MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

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

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

Taxonomic Range: Fungi , Metazoa , Bacteria , Viridiplantae

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

Citations: [Dekishima11, Lynen53, Stern60]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

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

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

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


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."

Lynen53: Lynen F, Ochoa S (1953). "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

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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 19.0 on Fri Oct 9, 2015, BIOCYC14B.