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MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

Arabidopsis thaliana col:
Escherichia coli K-12 substr. MG1655:
Homo sapiens:
Saccharomyces cerevisiae: medium-chain acyl-CoA synthetaseInferred from experiment: FAA2

In Pathway: fatty acid β-oxidation I, fatty acid β-oxidation II (peroxisome), fatty acid β-oxidation VI (peroxisome), fatty acid β-oxidation (peroxisome, yeast)

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.

Instance reactions:
laurate + ATP + coenzyme A → lauroyl-CoA + AMP + diphosphate (

decanoate + ATP + coenzyme A → decanoyl-CoA + AMP + diphosphate (

octanoate + ATP + coenzyme A → octanoyl-CoA + AMP + diphosphate (

pristanate + ATP + coenzyme A → pristanoyl-CoA + AMP + diphosphate (

stearate + ATP + coenzyme A → stearoyl-CoA + AMP + diphosphate (

palmitate + ATP + coenzyme A → palmitoyl-CoA + AMP + diphosphate (

7-hydroxylaurate + ATP + coenzyme A → 7-hydroxylauroyl-CoA + AMP + diphosphate (

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

phytanate + ATP + coenzyme A → phytanoyl-CoA + AMP + diphosphate (

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 (

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 (

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 (

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.-)

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): -331.11646Inferred 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:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O15840, UniProt:RELATED-TO:O30039, UniProt:RELATED-TO:O51162, UniProt:RELATED-TO:O51539, UniProt:RELATED-TO:O60135, UniProt:RELATED-TO:O81614, UniProt:RELATED-TO:O83181, UniProt:RELATED-TO:P18163, UniProt:RELATED-TO:P30624, UniProt:RELATED-TO:P33121, UniProt:RELATED-TO:P33124, UniProt:RELATED-TO:P39002, UniProt:RELATED-TO:P39518, UniProt:RELATED-TO:P44446, UniProt:RELATED-TO:P47912, UniProt:RELATED-TO:P69451, UniProt:RELATED-TO:P69452, UniProt:RELATED-TO:P73004, UniProt:RELATED-TO:P94547, UniProt:RELATED-TO:Q8JZR0, UniProt:RELATED-TO:Q96338, UniProt:RELATED-TO:Q96537, UniProt:RELATED-TO:Q96538, UniProt:RELATED-TO:Q9CHR0, UniProt:RELATED-TO:Q9JTK0, UniProt:RELATED-TO:Q9JYJ7, UniProt:RELATED-TO:Q9RTR4, UniProt:RELATED-TO:Q9RYK3, UniProt:RELATED-TO:Q9T009, UniProt:RELATED-TO:Q9T0A0, UniProt:RELATED-TO:Q9X7Y5, UniProt:RELATED-TO:Q9X7Z0, UniProt:RELATED-TO:Q9YCF0, UniProt:RELATED-TO:Q9ZBW6, UniProt:RELATED-TO:Q02602, UniProt:RELATED-TO:Q10776


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
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