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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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: ?

Instance reaction 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)

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):
i2: phytanate + ATP + coenzyme A → phytanoyl-CoA + AMP + diphosphate (6.2.1.24)

i3: octanoate + ATP + coenzyme A → octanoyl-CoA + AMP + diphosphate (6.2.1.3)

i4: decanoate + ATP + coenzyme A → decanoyl-CoA + AMP + diphosphate (6.2.1.3)

i5: hexanoate + ATP + coenzyme A → hexanoyl-CoA + AMP + diphosphate (6.2.1.-)

i6: pristanate + ATP + coenzyme A → pristanoyl-CoA + AMP + diphosphate (6.2.1.3)

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 Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: eicosapentaenoate 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 Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: stearate biosynthesis I (animals)


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 Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: stearate biosynthesis I (animals) , 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 Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: stearate biosynthesis I (animals)


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 Enzyme Commission system.

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 <=> arachidonyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

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 Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: γ-linolenate biosynthesis II (animals)

Exons/Introns:


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 18.5 on Wed Nov 26, 2014, BIOCYC14B.