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MetaCyc Reaction: 2.3.1.9

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

EC Number: 2.3.1.9

Enzymes and Genes:

Arabidopsis thaliana col: 3-ketoacyl-CoA thiolase: KAT2
Cupriavidus necator: β-ketothiolaseInferred 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 direction shown, i.e. which substrates are on the left and right sides, 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): 7.0598145Inferred by computational analysis [Latendresse, 2013]

Citations: [Dekishima11, Lynen53, Stern60]

Gene-Reaction Schematic

Gene-Reaction Schematic

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

Latendresse, 2013: 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


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 Wed Jan 2, 2002, biocyc12.