Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
twitter

MetaCyc Enzyme: long-chain-fatty-acid--CoA ligase 1

Gene: ACSL1 Accession Number: HS07766 (MetaCyc)

Synonyms: LACS2, LACS1, LACS, ACS1, FACL2, FACL1, fatty-acid-coenzyme A ligase, long-chain 1, long-chain fatty-acid-coenzyme A ligase 1, lignoceroyl-CoA synthase

Species: Homo sapiens

Summary:
There are several long-chain-fatty-acid--CoA ligases, each with its own fatty acid specificity and tissue distribution. ACSL1 is a well-characterized enzyme highly expressed in many tissues that exhibits a relatively broad fatty acid specificity.

ACS3 is a different isozyme that preferentially utilizes myristate, arachidonate, and eicosapentaenoate. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation.

long-chain-fatty-acid--CoA ligase 1 (also known as palmitoyl-CoA ligase), encoded by the ACSL1 gene, is highly expressed in liver, heart, skeletal muscle, kidney and erythroid cells, and to a lesser extent in brain, lung, placenta and pancreas. It was shown to use several substrates, including palmitate, oleate and arachidonate [Malhotra99].

See long-chain-fatty-acid-CoA ligase 1 for the rat enzyme.

Citations: [Ghosh95, Stanczak92]

Gene Citations: [Stanczak92]

Map Position: [186,356,631 <- 186,404,578]

Molecular Weight of Polypeptide: 77.943 kD (from nucleotide sequence), 78.0 kD (experimental) [Malhotra99 ]

Unification Links: ArrayExpress:P33121 , Ensembl:ENSG00000151726 , Entrez-gene:2179 , Entrez-gene:2180 , Entrez-Nucleotide:L09229 , GeneCards:FACL1 , OMIM:152425 , OMIM:152426 , PhosphoSite:P33121 , PhylomeDB:P33121 , Pride:P33121 , Protein Model Portal:P33121 , RefSeq:NM_001995 , RefSeq:NM_021122 , RefSeq:NP_001986 , SMR:P33121 , String:9606.ENSP00000281455 , UCSC Human Genome:NM_001995 , UniGene:406678 , UniProt:P33121

Relationship Links: Entrez-Nucleotide:PART-OF:D10040 , InterPro:IN-FAMILY:IPR000873 , InterPro:IN-FAMILY:IPR020845 , Pfam:IN-FAMILY:PF00501 , Prosite:IN-FAMILY:PS00455

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reactions of [a long-chain fatty acid + ATP + coenzyme A → a long-chain acyl-CoA + AMP + diphosphate] (6.2.1.3):
i1: palmitate + ATP + coenzyme A → palmitoyl-CoA + AMP + diphosphate (6.2.1.3)

i2: stearate + ATP + coenzyme A → stearoyl-CoA + AMP + diphosphate (6.2.1.3)

i3: 18-hydroxyoleate + ATP + coenzyme A → 18-hydroxyoleoyl-CoA + AMP + diphosphate (6.2.1.3)

i4: 16-hydroxypalmitate + ATP + coenzyme A → 16-hydroxypalmitoyl-CoA + AMP + diphosphate (6.2.1.3)

i5: 18-hydroxystearate + ATP + coenzyme A → 18-hydroxystearoyl-CoA + AMP + diphosphate (6.2.1.3)

i6: an ω-hydroxy long-chain fatty acid + ATP + coenzyme A → an ω-hydroxy long-chain fatty acyl-CoA + AMP + diphosphate (6.2.1.-)

Instance reactions of [a 2,3,4-saturated fatty acid + ATP + coenzyme A → a 2,3,4-saturated fatty acyl CoA + AMP + diphosphate] (6.2.1.3):
i7: 7-hydroxylaurate + ATP + coenzyme A → 7-hydroxylauroyl-CoA + AMP + diphosphate (6.2.1.3)

i8: octanoate + ATP + coenzyme A → octanoyl-CoA + AMP + diphosphate (6.2.1.3)

i9: decanoate + ATP + coenzyme A → decanoyl-CoA + AMP + diphosphate (6.2.1.3)

i10: pristanate + ATP + coenzyme A → pristanoyl-CoA + AMP + diphosphate (6.2.1.3)

i11: laurate + ATP + coenzyme A = lauroyl-CoA + AMP + diphosphate (6.2.1.3)

i12: hexanoate + ATP + coenzyme A → hexanoyl-CoA + AMP + diphosphate (6.2.1.-)

i13: phytanate + ATP + coenzyme A → phytanoyl-CoA + AMP + diphosphate (6.2.1.24)

i14: a 3-methyl-branched 2,3,4-saturated fatty acid + ATP + coenzyme A → a 3-methyl-branched 2,3,4-saturated fatty acyl-CoA + AMP + diphosphate (6.2.1.3)

i15: a 2-methyl branched 2,3,4-saturated fatty acid + ATP + coenzyme A → a 2-methyl branched 2,3,4-saturated fatty acyl-CoA + AMP + diphosphate (6.2.1.3)

i16: an odd numbered straight chain 2,3,4-saturated fatty acid + ATP + coenzyme A → an odd numbered straight chain 2,3,4-saturated fatty acyl CoA + AMP + diphosphate (6.2.1.3)

i17: a (2R)-2-hydroxy even numbered straight chain 2,3,4-saturated fatty acid + ATP + coenzyme A → a (R)-2-hydroxy even numbered straight chain 2,3,4-saturated fatty acyl CoA + AMP + diphosphate (6.2.1.-)

GO Terms:

Biological Process: GO:0006631 - fatty acid metabolic process
GO:0007586 - digestion
GO:0008152 - metabolic process
Molecular Function: GO:0000287 - magnesium ion binding
GO:0004467 - long-chain fatty acid-CoA ligase activity
GO:0016874 - ligase activity

Credits:
Created 31-Jul-2008 by Caspi R , SRI International


Enzymatic reaction of: α-linolenate—CoA ligase (long-chain-fatty-acid--CoA ligase 1)

EC Number: 6.2.1.3

ATP + α-linolenate + coenzyme A <=> α-linolenoyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: icosapentaenoate biosynthesis II (metazoa)


Enzymatic reaction of: long-chain-fatty-acid—CoA ligase (long-chain-fatty-acid--CoA ligase 1)

EC Number: 6.2.1.3

a long-chain fatty acid + ATP + coenzyme A <=> a long-chain acyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: stearate biosynthesis I (animals and fungi)


Enzymatic reaction of: fatty acid:CoA ligase (AMP-forming) (long-chain-fatty-acid--CoA ligase 1)

Synonyms: fatty acid:CoA ligase (AMP-forming)

EC Number: 6.2.1.3

a 2,3,4-saturated fatty acid + ATP + coenzyme A <=> a 2,3,4-saturated fatty acyl CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: fatty acid α-oxidation III , fatty acid α-oxidation II , stearate biosynthesis I (animals and fungi) , fatty acid β-oxidation I , fatty acid β-oxidation VI (peroxisome)


Enzymatic reaction of: palmitate:CoA ligase (AMP-forming) (long-chain-fatty-acid--CoA ligase 1)

EC Number: 6.2.1.3

palmitate + ATP + coenzyme A <=> palmitoyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: stearate biosynthesis I (animals and fungi)


Enzymatic reaction of: oleate:CoA ligase (AMP-forming) (long-chain-fatty-acid--CoA ligase 1)

EC Number: 6.2.1.3

oleate + ATP + coenzyme A <=> oleoyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: arachidonate:CoA ligase (AMP-forming) (long-chain-fatty-acid--CoA ligase 1)

EC Number: 6.2.1.15

arachidonate + ATP + coenzyme A <=> arachidonoyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: linoleate:CoA ligase (AMP-forming) (long-chain-fatty-acid--CoA ligase 1)

EC Number: 6.2.1.3

linoleate + ATP + coenzyme A <=> linoleoyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: γ-linolenate biosynthesis II (animals)

Exons/Introns:

Schematic showing introns, exons and/or isoforms of ACSL1


References

Ghosh95: Ghosh B, Barbosa E, Singh I (1995). "Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression." Mol Cell Biochem 151(1);77-81. PMID: 8584017

Malhotra99: Malhotra KT, Malhotra K, Lubin BH, Kuypers FA (1999). "Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors." Biochem J 344 Pt 1;135-43. PMID: 10548543

Stanczak92: Stanczak H, Stanczak JJ, Singh I (1992). "Chromosomal localization of the human gene for palmitoyl-CoA ligase (FACL1)." Cytogenet Cell Genet 59(1);17-9. PMID: 1531127


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Tue Sep 1, 2015, BIOCYC14A.