Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

MetaCyc Reaction: 6.2.1.3

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 6.2.1.3

Enzymes and Genes:

Arabidopsis thaliana col: long-chain acyl-CoA synthetase 9Inferred from experiment: LACS9
Homo sapiens: long-chain-fatty-acid--CoA ligase 1Inferred from experiment: ACSL1
Saccharomyces cerevisiae: medium-chain acyl-CoA synthetase: FAA2

In Pathway: linoleate biosynthesis II (animals), oleate biosynthesis I (plants)

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: long-chain-fatty-acid—CoA ligase

Enzyme Commission Synonyms: acyl-CoA synthetase, fatty acid thiokinase (long chain), acyl-activating enzyme, palmitoyl-CoA synthase, lignoceroyl-CoA synthase, arachidonyl-CoA synthetase, acyl coenzyme A synthetase, acyl-CoA ligase, palmitoyl coenzyme A synthetase, thiokinase, palmitoyl-CoA ligase, acyl-coenzyme A ligase, fatty acid CoA ligase, long-chain fatty acyl coenzyme A synthetase, oleoyl-CoA synthetase, stearoyl-CoA synthetase, long chain fatty acyl-CoA synthetase, long-chain acyl CoA synthetase, fatty acid elongase, LCFA synthetase, pristanoyl-CoA synthetase, ACS3, long-chain acyl-CoA synthetase I, long-chain acyl-CoA synthetase II, fatty acyl-coenzyme A synthetase, long-chain acyl-coenzyme A synthetase, FAA1

Standard Gibbs Free Energy (ΔrG in kcal/mol): -12.711731Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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.

Citations: [Bakken89, Hosaka79, Nagamatsu85, Tanaka79]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:6.2.1.3, ENZYME:EC:6.2.1.3, IUBMB-ExplorEnz:EC:6.2.1.3


References

Bakken89: Bakken AM, Farstad M (1989). "Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets." Biochem J 261(1);71-6. PMID: 2528345

Hosaka79: Hosaka K, Mishina M, Tanaka T, Kamiryo T, Numa S (1979). "Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification, properties and immunochemical studies." Eur J Biochem 93(1);197-203. PMID: 108099

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Nagamatsu85: Nagamatsu K, Soeda S, Mori M, Kishimoto Y (1985). "Lignoceroyl-coenzyme A synthetase from developing rat brain: partial purification, characterization and comparison with palmitoyl-coenzyme A synthetase activity and liver enzyme." Biochim Biophys Acta 836(1);80-8. PMID: 3161545

Tanaka79: Tanaka T, Hosaka K, Hoshimaru M, Numa S (1979). "Purification and properties of long-chain acyl-coenzyme-A synthetase from rat liver." Eur J Biochem 98(1);165-72. PMID: 467438


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 Pathway Tools version 19.5 (software by SRI International) on Thu Feb 11, 2016, biocyc13.