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Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase and Organism(s) Clostridium acetobutylicum and UniProt Accession P45359
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2.3.1.9 acetyl-CoA C-acetyltransferaseIUBMB Comments
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
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Word Map
- 2.3.1.9
- ketone
- mevalonate
- hmg-coa
- acetoacetate
-
beta-oxidation
- 3-hydroxy-3-methylglutaryl-coa
- beta-ketothiolase
- 2-methyl-3-hydroxybutyrate
- 3-hydroxybutyrate
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acetoacetyl-coenzyme
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ketoacidotic
-
ketogenesis
-
tiglylglycine
-
aacts
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coa-transferase
- 2-methylacetoacetate
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thiolytic
- 3-oxoacyl-coas
- 3-ketothiolase
- 3-hydroxyacyl-coa
- coash
- 3-hydroxybutyryl-coa
-
lyso-paf
-
ketone-body
- synthesis
- analysis
- biofuel production
The taxonomic range for the selected organisms is: Clostridium acetobutylicum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
acetoacetyl-coa thiolase, acetyl-coa acetyltransferase, erg10, acoat, acetyl-coa c-acetyltransferase, cytosolic acetoacetyl-coa thiolase, 2-methylacetoacetyl-coa thiolase, osat1, acetoacetyl coa thiolase, aact2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-methylacetoacetyl-CoA thiolase
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-
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3-oxothiolase
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-
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acetoacetyl CoA thiolase
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-
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acetoacetyl-CoA thiolase
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acetyl coenzyme A thiolase
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acetyl-CoA acetyltransferase
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acetyl-CoA:N-acetyltransferase
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acetyltransferase, acetyl coenzyme A
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-
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beta-acetoacetyl coenzyme A thiolase
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-
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thiolase II
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
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-
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Acyl group transfer
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-
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thiolytic cleavage
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Benzoate degradation, Biosynthesis of secondary metabolites, Butanoate metabolism, Carbon fixation pathways in prokaryotes, Fatty acid degradation, Glyoxylate and dicarboxylate metabolism, Lysine degradation, Microbial metabolism in diverse environments, Pyruvate metabolism, Terpenoid backbone biosynthesis, Tryptophan metabolism, Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
9027-46-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM phosphate-citrate pH 4.2, 10% (w/v) polyethylene glycol 3350, 200 mM sodium chloride
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V77Q/N153Y/A286K
the mutant, which is not able to form disulfide bonds, exhibits higher activity than the wild type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 mM dithiothreitol, 10% v/v glycerol, N2 atmosphere, 1 month, less than 10% loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and HiTrap Q ion exchange column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
the enzyme catalyses the condensation of two acetyl-coenzyme A molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wiesenborn, D.P.; Rudolph, F.B.; Papoutsakis, E.T.
Thiolase from Clostridium acetobutylicum ATCC 824 and its role in the synthesis of acids and solvents
Appl. Environ. Microbiol.
54
2717-2722
1988
Clostridium acetobutylicum
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