	671234
membrane	Saccharomyces cerevisiae	P38137, P38225, P39518	-	16020	672419
microbody	Yarrowia lipolytica	-	enzyme form acyl-CoA synthetase II	42579	759
microsome	Rattus norvegicus	-	-	-	649789, 662994, 732, 734, 737, 738, 752, 754, 755, 758, 760, 764, 765
microsome	Homo sapiens	-	-	-	662072, 671606
microsome	Mus musculus	-	-	-	671606
microsome	Yarrowia lipolytica	-	enzyme form acyl-CoA synthetase I	-	759
mitochondrial outer membrane	Pisum sativum	-	-	5741	746
mitochondrion	Rattus norvegicus	-	mitochondrial membrane, ACS5. ACS1 is not detected in mitochondria	5739	652139
mitochondrion	Chaenocephalus aceratus, Notothenia coriiceps	-	-	5739	661519
mitochondrion	Homo sapiens	-	-	5739	662072, 671606, 714313, 715838
mitochondrion	Rattus norvegicus	-	; 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	5739	662463
mitochondrion	Mus musculus	-	-	5739	671606, 674830, 714678
mitochondrion	Rattus norvegicus	-	-	5739	738, 752, 756, 758, 762, 763, 764
mitochondrion	Pichia pastoris	-	-	5739	742
mitochondrion	Pisum sativum	-	-	5739	746
nucleus	Rattus norvegicus	-	-	5634	662994
peroxisome	Luciola cruciata, Photinus pyralis	-	-	5777	658709
peroxisome	Arabidopsis thaliana	-	-	5777	663057, 693420
peroxisome	Saccharomyces cerevisiae	P38137, P38225, P39518	; ;	5777	672419
peroxisome	Mus musculus	O88561	-	5777	674830
peroxisome	Emericella nidulans	-	FaaB	5777	713991
peroxisome	Rattus norvegicus	-	-	5777	738, 752
peroxisome	Rattus norvegicus	-	cytoplasmic side of the peroxisomal membrane	5777	757
plasma membrane	Escherichia coli	-	fatty acyl-CoA synthetase facilitates long chain fatty acid permeation of the inner membrane by a vectorial thioesterification	5886	662226
plasma membrane	Rattus norvegicus	-	-	5886	662994
plasma membrane	Homo sapiens	-	isozyme ACSL6	5886	714605
vesicle	Homo sapiens	O95573	-	31982	674910
mitochondrion	Yarrowia lipolytica	-	enzyme form acyl-CoA synthetase I	5739	759
additional information	Rattus norvegicus	-	not localized in mitochondrion or plasma membrane	-	674710
additional information	Homo sapiens	Q6P1M0	not found at the plasma membrane	-	675015
additional information	Mus musculus	Q91VE0	not found at the plasma membrane	-	675015
additional information	Arabidopsis thaliana	-	subcellular localization study	-	693420
additional information	Arabidopsis thaliana	-	subcellular localization of isozymes, overview	-	716538

PDB	SCOP	CATH	ORGANISM
3ivr, download	SCOP (3ivr)	CATH (3ivr)	Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
1ult, download	SCOP (1ult)	CATH (1ult)	Thermus thermophilus
1v25, download	SCOP (1v25)	CATH (1v25)	Thermus thermophilus

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
45000	47000	Escherichia coli	-	gel filtration	753
50000	-	Escherichia coli	-	sedimentation equilibrium ultracentrifugation	753
52500	-	Drosophila melanogaster	-	SDS-PAGE	672684
64000	-	Mus musculus	Q924N5	SDS-PAGE, only in the ovary	675688
64000	-	Rattus norvegicus	-	SDS-PAGE, only in the brain	675688
72000	-	Homo sapiens	Q9UKU0	predicted molecular mass	672807
75000	-	Homo sapiens	-	SDS-PAGE	673484
77870	-	Saccharomyces cerevisiae	P38137, P38225, P39518	calculated from amino acid sequence	672419
78000	-	Babesia bovis	Q6QLU3	SDS-PAGE	675867
79000	-	Mus musculus	Q924N5	SDS-PAGE	675688
79000	-	Rattus norvegicus	-	SDS-PAGE	675688
80000	-	Rattus norvegicus	-	SDS-PAGE	675554
130000	-	Escherichia coli	-	gel filtration, gradient PAGE	761
145000	-	Saccharomyces cerevisiae	-	gel filtration	672418
250000	-	Rattus norvegicus	-	aggregates quite readily to form species with MW of over 1 million, gel filtration	763

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Oryctolagus cuniculus	-	x * 81516, calculation from nucleotide sequence	650399
?	Brassica napus	Q9FNT6	x * 76000, calculation from nucleotide sequence	653493
?	Rattus norvegicus	-	x * 78177, liver enzyme, caculation from nucleotide sequence	733
?	Escherichia coli	-	x * 62028, calculation from nucleotide sequence	743
?	Escherichia coli	-	x * 42000, SDS-PAGE	751
?	Rattus norvegicus	-	x * 76000, SDS-PAGE	758, 764
?	Yarrowia lipolytica	-	x * 84000, SDS-PAGE, enzyme form acyl-CoA synthetase I	759
?	Rattus norvegicus	-	SDS-PAGE results in 4 protein components with MW 135000, 115000, 65000 and 55000	763
dimer	Homo sapiens	Q9UKU0	SDS-PAGE; SDS-PAGE	672807
dimer	Escherichia coli	-	2 * or 3 * 47000, SDS-PAGE	761
trimer	Escherichia coli	-	3 * or 2 * 47000, SDS-PAGE	761
homodimer	Saccharomyces cerevisiae	-	2 * 72500, gel filtration	672418
additional information	Mus musculus	-	fatty acid transport protein FATP1 and ACSL1 participate in an oligomeric complex in 3T3-L1 adipocytes. The interaction between ACSL1 and FATP1 is constitutive	662593
additional information	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	FadDs contain ATP/AMP signature and FA-binding motifs; FadDs contain ATP/AMP signature and FA-binding motifs	716680

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	Escherichia coli	-	enzyme does not contain carbohydrate, phospholipid and fatty acid	751

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	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	Thermus thermophilus	-	662243

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
4	-	Escherichia coli	-	complete inactivation within 24 h	761
35	-	Rattus norvegicus	-	2.5 min: 17-20% loss of activity, 5 min: 33-37% loss of activity, 15 min: 58-59% loss of activity	764
37	-	Rattus norvegicus	-	half-life is 26.5 min	755
43	-	Rattus norvegicus	-	half-life: about 10 min for ACS1, shorter thah 1 min fpr ACS4 and about 4 min for ACS5	652138
43	-	Rattus norvegicus	P33124	half-life of isoenzyme ACSL6_v1 is 5 min; half-life of isoenzyme ACSL6_v2 is 5 min	661181
45	-	Plasmodium knowlesi	-	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	747
45	-	Rattus norvegicus	-	half-life: 3.3 min	755
45	-	Rattus norvegicus	-	half-life: 15 min	765
46	-	Escherichia coli	-	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	751
additional information	-	Homo sapiens	-	heat inactivation does not distinguish between arachidonoyl-CoA synthetase, EC 6.2.1.15, and palmitoyl-CoA synthetase	637

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
100 mM potassium phosphate stabilizes at 4�C	Escherichia coli	-	753
ATP, stabilizes at 4EC	Escherichia coli	-	753
36% loss of activity after freezing and thawing	Rattus norvegicus	-	755
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	Rattus norvegicus	-	758

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-70�C, indefinitely stable	Escherichia coli	-	761
4�C, 10 mM potassium phosphate, 12 h, 70% loss of activity. 100 mM potassium phosphate or ATP stabilizes	Escherichia coli	-	753
-70�C, stable for at least 4 months	Rattus norvegicus	-	758, 764
-70�C, stable for at least 1 month	Yarrowia lipolytica	-	759

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
partial, recombinant enzyme	Brassica napus	Q9FNT6	653493
-	Drosophila melanogaster	-	697221
Ni-chelate affinity column chromatography	Drosophila melanogaster	-	672684
-	Escherichia coli	-	652285, 662226, 753, 761
partial	Homo sapiens	-	638
-	Mus musculus	-	662341
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography	Mycobacterium tuberculosis	-	691308
partial	Oryctolagus cuniculus	-	650399
recombinant His-tagged AcsA by nickel affinity chromatography	Pseudomonas chlororaphis	Q5CD72	693035
-	Rattus norvegicus	-	649789, 652138, 758, 763, 764
ACS3, one of multiple forms of enzyme in brain	Rattus norvegicus	Q63151	740
M2-anti-FLAG agarose column chromatography	Rattus norvegicus	-	672417
Ni-NTA resin column chromatography and Sephacryl S-200 HR gel filtration	Saccharomyces cerevisiae	-	672418
-	Trypanosoma brucei	-	649717, 662797
-	Yarrowia lipolytica	-	759

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
expression in Escherichia coli	Brassica napus	Q9FNT6	653493
gene acs-3, expression as GFP-tagged protein in worm embryos	Caenorhabditis elegans	-	714677
dACS1, genotyping	Drosophila melanogaster	-	714799
expressed in Escherichia coli	Drosophila melanogaster	-	672684
expression in Escherichia coli	Drosophila melanogaster	-	697221
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	Emericella nidulans	-	713991
-	Escherichia coli	-	652285, 743
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	Homo sapiens	-	714605
expressed in COS-7 cells	Homo sapiens	Q5FVE4	671606
expressed in Escherichia coli	Homo sapiens	Q9UKU0	672807
FACL3, quantitative real-time quantitative PCR expression analysis	Homo sapiens	-	716813
gene acs-3, quantitative reverse transcription PCR expression analysis	Homo sapiens	-	715715
-	Mus musculus	-	649559
expressed in COS cells	Mus musculus	Q924N5	675688
expressed in COS-7 cells	Mus musculus	-	671606
expression in COS1 cells	Mus musculus	-	662341
menE, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)	Mycobacterium tuberculosis	-	691308
-	Oryctolagus cuniculus	-	650399
DNA and amino acid sequence determination and analysis, phylogenetic analysis, overview	Photinus pyralis	P08659	694271
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	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	716680
gene acsA, expression of His-tagged enzyme	Pseudomonas chlororaphis	Q5CD72	693035
-	Rattus norvegicus	-	672417
ACS3, one of multiple forms of enzyme in brain, expression in COS cells	Rattus norvegicus	Q63151	740
ACSl5, quantitative real-time PCR expression analysis	Rattus norvegicus	O88813	715835
ectopical overexpression of ACSL5 in rat hepatoma McArdle-RH7777 cells	Rattus norvegicus	-	662463
expressed in COS cells	Rattus norvegicus	-	675688
expressed in rat primary hepatocytes	Rattus norvegicus	-	674710
expression in Cos-1 cells	Rattus norvegicus	Q924N5	653671
expression of ACS-Flag fusion proteins in Escherichia coli	Rattus norvegicus	-	652138
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	Rattus norvegicus	P33124	662225
expression of isoenzyme ACSL6_v1 in Escherichia coli; expression of isoenzyme ACSL6_v2 in Escherichia coli	Rattus norvegicus	P33124	661181
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; 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	Rattus norvegicus	Q63151	662185
liver enzyme	Rattus norvegicus	-	733
overexpression in PC12 cells	Rattus norvegicus	-	662330
expressed in Escherichia coli	Saccharomyces cerevisiae	-	672418
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	Thalassiosira pseudonana	-	663142
DNA and amino acid sequence determination and analysis, phylogenetic analysis, luciferase-like paralogues are located in close proximity on a chromosome, overview	Tribolium castaneum	-	694271
expression in Escherichia coli	Trypanosoma brucei	-	649717

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
FaaB but not FaaA is induced in the presence of both sort-chain fatty acids and long-chain fatty acids	Emericella nidulans	-	713991
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	Homo sapiens	-	715715
lipid-induced up-regulation of acyl-CoA synthetase 5 promotes hepatocellular apoptosis. ACSL5 expression is enhanced in steatotic liver	Homo sapiens	-	714313
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	Homo sapiens	-	715715
FACL3 is upregulated by 1alpha, 25(OH)2D3 at an mRNA and enzyme activity levels in prostate cancer cells, overview	Homo sapiens	-	716813
functional expression in yeast Saccharomyces cerevisiae results in the accumulation of 18-, 19-, and 20-carbon monounsaturated fatty acids and eicosanoic acid. The transformant efficiently elongates exogenous 9-hexadecenoic acid, 9,12-octadecadienoic acid, and 9,12,15-octadecatrienoic acid	Mortierella alpina	C8KHM6	701851

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
C343S	Agrypnus binodulus	-	no luminescence enhancement	697221
C343S/G344T	Agrypnus binodulus	-	no luminescence enhancement	697221
C343S/G344T/L345S	Agrypnus binodulus	-	increase of luminescence activity to 100%	697221
C343S/L345S	Agrypnus binodulus	-	increase of luminescence activity	697221
G344T	Agrypnus binodulus	-	no luminescence enhancement	697221
G344T/L345S	Agrypnus binodulus	-	increase of luminescence activity to 27%	697221
L216R	Agrypnus binodulus	-	no luminescence enhancement	697221
Q419R	Drosophila melanogaster	-	naturally occuring mutant of dAcs1	714799
E361A	Escherichia coli	-	inactive mutant enzyme	652285
G216A	Escherichia coli	-	the ratio of turnover number to Km-value for the reaction with oleate is 32.7% of the wild-type ratio	652285
G219A	Escherichia coli	-	the ratio of turnover number to Km-value for the reaction with oleate is 1.3fold higher than the wild-type ratio	652285
K222A	Escherichia coli	-	the ratio of turnover number to Km-value for the reaction with oleate is 8% of the wild-type ratio	652285
N431A	Escherichia coli	-	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	739
T214A	Escherichia coli	-	the ratio of turnover number to Km-value for the reaction with oleate is 10.3% of the wild-type ratio	652285
T217A	Escherichia coli	-	the ratio of turnover number to Km-value for the reaction with oleate is 6.7% of the wild-type ratio	652285
Y213A	Escherichia coli	-	inactive mutant enzyme	652285
F319A	Homo sapiens	-	site-directed mutagenesis	714605
F319W	Homo sapiens	-	site-directed mutagenesis	714605
F319Y	Homo sapiens	-	site-directed mutagenesis	714605
H316L	Homo sapiens	-	site-directed mutagenesis	714605
Y319A	Homo sapiens	-	site-directed mutagenesis	714605
G401L	Rattus norvegicus	-	inactive enzyme	672417
Q525K	Rattus norvegicus	-	reduced activity	672417
S291Y	Rattus norvegicus	-	mutant prefers 20:5 and 22:6 substrates and has an increased Km for ATP	672417
L345S	Agrypnus binodulus	-	enhancement of luminescence	697221
additional information	Arabidopsis thaliana	-	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	693420
K294E	Drosophila melanogaster	-	naturally occuring mutant of dAcs1, K294E is located in the AMP-binding domain	714799
additional information	Drosophila melanogaster	-	chimeric protein with firefly luciferase, EC 1.13.12.7, 4% of luminescence activity from Photinus pyralis luciferase activity	697221
W685stop	Drosophila melanogaster	-	naturally occuring mutant of dAcs1, W685stop removes the last 33 amino acids	714799
additional information	Emericella nidulans	-	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	713991
L316H	Homo sapiens	-	site-directed mutagenesis	714605
additional information	Homo sapiens	-	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	714313
additional information	Homo sapiens	-	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	714605
additional information	Homo sapiens	-	overexpression of ACSL1 results in a less marked increase in arachidonoyl-CoA synthesis	715838
Y319F	Homo sapiens	-	site-directed mutagenesis	714605
additional information	Mus musculus	-	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	714678
additional information	Pseudomonas aeruginosa	Q9HYU3, Q9HYU4	construction of fadD1 mutants, phenotype, overview; construction of fadD1 mutants, phenotype, overview	716680
L399M	Rattus norvegicus	-	no significant alteration of activity compared to the wild type enzyme	672417
additional information	Rattus norvegicus	O88813	siRNA knockdown of ACSL5 in rat primary hepatocytes	715835

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

DISEASE	TITLE OF PUBLICATION	LINK TO PUBMED
Acidosis	Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions.	PubMed
Adenocarcinoma	Fatty acid CoA ligase 4 is up-regulated in colon adenocarcinoma.	PubMed
Adenocarcinoma	Impaired expression of acyl-CoA synthetase 5 in sporadic colorectal adenocarcinomas.	PubMed
Adrenoleukodystrophy	A mouse model for X-linked adrenoleukodystrophy.	PubMed
Adrenoleukodystrophy	Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme A synthetase with the peroxisome.	PubMed
Adrenoleukodystrophy	cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA synthetase.	PubMed
Adrenoleukodystrophy	Disruption of the Saccharomyces cerevisiae FAT1 gene decreases very long-chain fatty acyl-CoA synthetase activity and elevates intracellular very long-chain fatty acid concentrations.	PubMed
Adrenoleukodystrophy	Expression of an acyl-CoA synthetase, lipidosin, in astrocytes of the murine brain and its up-regulation during remyelination following cuprizone-induced demyelination.	PubMed
Adrenoleukodystrophy	Molecular organization of peroxisomal enzymes: protein-protein interactions in the membrane and in the matrix.	PubMed
Adrenoleukodystrophy	Mouse very long-chain acyl-CoA synthetase in X-linked adrenoleukodystrophy.	PubMed
Adrenoleukodystrophy	Peroxisomal activation of long- and very long-chain fatty acids in the yeast Pichia pastoris.	PubMed
Adrenoleukodystrophy	Peroxisomal fatty acid beta-oxidation in relation to the accumulation of very long chain fatty acids in cultured skin fibroblasts from patients with Zellweger syndrome and other peroxisomal disorders.	PubMed
Adrenoleukodystrophy	Prenatal diagnosis of Zellweger syndrome by measurement of very long chain fatty acid (C26:0) beta-oxidation in cultured chorionic villous fibroblasts: implications for early diagnosis of other peroxisomal disorders.	PubMed
Adrenoleukodystrophy	The red-green visual pigment gene region in adrenoleukodystrophy.	PubMed
Adrenoleukodystrophy	X-linked adrenoleukodystrophy: identification of the primary defect at the level of a deficient peroxisomal very long chain fatty acyl-CoA synthetase using a newly developed method for the isolation of peroxisomes from skin fibroblasts.	PubMed
Adrenoleukodystrophy	X-linked adrenoleukodystrophy: role of very long-chain acyl-CoA synthetases.	PubMed
Adrenoleukodystrophy	[Examination of very long chain fatty acids in diagnosis of x-linked adrenoleukodystrophy]	PubMed
Asthma	Relation of DNA methylation of 5'-CpG island of ACSL3 to transplacental exposure to airborne polycyclic aromatic hydrocarbons and childhood asthma.	PubMed
Atherosclerosis	Diabetes promotes an inflammatory macrophage phenotype and atherosclerosis through acyl-CoA synthetase 1.	PubMed
Breast Neoplasms	Expression of Long-chain Fatty Acyl-CoA Synthetase 4 in Breast and Prostate Cancers Is Associated with Sex Steroid Hormone Receptor Negativity.	PubMed
Breast Neoplasms	Functional interaction between acyl-CoA synthetase 4, lipooxygenases and cyclooxygenase-2 in the aggressive phenotype of breast cancer cells.	PubMed
Carcinoma, Endometrioid	Expression of acyl-CoA synthetase 5 in human endometrium and in endometrioid adenocarcinomas.	PubMed
Carcinoma, Hepatocellular	Activation of AMP-kinase by Policosanol Requires Peroxisomal Metabolism.	PubMed
Carcinoma, Hepatocellular	Biosynthesis of glycerolipids by hepatoma and liver microsomes. I. Fatty acyl-CoA ligase and acyl-CoA:sn-glycerol-3-phosphate acyltransferase.	PubMed
Carcinoma, Hepatocellular	Expression of putative fatty acid transporter genes are regulated by peroxisome proliferator-activated receptor alpha and gamma activators in a tissue- and inducer-specific manner.	PubMed
Carcinoma, Hepatocellular	Fatty acid-CoA ligase 4 is overexpressed in human hepatocellular carcinoma.	PubMed
Carcinoma, Hepatocellular	Functional interaction between acyl-CoA synthetase 4, lipooxygenases and cyclooxygenase-2 in the aggressive phenotype of breast cancer cells.	PubMed
Carcinoma, Hepatocellular	Involvement of fatty acid-CoA ligase 4 in hepatocellular carcinoma growth: roles of cyclic AMP and p38 mitogen-activated protein kinase.	PubMed
Carcinoma, Hepatocellular	Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells.	PubMed
Carcinoma, Hepatocellular	New actions of melatonin on tumor metabolism and growth.	PubMed
Carcinoma, Hepatocellular	Overexpression of acyl-CoA synthetase-1 increases lipid deposition in hepatic (HepG2) cells and rodent liver in vivo.	PubMed
Carcinoma, Hepatocellular	Overexpression of CD36 and acyl-CoA synthetases FATP2, FATP4 and ACSL1 increases fatty acid uptake in human hepatoma cells.	PubMed
Carcinoma, Hepatocellular	Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglycerol in McArdle-RH7777 cells.	PubMed
Carcinoma, Hepatocellular	Regulation of cell growth by fatty acid-CoA ligase 4 in human hepatocellular carcinoma cells.	PubMed
Carcinoma, Hepatocellular	The functional interaction between Acyl-CoA synthetase 4, 5-lipooxygenase and cyclooxygenase-2 controls tumor growth: a novel therapeutic target.	PubMed
Cardiomegaly	Metabolic activation and major protein target of a 1-benzyl-3-carboxyazetidine sphingosine-1-phosphate-1 receptor agonist.	PubMed
Cardiomegaly	Mouse cardiac acyl coenzyme a synthetase 1 deficiency impairs Fatty Acid oxidation and induces cardiac hypertrophy.	PubMed
Cardiomyopathies	A novel mouse model of lipotoxic cardiomyopathy.	PubMed
Cardiomyopathies	DGAT1 expression increases heart triglyceride content but ameliorates lipotoxicity.	PubMed
Cardiomyopathies	Transgenic expression of fatty acid transport protein 1 in the heart causes lipotoxic cardiomyopathy.	PubMed
Cell Transformation, Neoplastic	Involvement of fatty acid-CoA ligase 4 in hepatocellular carcinoma growth: roles of cyclic AMP and p38 mitogen-activated protein kinase.	PubMed
Colitis, Ulcerative	Alterations in intestinal fatty acid metabolism in inflammatory bowel disease.	PubMed
Colonic Neoplasms	Involvement of fatty acid-CoA ligase 4 in hepatocellular carcinoma growth: roles of cyclic AMP and p38 mitogen-activated protein kinase.	PubMed
Crohn Disease	Expression of acyl-CoA synthetase 5 reflects the state of villus architecture in human small intestine.	PubMed
Dehydration	Epidermal hyperproliferation in mice lacking fatty acid transport protein 4 (FATP4) involves ectopic EGF receptor and STAT3 signaling.	PubMed
Dehydration	Keratinocyte-specific expression of fatty acid transport protein 4 rescues the wrinkle-free phenotype in Slc27a4/Fatp4 mutant mice.	PubMed
Demyelinating Diseases	Expression of an acyl-CoA synthetase, lipidosin, in astrocytes of the murine brain and its up-regulation during remyelination following cuprizone-induced demyelination.	PubMed
Dyslipidemias	Increased hepatic CD36 expression contributes to dyslipidemia associated with diet-induced obesity.	PubMed
Erythema	Association of a long-chain fatty acid-CoA ligase 4 gene polymorphism with depression and with enhanced niacin-induced dermal erythema.	PubMed
Fatty Liver	ApoB siRNA-induced Liver Steatosis is Resistant to Clearance by the Loss of Fatty Acid Transport Protein 5 (Fatp5).	PubMed
Fatty Liver	Osthole improves fat milk-induced fatty liver in rats: modulation of hepatic PPAR-alpha/gamma-mediated lipogenic gene expression.	PubMed
Fatty Liver	Silencing of hepatic fatty acid transporter protein 5 in vivo reverses diet-induced non-alcoholic fatty liver disease and improves hyperglycemia.	PubMed
Fatty Liver	[The expression and the significance of L-FABP and FATP4 in the development of nonalcoholic fatty liver disease in rats]	PubMed
Glioma	Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide.	PubMed
Glioma	Acyl-CoA synthetase VL3 knockdown inhibits human glioma cell proliferation and tumorigenicity.	PubMed
Glioma	Fatty acid induced glioma cell growth is mediated by the acyl-CoA synthetase 5 gene located on chromosome 10q25.1-q25.2, a region frequently deleted in malignant gliomas.	PubMed
Glioma	Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions.	PubMed
Hyperthyroidism	Effects of experimental hypo- and hyperthyroidism on hepatic long-chain fatty acyl-CoA synthetase and hydrolase.	PubMed
Hypertriglyceridemia	Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation.	PubMed
Hypertrophy, Left Ventricular	A variant in the heart-specific fatty acid transport protein 6 is associated with lower fasting and postprandial TAG, blood pressure and left ventricular hypertrophy.	PubMed
Ichthyosis	Epidermal hyperproliferation in mice lacking fatty acid transport protein 4 (FATP4) involves ectopic EGF receptor and STAT3 signaling.	PubMed
Ichthyosis	FATP4 missense and nonsense mutations cause similar features in Ichthyosis Prematurity Syndrome.	PubMed
Ichthyosis	Ichthyosis prematurity syndrome caused by a novel fatty acid transport protein 4 gene mutation in a German infant.	PubMed
Ichthyosis	Mutations in the fatty acid transport protein 4 gene cause the ichthyosis prematurity syndrome.	PubMed
Ichthyosis	Role of fatty acid transporters in epidermis: Implications for health and disease.	PubMed
Infection	Enzymatic properties of purified murine fatty acid transport protein 4 and analysis of acyl-CoA synthetase activities in tissues from FATP4 null mice.	PubMed
Infection	Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells.	PubMed
Infection	Reduction of serum free fatty acids and triglycerides by liver-targeted expression of long chain acyl-CoA synthetase 3.	PubMed
Infertility	Activity of Long-Chain Acyl-CoA Synthetase Is Required for Maintaining Meiotic Arrest in Xenopus laevis.	PubMed
Insulin Resistance	A null mutation in skeletal muscle FAT/CD36 reveals its essential role in insulin- and AICAR-stimulated fatty acid metabolism.	PubMed
Insulin Resistance	Expression of fatty-acid-handling proteins in human adipose tissue in relation to obesity and insulin resistance.	PubMed
Insulin Resistance	Fatty acid handling protein expression in adipose tissue, fatty acid composition of adipose tissue and serum, and markers of insulin resistance.	PubMed
Insulin Resistance	Fatty acid transport proteins and insulin resistance.	PubMed
Insulin Resistance	Fatty acid transport proteins.	PubMed
Insulin Resistance	Functional analysis of long-chain acyl-coa synthetase 1 in 3T3-L1 adipocytes.	PubMed
Insulin Resistance	Genetic and structural evaluation of fatty acid transport protein-4 in relation to markers of the insulin resistance syndrome.	PubMed
Insulin Resistance	Inactivation of fatty acid transport protein 1 prevents fat-induced insulin resistance in skeletal muscle.	PubMed
Insulin Resistance	Increasing skeletal muscle fatty acid transport protein 1 (FATP1) targets fatty acids to oxidation and does not predispose mice to diet-induced insulin resistance.	PubMed
Intellectual Disability	A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients.	PubMed
Intellectual Disability	FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation.	PubMed
Intellectual Disability	Localization of a non-syndromic X-linked mental retardation gene (MRX80) to Xq22-q24.	PubMed
Intellectual Disability	No association between polymorphisms in the FACL4 (fatty acid-CoA ligase 4) gene and nonspecific mental retardation in Qin-Ba mountain region of China.	PubMed
Leishmaniasis	Bioinformatic Analysis of Leishmania donovani Long-Chain Fatty Acid-CoA Ligase as a Novel Drug Target.	PubMed
Leukemia, Lymphoid	Eight genes are highly associated with BMD variation in postmenopausal Caucasian women.	PubMed
Liver Diseases	Silencing of hepatic fatty acid transporter protein 5 in vivo reverses diet-induced non-alcoholic fatty liver disease and improves hyperglycemia.	PubMed
Liver Diseases	[The expression and the significance of L-FABP and FATP4 in the development of nonalcoholic fatty liver disease in rats]	PubMed
Liver Neoplasms	The effect of fatty acid-CoA ligase 4 on the growth of hepatic cancer cells.	PubMed
Liver Neoplasms, Experimental	Biosynthesis of glycerolipids by hepatoma and liver microsomes. I. Fatty acyl-CoA ligase and acyl-CoA:sn-glycerol-3-phosphate acyltransferase.	PubMed
long-chain-fatty-acid-coa ligase deficiency	Abnormal uterus with polycysts, accumulation of uterine prostaglandins, and reduced fertility in mice heterozygous for acyl-CoA synthetase 4 deficiency.	PubMed
long-chain-fatty-acid-coa ligase deficiency	Adipocyte-specific inactivation of the acyl-CoA-synthetase fatty acid transport protein 4 (Fatp4) in mice causes adipose hypertrophy and alterations in metabolism of complex lipids under high-fat diet.	PubMed
long-chain-fatty-acid-coa ligase deficiency	Disturbed epidermal structure in mice with temporally controlled fatp4 deficiency.	PubMed
long-chain-fatty-acid-coa ligase deficiency	Fatty acid transport protein 4 is the principal very long chain fatty acyl-CoA synthetase in skin fibroblasts.	PubMed
long-chain-fatty-acid-coa ligase deficiency	Mutations in the fatty acid transport protein 4 gene cause the ichthyosis prematurity syndrome.	PubMed
Lupus Erythematosus, Systemic	High ACSL5 transcript levels associate with systemic lupus erythematosus and apoptosis in Jurkat T lymphocytes and peripheral blood cells.	PubMed
Mental Retardation, X-Linked	A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients.	PubMed
Mental Retardation, X-Linked	FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation.	PubMed
Neoplasms	Biosynthesis of glycerolipids by hepatoma and liver microsomes. I. Fatty acyl-CoA ligase and acyl-CoA:sn-glycerol-3-phosphate acyltransferase.	PubMed
Neoplasms	Expression and vitamin D(3) regulation of long-chain fatty-acid-CoA ligase 3 in human prostate cancer cells.	PubMed
Neoplasms	Lack of association between certain candidate gene polymorphisms and the metabolic syndrome.	PubMed
Neoplasms	Persistent activity modification of phosphatidate phosphohydrolase and fatty acyl-CoA synthetase on incubation of adipocytes with the tumour promoter 12-O-tetradecanoylphorbol 13-acetate.	PubMed
Neoplasms	Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions.	PubMed
Neoplasms	The functional interaction between Acyl-CoA synthetase 4, 5-lipooxygenase and cyclooxygenase-2 controls tumor growth: a novel therapeutic target.	PubMed
Nephritis, Hereditary	FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation.	PubMed
Neuroblastoma	RNA interference of long-chain acyl-CoA synthetase 6 suppresses the neurite outgrowth of mouse neuroblastoma NB41A3 cells.	PubMed
Obesity	Acute effects of epigallocatechin gallate from green tea on oxidation and tissue incorporation of dietary lipids in mice fed a high-fat diet.	PubMed
Obesity	Cloning of wrinkle-free, a previously uncharacterized mouse mutation, reveals crucial roles for fatty acid transport protein 4 in skin and hair development.	PubMed
Obesity	Expression of fatty-acid-handling proteins in human adipose tissue in relation to obesity and insulin resistance.	PubMed
Obesity	Fatty acid transport proteins and insulin resistance.	PubMed
Obesity	Increased rates of fatty acid uptake and plasmalemmal fatty acid transporters in obese Zucker rats.	PubMed
Obesity	Liver fatty acid-binding protein gene-ablated female mice exhibit increased age-dependent obesity.	PubMed
Obesity	Long chain acyl CoA synthetase 1 and gelsolin are oppositely regulated in adipogenesis and lipogenesis.	PubMed
Obesity	Mice deleted for Fatty Acid transport protein 5 have defective bile Acid conjugation and are protected from obesity.	PubMed
Obesity, Abdominal	Fatty acid handling protein expression in adipose tissue, fatty acid composition of adipose tissue and serum, and markers of insulin resistance.	PubMed
Peroxisomal Disorders	A mouse model for X-linked adrenoleukodystrophy.	PubMed
Peroxisomal Disorders	cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA synthetase.	PubMed
Photosensitivity Disorders	Photodynamic effects of antioxidant substituted porphyrin photosensitizers on gram-positive and -negative bacterial.	PubMed
Primary Ovarian Insufficiency	Activity of Long-Chain Acyl-CoA Synthetase Is Required for Maintaining Meiotic Arrest in Xenopus laevis.	PubMed
Prostatic Neoplasms	Expression and vitamin D(3) regulation of long-chain fatty-acid-CoA ligase 3 in human prostate cancer cells.	PubMed
Prostatic Neoplasms	Expression of Long-chain Fatty Acyl-CoA Synthetase 4 in Breast and Prostate Cancers Is Associated with Sex Steroid Hormone Receptor Negativity.	PubMed
Prostatic Neoplasms	The role of long-chain fatty-acid-CoA ligase 3 in vitamin D3 and androgen control of prostate cancer LNCaP cell growth.	PubMed
Prostatic Neoplasms	Vitamin D3 inhibits fatty acid synthase expression by stimulating the expression of long-chain fatty-acid-CoA ligase 3 in prostate cancer cells.	PubMed
Skin Abnormalities	Keratinocyte-specific expression of fatty acid transport protein 4 rescues the wrinkle-free phenotype in Slc27a4/Fatp4 mutant mice.	PubMed
Starvation	Effect of starvation on hepatic acyl-CoA synthetase, carnitine palmitoyltransferase-I, and acetyl-CoA carboxylase mRNA levels in rats.	PubMed
Starvation	Fatty acid uptake in Escherichia coli: regulation by recruitment of fatty acyl-CoA synthetase to the plasma membrane.	PubMed
Starvation	Mevalonate governs interdependency of ergosterol and siderophore biosyntheses in the fungal pathogen Aspergillus fumigatus.	PubMed
Starvation	Triacylglycerol synthesis in the oleaginous yeast Candida curvata D.	PubMed
Thymoma	Characterization of an arachidonic acid-selective acyl-CoA synthetase from murine T lymphocytes.	PubMed
Tuberculosis	Attenuation of Mycobacterium tuberculosis functionally disrupted in a fatty acyl-coenzyme A synthetase gene fadD5.	PubMed
Tuberculosis	Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis.	PubMed
Tuberculosis	The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase: structural basis for housing lipid substrates longer than the enzyme.	PubMed
Vascular Diseases	Diabetes promotes an inflammatory macrophage phenotype and atherosclerosis through acyl-CoA synthetase 1.	PubMed
Vesicular Stomatitis	The Lyn kinase C-lobe mediates Golgi export of Lyn through conformation-dependent ACSL3 association.	PubMed

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
634	Hartman, E.J.; Omura, S.; Laposata, M.	Triacsin C: a differential inhibitor of arachidonoyl-CoA synthetase and nonspecific long chain acyl-CoA synthetase	Prostaglandins	37	655-671	1989	Mus musculus	PubMed
636	Gerritsen, M.E.; Perry, C.A.	Regulation of eicosanoid synthesis in microvessel endothelium: glucocorticoids do not affect arachidonyl CoA synthetase activity	Biochim. Biophys. Acta	1045	174-179	1990	Oryctolagus cuniculus	PubMed
637	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	PubMed
638	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	PubMed
732	Coleman, R.A.; Rao, P.; Fogelsong, R.J.; Bardes, E.S.G.	2-Bromopalmitoyl-CoA and 2-bromopalmitate: promiscuous inhibitors of membrane-bound enzymes	Biochim. Biophys. Acta	1125	203-209	1992	Rattus norvegicus	PubMed
733	Suzuki, H.; Kawarabayashi, Y.; Kondo, J.; Abe, T.; Hishikawa, K.; Kimura, S.; Hashimoto, T.; Yamamoto, T.	Structure and regulation of rat long-chain acyl-CoA synthetase	J. Biol. Chem.	265	8681-8685	1990	Rattus norvegicus	PubMed
734	Hurtado del Catalfo, G.E.; De Gomez Dumm, I.N.T.; Mandon, E.C.	Long chain acyl-CoA synthetase of rat testis microsomes. Substrate specificity and hormonal regulation	Biochem. Mol. Biol. Int.	31	643-649	1993	Rattus norvegicus	PubMed
736	Vanden Heuvel, J.P.; Kuslikis, B.I.; Shrago, E.; Peterson, R.E.	Inhibition of long-chain acyl-CoA synthetase by the peroxisome proliferator perfluorodecanoic acid in rat hepatocytes	Biochem. Pharmacol.	42	295-302	1991	Rattus norvegicus	PubMed
737	Knights, K.M.; Jones, M.E.	Inhibition kinetics of hepatic microsomal long chain fatty acid-CoA ligase by 2-arylpropionic acid non-steroidal anti-inflammatory drugs	Biochem. Pharmacol.	43	1465-1471	1992	Rattus norvegicus	PubMed
738	Wanders, R.J.A.; Denis, S.; Roermund, C.W.T.; Jakobs, C.; ten Brink, H.J.	Characteristics and subcellular localization of pristanoyl-CoA synthetase in rat liver	Biochim. Biophys. Acta	1125	274-279	1992	Rattus norvegicus	PubMed
739	Black, P.N.; Zhang, Q.; Weimar, J.D.; DiRusso, C.C.	Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity	J. Biol. Chem.	272	4896-4903	1997	Escherichia coli	PubMed
740	Fujino, T.; Kang, M.J.; Suzuki, H.; Iijima, H.; Yamamoto, T.	Molecular characterization and expression of rat acyl-CoA synthetase 3	J. Biol. Chem.	271	16748-16752	1996	Rattus norvegicus	PubMed
741	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	PubMed
742	Kalish, J.E.; Chen, C.I.; Gould, S.J.; Watkins, P.A.	Peroxisomal activation of long- and very long-chain fatty acids in the yeast Pichia pastoris	Biochem. Biophys. Res. Commun.	206	335-340	1995	Pichia pastoris	PubMed
743	Black, P.N.; DiRusso, C.C.; Metzger, A.K.; Heimert, T.L.	Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase	J. Biol. Chem.	267	25513-25520	1992	Escherichia coli	PubMed
744	Duronio, R.J.; Knoll, L.J.; Gordon, J.I.	Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation	J. Cell Biol.	117	515-529	1992	Saccharomyces cerevisiae	PubMed
745	Olsen, J.A.; Huang, A.H.C.	Glyoxysomal acyl-CoA synthetase and oxidase from germinating elm, rape and maize seed	Phytochemistry	27	1601-1603	1988	Brassica napus, Ulmus sp., Zea mays	-
746	Thomas, D.R.; Wood, C.; Masterson, C.	Long-chain acyl CoA synthetase, carnitine and beta-oxidation in the pea-seed mitochondrion	Planta	173	263-266	1988	Pisum sativum	-
747	Beaumelle, B.D.; Vial, H.J.	Acyl-CoA synthetase activity in Plasmodium knowlesi-infected erythrocytes displays peculiar substrate specificities	Biochim. Biophys. Acta	958	1-9	1988	Plasmodium knowlesi	PubMed
748	Tomoda, H.; Igarashi, K.; Omura, S.	Inhibition of acyl-CoA synthetase by triacsins	Biochim. Biophys. Acta	921	595-598	1987	Pseudomonas aeruginosa, Rattus norvegicus	PubMed
749	Haq, R.U.; Tsao, F.; Shrago, E.	Activity of long chain acyl-CoA synthetase in isolated alveolar type II cells	Biochim. Biophys. Acta	918	36-39	1987	Rattus norvegicus	PubMed
750	Morisaki, N.; Kanzaki, T.; Saito, Y.; Yoshida, S.	Fatty acid specificity of acyl-CoA synthetase in rat glomeruli	Biochim. Biophys. Acta	875	311-315	1986	Rattus norvegicus	PubMed
751	Kameda, K.; Imai, Y.	Isolation and characterization of the multiple charge isoforms of acyl-CoA synthetase from Escherichia coli	Biochim. Biophys. Acta	832	343-350	1985	Escherichia coli	PubMed
752	Miyazawa, S.; Hashimoto, T.; Yokota, S.	Identity of long-chain acyl-coenzyme A synthetase of microsomes, mitochondria, and peroxisomes in rat liver	J. Biochem.	98	723-733	1985	Rattus norvegicus	PubMed
753	Kameda, K.; Suzuki, L.K.; Imai, Y.	Further purification, characterization and salt activation of acyl-CoA synthetase from Escherichia coli	Biochim. Biophys. Acta	840	29-36	1985	Escherichia coli	PubMed
754	Noy, N.; Zakim, D.	Substrate specificity of fatty-acyl-CoA ligase in liver microsomes	Biochim. Biophys. Acta	833	239-244	1985	Rattus norvegicus	PubMed
755	Reddy, T.S.; Sprecher, H.; Bazan, N.G.	Long-chain acyl-coenzyme A synthetase from rat liver brain microsomes. Kinetic studies using [1-14C]docosahexaenoic acid substrate	Eur. J. Biochem.	145	21-29	1984	Rattus norvegicus	PubMed
756	Normann, P.T.; Norseth, J.; Flatmark, T.	Acyl-CoA synthetase activity of rat heart mitochondria. Substrate specificity with special reference to very-long-chain and isomeric fatty acids	Biochim. Biophys. Acta	752	474-481	1983	Rattus norvegicus	PubMed
757	Mannaerts, G.P.; Van Veldhoven, P.; Van Broekhoven, A.; Vanderbroek, C.; Debeer, L.J.	Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane	Biochem. J.	204	17-23	1982	Rattus norvegicus	PubMed
758	Tanaka, T.; Hosaka, K.; Numa, S.	Long-chain acyl-CoA synthetase from rat liver	Methods Enzymol.	71	334-341	1981	Rattus norvegicus	PubMed
759	Hosaka, K.; Mishina, M.; Kamiryo, T.; Numa, S.	Long-chain acyl-CoA synthetase I and II from Candida lipolytica	Methods Enzymol.	71	325-333	1981	Yarrowia lipolytica	-
760	Normann, P.T.; Thomassen, M.S.; Christiansen, E.N.; Flatmark, T.	Acyl-CoA synthetase activity of rat liver microsomes. Substrate specificity with special reference to very-long-chain and isomeric fatty acids	Biochim. Biophys. Acta	664	416-427	1981	Rattus norvegicus	PubMed
761	Kameda, K.; Nunn, W.D.	Purification and characterization of acyl coenzyme A synthetase from Escherichi coli	J. Biol. Chem.	256	5702-5707	1981	Escherichia coli	PubMed
762	Philipp, D.P.; Parsons, P.	Kinetic characterization of long chain fatty acyl coenzyme A ligase from rat liver mitochondria	J. Biol. Chem.	254	10785-10790	1979	Rattus norvegicus	-
763	Philipp, D.P.; Parsons, P.	Isolation and purification of long chain fatty acyl coenzyme A ligase from rat liver mitochondria	J. Biol. Chem.	254	10776-10784	1979	Rattus norvegicus	PubMed
764	Tanaka, T.; Hosaka, M.; Hoshimaru, M.; Numa, S.	Purification and properties of long-chain acyl-coenzyme -A synthetase from rat liver	Eur. J. Biochem.	98	165-172	1979	Rattus norvegicus	PubMed
765	Marcel, Y.L.; Suzue, G.	Kinetic studies on the specificity of long chain acyl coenzyme A synthetase from rat liver microsomes	J. Biol. Chem.	247	4433-4436	1972	Rattus norvegicus	PubMed
649559	Moriya-Sato, A.; Hida, A.; Inagawa-Ogashiwa, M.; Wada, M.R.; Sugiyama, K.; Shimizu, J.; Yabuki, T.; Seyama, Y.; Hashimoto, N.	Novel acyl-CoA synthetase in adrenoleukodystrophy target tissues	Biochem. Biophys. Res. Commun.	279	62-68	2000	Mus musculus	PubMed
649717	Jiang, D.W.; Englund, P.T.	Four Trypanosoma brucei fatty acyl-CoA synthetases: fatty acid specificity of the recombinant proteins	Biochem. J.	358	757-761	2001	Trypanosoma brucei	PubMed
649789	Brugger, R.; Reichel, C.; Garcia Alia, B.; Brune, K.; Yamamoto, T.; Tegeder, I.; Geissinger, G.	Expression of rat liver long-chain acyl-CoA synthetase and characterization of its role in the metabolism of R-ibuprofen and other fatty acid-like xenobiotics	Biochem. Pharmacol.	61	651-656	2001	Rattus norvegicus	PubMed
650399	Uberti, M.A.; Pierce, J.; Weis, M.T.	Molecular characterization of a rabbit long-chain fatty acyl CoA synthetase that is highly expressed in the vascular endothelium	Biochim. Biophys. Acta	1645	193-204	2003	Oryctolagus cuniculus	PubMed
652138	Kim, J.H.; Lewin, T.M.; Coleman, R.A.	Expression and characterization of recombinant rat acyl-CoA synthetases 1, 4, and 5: selective inhibition by triacsin C and thiazolidinediones	J. Biol. Chem.	276	24667-24673	2001	Rattus norvegicus	PubMed
652139	Lewin, T.M.; Kim, J.H.; Granger, D.A.; Vance, J.E.; Coleman, R.A.	Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently	J. Biol. Chem.	276	24674-24679	2001	Rattus norvegicus	PubMed
652285	Weimar, J.D.; DiRusso, C.C.; Delio, R.; Black, P.N.	Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids: Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport	J. Biol. Chem.	277	29369-29376	2002	Escherichia coli	PubMed
653493	Pongdontri, P.; Hills, M.	Characterization of a novel plant acyl-coA synthetase that is expressed in lipogenic tissues of Brassica napus L	Plant Mol. Biol.	47	717-726	2001	Brassica napus	PubMed
653671	Tang, P.Z.; Tsai-Morris, C.H.; Dufau, M.L.	Cloning and characterization of a hormonally regulated rat long chain acyl-CoA synthetase	Proc. Natl. Acad. Sci. USA	98	6581-6586	2001	Rattus norvegicus	PubMed
658314	Oba, Y.; Sato, M.; Ojika, M.; Inouye, S.	Enzymatic and genetic characterization of firefly luciferase and Drosophila CG6178 as a fatty acyl-CoA synthetase	Biosci. Biotechnol. Biochem.	69	819-828	2005	Luciola cruciata, Photinus pyralis	PubMed
658709	Oba, Y.; Ojika, M.; Inouye, S.	Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase	FEBS Lett.	540	251-254	2003	Luciola cruciata, Photinus pyralis	PubMed
660874	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	PubMed
661181	Van Horn, C.G.; Caviglia, J.M.; Li, L.O.; Wang, S.; Granger, D.A.; Coleman, R.A.	Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6	Biochemistry	44	1635-1642	2005	Rattus norvegicus	PubMed
661284	Achouri, Y.; Hegarty, B.D.; Allanic, D.; Becard, D.; Hainault, I.; Ferre, P.; Foufelle, F.	Long chain fatty acyl-CoA synthetase 5 expression is induced by insulin and glucose: involvement of sterol regulatory element-binding protein-1c	Biochimie	87	1149-1155	2005	Rattus norvegicus	PubMed
661519	Grove, T.J.; Sidell, B.D.	Fatty acyl CoA synthetase from Antarctic notothenioid fishes may influence substrate specificity of fat oxidation	Comp. Biochem. Physiol. B	139	53-63	2004	Chaenocephalus aceratus, Notothenia coriiceps	PubMed
661822	Sheng, Y.; Li, J.; Dufau, M.L.; Tsai-Morris, C.H.	The gonadotropin-regulated long-chain acyl CoA synthetase gene: a novel downstream Sp1/Sp3 binding element critical for transcriptional promoter activity	Gene	360	20-26	2005	Mus musculus	PubMed
662072	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	PubMed
662185	Caviglia, J.M.; Li, L.O.; Wang, S.; DiRusso, C.C.; Coleman, R.A.; Lewin, T.M.	Rat long chain acyl-CoA synthetase 5, but not 1, 2, 3, or 4, complements Escherichia coli fadD	J. Biol. Chem.	279	11163-11169	2004	Rattus norvegicus	PubMed
662225	Marszalek, J.R.; Kitidis, C.; Dararutana, A.; Lodish, H.F.	Acyl-CoA synthetase 2 overexpression enhances fatty acid internalization and neurite outgrowth	J. Biol. Chem.	279	23882-23891	2004	Rattus norvegicus	PubMed
662226	Schmelter, T.; Trigatti, B.L.; Gerber, G.E.; Mangroo, D.	Biochemical demonstration of the involvement of fatty acyl-CoA synthetase in fatty acid translocation across the plasma membrane	J. Biol. Chem.	279	24163-24170	2004	Escherichia coli	PubMed
662243	Hisanaga, Y.; Ago, H.; Nakagawa, N.; Hamada, K.; Ida, K.; Yamamoto, M.; Hori, T.; Arii, Y.; Sugahara, M.; Kuramitsu, S.; Yokoyama, S.; Miyano, M.	Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer	J. Biol. Chem.	279	31717-31726	2004	Thermus thermophilus	PubMed
662330	Marszalek, J.R.; Kitidis, C.; Dirusso, C.C.; Lodish, H.F.	Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism	J. Biol. Chem.	280	10817-10826	2005	Rattus norvegicus	PubMed
662341	Hall, A.M.; Wiczer, B.M.; Herrmann, T.; Stremmel, W.; Bernlohr, D.A.	Enzymatic properties of purified murine fatty acid transport protein 4 and analysis of acyl-CoA synthetase activities in tissues from FATP4 null mice	J. Biol. Chem.	280	11948-11954	2005	Mus musculus	PubMed
662463	Mashek, D.G.; McKenzie, M.A.; Van Horn, C.G.; Coleman, R.A.	Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglcyerol in McArdle-RH7777 cells	J. Biol. Chem.	281	945-950	2005	Rattus norvegicus	PubMed
662593	Richards, M.R.; Harp, J.D.; Ory, D.S.; Schaffer, J.E.	Fatty acid transport protein 1 and long chain acyl CoA synthetase 1 interact in adipocytes	J. Lipid Res.	47	665-672	2005	Mus musculus	PubMed
662797	Jiang, D.W.; Werbovetz, K.A.; Varadhachary, A.; Cole, R.N.; Englund, P.T.	Purification and identification of a fatty acyl-CoA synthetase from Trypanosoma brucei	Mol. Biochem. Parasitol.	135	149-152	2004	Trypanosoma brucei	PubMed
662994	Wang, Y.L.; Guo, W.; Zang, Y.; Yaney, G.C.; Vallega, G.; Getty-Kaushik, L.; Pilch, P.; Kandror, K.; Corkey, B.E.	Acyl coenzyme a synthetase regulation: putative role in long-chain acyl coenzyme a partitioning	Obes. Res.	12	1781-1788	2004	Rattus norvegicus	PubMed
663057	Fulda, M.; Schnurr, J.; Abbadi, A.; Heinz, E.; Browse, J.	Peroxisomal Acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana	Plant Cell	16	394-405	2004	Arabidopsis thaliana	PubMed
663058	Schnurr, J.; Shockey, J.; Browse, J.	The acyl-CoA synthetase encoded by LACS2 is essential for normal cuticle development in Arabidopsis	Plant Cell	16	629-642	2004	Arabidopsis thaliana	PubMed
663142	Tonon, T.; Qing, R.; Harvey, D.; Li, Y.; Larson, T.R.; Graham, I.A.	Identification of a long-chain polyunsaturated fatty acid acyl-coenzyme A synthetase from the diatom Thalassiosira pseudonana	Plant Physiol.	138	402-408	2005	Thalassiosira pseudonana	PubMed
671234	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, Mus musculus, Rattus norvegicus	PubMed
671244	Durgan, D.J.; Smith, J.K.; Hotze, M.A.; Egbejimi, O.; Cuthbert, K.D.; Zaha, V.G.; Dyck, J.R.; Abel, E.D.; Young, M.E.	Distinct transcriptional regulation of long-chain acyl-CoA synthetase isoforms and cytosolic thioesterase 1 in the rodent heart by fatty acids and insulin	Am. J. Physiol. Heart Circ. Physiol.	290	H2480-H2497	2006	Mus musculus, Rattus norvegicus	PubMed
671335	Mercade, A.; Estelle, J.; Perez-Enciso, M.; Varona, L.; Silio, L.; Noguera, J.L.; Sanchez, A.; Folch, J.M.	Characterization of the porcine acyl-CoA synthetase long-chain 4 gene and its association with growth and meat quality traits	Anim. Genet.	37	219-224	2006	Sus scrofa	PubMed
671606	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, Mus musculus	PubMed
672182	Golovko, M.Y.; Rosenberger, T.A.; Faergeman, N.J.; Feddersen, S.; Cole, N.B.; Pribill, I.; Berger, J.; Nussbaum, R.L.; Murphy, E.J.	Acyl-CoA synthetase activity links wild-type but not mutant alpha-synuclein to brain arachidonate metabolism	Biochemistry	45	6956-6966	2006	Mus musculus	PubMed
672417	Stinnett, L.; Lewin, T.M.; Coleman, R.A.	Mutagenesis of rat acyl-CoA synthetase 4 indicates amino acids that contribute to fatty acid binding	Biochim. Biophys. Acta	1771	119-125	2007	Rattus norvegicus	PubMed
672418	Li, H.; Melton, E.M.; Quackenbush, S.; DiRusso, C.C.; Black, P.N.	Mechanistic studies of the long chain acyl-CoA synthetase Faa1p from Saccharomyces cerevisiae	Biochim. Biophys. Acta	1771	1246-1253	2007	Saccharomyces cerevisiae	PubMed
672419	Black, P.N.; DiRusso, C.C.	Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation	Biochim. Biophys. Acta	1771	286-298	2007	Rattus norvegicus, Saccharomyces cerevisiae	PubMed
672421	De Jong, H.; Neal, A.C.; Coleman, R.A.; Lewin, T.M.	Ontogeny of mRNA expression and activity of long-chain acyl-CoA synthetase (ACSL) isoforms in Mus musculus heart	Biochim. Biophys. Acta	1771	75-82	2007	Mus musculus	PubMed
672490	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	PubMed
672684	Oba, Y.; Tanaka, K.; Inouye, S.	Catalytic properties of domain-exchanged chimeric proteins between firefly luciferase and Drosophila fatty acyl-CoA synthetase CG6178	Biosci. Biotechnol. Biochem.	70	2739-2744	2006	Drosophila melanogaster	PubMed
672807	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	PubMed
673484	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	PubMed
674710	Li, L.O.; Mashek, D.G.; An, J.; Doughman, S.D.; Newgard, C.B.; Coleman, R.A.	Overexpression of rat long chain acyl-coa synthetase 1 alters fatty acid metabolism in rat primary hepatocytes	J. Biol. Chem.	281	37246-37255	2006	Rattus norvegicus	PubMed
674830	Jia, Z.; Moulson, C.L.; Pei, Z.; Miner, J.H.; Watkins, P.A.	Fatty acid transport protein 4 is the principal very long chain fatty acyl-CoA synthetase in skin fibroblasts	J. Biol. Chem.	282	20573-20583	2007	Mus musculus	PubMed
674910	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	PubMed
675015	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, Mus musculus	PubMed
675267	Mashek, D.G.; Li, L.O.; Coleman, R.A.	Rat long-chain acyl-CoA synthetase mRNA, protein, and activity vary in tissue distribution and in response to diet	J. Lipid Res.	47	2004-2010	2006	Rattus norvegicus	PubMed
675554	Song, S.Y.; Kato, C.; Adachi, E.; Moriya-Sato, A.; Inagawa-Ogashiwa, M.; Umeda, R.; Hashimoto, N.	Expression of an acyl-CoA synthetase, lipidosin, in astrocytes of the murine brain and its up-regulation during remyelination following cuprizone-induced demyelination	J. Neurosci. Res.	85	3586-3597	2007	Rattus norvegicus	PubMed
675688	Li, J.; Sheng, Y.; Tang, P.Z.; Tsai-Morris, C.H.; Dufau, M.L.	Tissue-cell- and species-specific expression of gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain. Identification of novel forms in the brain	J. Steroid Biochem. Mol. Biol.	98	207-217	2006	Mus musculus, Rattus norvegicus	PubMed
675690	Cano, F.; Poderoso, C.; Cornejo Maciel, F.; Castilla, R.; Maloberti, P.; Castillo, F.; Neuman, I.; Paz, C.; Podesta, E.J.	Protein tyrosine phosphatases regulate arachidonic acid release, StAR induction and steroidogenesis acting on a hormone-dependent arachidonic acid-preferring acyl-CoA synthetase	J. Steroid Biochem. Mol. Biol.	99	197-202	2006	Mus musculus	PubMed
675867	Norimine, J.; Ruef, B.J.; Palmer, G.H.; Knowles, D.P.; Herndon, D.R.; Rice-Ficht, A.C.; Brown, W.C.	A novel 78-kDa fatty acyl-CoA synthetase (ACS1) of Babesia bovis stimulates memory CD4+ T lymphocyte responses in B. bovis-immune cattle	Mol. Biochem. Parasitol.	147	20-29	2006	Babesia bovis	PubMed
675872	Bethke, L.L.; Zilversmit, M.; Nielsen, K.; Daily, J.; Volkman, S.K.; Ndiaye, D.; Lozovsky, E.R.; Hartl, D.L.; Wirth, D.F.	Duplication, gene conversion, and genetic diversity in the species-specific acyl-CoA synthetase gene family of Plasmodium falciparum	Mol. Biochem. Parasitol.	150	10-24	2006	Plasmodium falciparum	PubMed
691308	Lu, X.; Zhang, H.; Tonge, P.J.; Tan, D.S.	Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis	Bioorg. Med. Chem. Lett.	18	5963-5966	2008	Mycobacterium tuberculosis	PubMed
692792	Matsuda, D.; Namatame, I.; Ohshiro, T.; Ishibashi, S.; Omura, S.; Tomoda, H.	Anti-atherosclerotic activity of triacsin C, an acyl-CoA synthetase inhibitor	J. Antibiot.	61	318-321	2008	Mus musculus	PubMed
693035	Abe, T.; Hashimoto, Y.; Hosaka, H.; Tomita-Yokotani, K.; Kobayashi, M.	Discovery of amide (peptide) bond synthetic activity in acyl-CoA synthetase	J. Biol. Chem.	283	11312-11321	2008	Pseudomonas chlororaphis	PubMed
693420	Kienow, L.; Schneider, K.; Bartsch, M.; Stuible, H.P.; Weng, H.; Miersch, O.; Wasternack, C.; Kombrink, E.	Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana	J. Exp. Bot.	59	403-419	2008	Arabidopsis thaliana	PubMed
694271	Day, J.C.; Goodall, T.I.; Bailey, M.J.	The evolution of the adenylate-forming protein family in beetles: Multiple luciferase gene paralogues in fireflies and glow-worms	Mol. Phylogenet. Evol.	50	93-101	2008	Photinus pyralis, Tribolium castaneum	PubMed
697221	Inouye, S.	Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions	Cell. Mol. Life Sci.	67	387-404	2010	Agrypnus binodulus, Drosophila melanogaster	PubMed
701851	Sakuradani, E.; Nojiri, M.; Suzuki, H.; Shimizu, S.	Identification of a novel fatty acid elongase with a wide substrate specificity from arachidonic acid-producing fungus Mortierella alpina 1S-4	Appl. Microbiol. Biotechnol.	84	709-716	2009	Mortierella alpina	PubMed
713991	Reiser, K.; Davis, M.A.; Hynes, M.J.	Aspergillus nidulans contains six possible fatty acyl-CoA synthetases with FaaB being the major synthetase for fatty acid degradation	Arch. Microbiol.	192	373-382	2010	Emericella nidulans	PubMed
713994	Zalatan, F.; Black, P.	Characterization of long-chain fatty acid uptake in Caulobacter crescentus	Arch. Microbiol.	193	479-487	2011	Caulobacter vibrioides	PubMed
714313	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	PubMed
714605	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	PubMed
714677	Mullaney, B.C.; Blind, R.D.; Lemieux, G.A.; Perez, C.L.; Elle, I.C.; Faergeman, N.J.; Van Gilst, M.R.; Ingraham, H.A.; Ashrafi, K.	Regulation of C. elegans fat uptake and storage by acyl-CoA synthase-3 is dependent on NR5A family nuclear hormone receptor nhr-25	Cell Metab.	12	398-410	2010	Caenorhabditis elegans	PubMed
714678	Ellis, J.M.; Li, L.O.; Wu, P.C.; Koves, T.R.; Ilkayeva, O.; Stevens, R.D.; Watkins, S.M.; Muoio, D.M.; Coleman, R.A.	Adipose acyl-CoA synthetase-1 directs fatty acids toward beta-oxidation and is required for cold thermogenesis	Cell Metab.	12	53-64	2010	Mus musculus	PubMed
714799	Zhang, Y.; Zhang, Y.; Gao, Y.; Zhao, X.; Wang, Z.	Drosophila long-chain acyl-CoA synthetase acts like a gap gene in embryonic segmentation	Dev. Biol.	353	259-265	2011	Drosophila melanogaster	PubMed
715715	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	PubMed
715835	Bu, S.Y.; Mashek, D.G.	Hepatic long-chain acyl-CoA synthetase 5 mediates fatty acid channeling between anabolic and catabolic pathways	J. Lipid Res.	51	3270-3280	2010	Rattus norvegicus	PubMed
715838	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	PubMed
716538	Zhao, L.; Katavic, V.; Li, F.; Haughn, G.W.; Kunst, L.	Insertional mutant analysis reveals that long-chain acyl-CoA synthetase 1 (LACS1), but not LACS8, functionally overlaps with LACS9 in Arabidopsis seed oil biosynthesis	Plant J.	64	1048-1058	2010	Arabidopsis thaliana	PubMed
716680	Kang, Y.; Zarzycki-Siek, J.; Walton, C.B.; Norris, M.H.; Hoang, T.T.	Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa	PLoS ONE	5	e13557	2010	Pseudomonas aeruginosa	PubMed
716813	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	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 6.2.1.3)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

All organisms
Agrypnus binodulus
Arabidopsis thaliana
Babesia bovis
Brassica napus
Caenorhabditis elegans
Caulobacter vibrioides
Chaenocephalus aceratus
Drosophila melanogaster
Emericella nidulans
Escherichia coli
Homo sapiens
Luciola cruciata
Mortierella alpina
Mortierella alpina 1S-4
Mus musculus
Mycobacterium tuberculosis
Notothenia coriiceps
Oryctolagus cuniculus
Photinus pyralis
Pichia pastoris
Pisum sativum
Plasmodium falciparum
Plasmodium knowlesi
Pseudomonas aeruginosa
Pseudomonas chlororaphis
Pseudomonas chlororaphis B23
Rattus norvegicus
Saccharomyces cerevisiae
Sus scrofa
Thalassiosira pseudonana
Thermus thermophilus
Tribolium castaneum
Trypanosoma brucei
Trypanosoma brucei 427
Ulmus sp.
Yarrowia lipolytica
Zea mays