Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 6.2.1.3

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 6.2.1.3

Enzymes and Genes:
acyl-CoA synthetase : FAA2 ( Saccharomyces cerevisiae )
long-chain-fatty-acid--CoA ligase 1 Inferred from experiment : ACSL1 ( Homo sapiens )
acyl-CoA synthetase Inferred from experiment : LACS9 ( Arabidopsis thaliana col )

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

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

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

Mass balance status: Balanced.

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

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

Standard Gibbs Free Energy (ΔrG in kcal/mol): -12.711731 Inferred 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: ?

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)

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 SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, BIOCYC13B.