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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 2.3.1.9

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

EC Number: 2.3.1.9

Enzymes and Genes:
β-ketothiolase Inferred from experiment : bktB ( Cupriavidus necator )
β-ketoadipyl CoA thiolase : pcaF ( Pseudomonas putida )
3-ketoacyl-CoA thiolase : KAT2 ( Arabidopsis thaliana col )
peroxisomal 3-ketoacyl-CoA thiolase : ACAA1 ( Homo sapiens )
mitochondrial 3-ketoacyl-CoA thiolase : ACAA2 ( Homo sapiens )
Non-specific lipid-transfer protein : SCP2 ( Homo sapiens )
trifunctional enzyme beta subunit, mitochondrial precursor : HADHB ( Homo sapiens )
3-oxoacyl CoA thiolase : POT1 ( Saccharomyces cerevisiae )
fatty acid oxidation complex, β component : fadA ( Escherichia coli K-12 substr. MG1655 )
Fad I component of anaerobic fatty acid oxidation complex : fadI ( Escherichia coli K-12 substr. MG1655 )

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: acetyl-CoA C-acetyltransferase

Enzyme Commission Synonyms: acetoacetyl-CoA thiolase, β-acetoacetyl coenzyme A thiolase, 2-methylacetoacetyl-CoA thiolase [misleading], 3-oxothiolase, acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA:N-acetyltransferase, thiolase II

Standard Gibbs Free Energy (ΔrG in kcal/mol): 7.0598145 Inferred by computational analysis [Latendresse13]

Citations: [Dekishima11, LYNEN, STERN60]

Gene-Reaction Schematic: ?

Instance reaction of [a 2,3,4-saturated fatty acyl CoA + acetyl-CoA ↔ a 3-oxoacyl-CoA + coenzyme A] (2.3.1.16):
i1: acetyl-CoA + propanoyl-CoA = β-ketovaleryl-CoA + coenzyme A (2.3.1.9)

Relationship Links: BRENDA:EC:2.3.1.9 , ENZYME:EC:2.3.1.9 , IUBMB-ExplorEnz:EC:2.3.1.9

Credits:
Created 12-Aug-2011 by Caspi R , SRI International


References

Dekishima11: Dekishima Y, Lan EI, Shen CR, Cho KM, Liao JC (2011). "Extending Carbon Chain Length of 1-Butanol Pathway for 1-Hexanol Synthesis from Glucose by Engineered Escherichia coli." J Am Chem Soc 133(30);11399-401. PMID: 21707101

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

LYNEN: LYNEN F, OCHOA S "Enzymes of fatty acid metabolism." Biochim Biophys Acta 12(1-2);299-314. PMID: 13115439

STERN60: STERN JR, DRUMMOND GI, COON MJ, DEL CAMPILLO A (1960). "Enzymes of ketone body metabolism. I. Purification of an acetoacetate-synthesizing enzyme from ox liver." J Biol Chem 235;313-7. PMID: 13834445


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 Thu Nov 27, 2014, BIOCYC14A.