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Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase and Organism(s) Rattus norvegicus

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EC Tree
IUBMB 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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Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-methylacetoacetyl-CoA thiolase
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-
-
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3-oxothiolase
-
-
-
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acetoacetyl CoA thiolase
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-
-
-
acetoacetyl-CoA thiolase
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-
-
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acetyl coenzyme A thiolase
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-
-
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acetyl-CoA acetyltransferase
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-
-
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acetyl-CoA:N-acetyltransferase
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-
-
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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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thiolase II
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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condensation
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-
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thiolytic cleavage
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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 hide
9027-46-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
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natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
acetoacetyl-CoA
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isoenzyme A: above 0.015 mM, isoenzyme B: above 0.01 mM
CoA
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competitive vs. acetoacetyl-CoA in thiolysis
iodoacetamide
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0.005 mM, inactivation half-life: 3 min
Mg2+
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inhibits the rate of acetoacetyl-CoA thiolysis but not the rate of synthesis of acetoacetyl-CoA
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lovostatin
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1.9fold activity increase in rats treated with lovostatin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.08
acetoacetyl-CoA
0.0062 - 0.03
acetyl-CoA
0.008 - 0.022
CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014
acetoacetyl-CoA
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isoenzyme A
0.067
CoA
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-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
Rattus norvegicus
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natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100 - 130
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peroxisomal thiolase, thiolysis
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THIM_RAT
397
0
41871
Swiss-Prot
Mitochondrion (Reliability: 4)
THIL_RAT
424
0
44695
Swiss-Prot
Mitochondrion (Reliability: 1)
THIC_RAT
397
0
41108
Swiss-Prot
other Location (Reliability: 4)
THIKA_RAT
434
0
44839
Swiss-Prot
Mitochondrion (Reliability: 3)
THIKB_RAT
424
0
43820
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
151000
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gel filtration, isoenzyme A and B
160000
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peroxisomal thiolase, gel filtration
170000
-
gel filtration
40000
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4 * 40000, enzyme A and B, SDS-PAGE
42000
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4 * 42000, peroxisomal thiolase, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 forms: A and B
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peroxisomal thiolase, DEAE-cellulose, phosphocellulose column, Blue-Sepharose
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pH 5.5, DEAE-cellulose, calcium phosphate column, celulose phosphate column
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Middleton, B.
The kinetic mechanism and properties of the cytoplasmic acetoacetyl-coenzyme A thiolase from rat liver
Biochem. J.
139
109-121
1974
Rattus norvegicus
Manually annotated by BRENDA team
Schwabe, D.; Huth, W.
Immunochemical aspects, molecular and kinetic properties of multiple forms of acetyl-CoA acetyltransferase from rat liver mitochondria
Biochim. Biophys. Acta
575
112-120
1979
Rattus norvegicus
Manually annotated by BRENDA team
Huth, W.; Dierich, C.; von Oeynhausen, V.; Seubert, W.
Multiple mitochondrial forms of acetoacetyl-CoA thiolase in rat liver: possible regulatory role in ketogenesis
Biochem. Biophys. Res. Commun.
56
1069-1077
1974
Rattus norvegicus
Manually annotated by BRENDA team
Greenspan, M.D.; Yudkovitz, J.B.; Chen, J.S.; Hanf, D.P.; Chang, M.N.; Chiang, P.Y.C.; Chabala, J.C.; Alberts, A.W.
The inhibition of cytoplasmic acetoacetyl-CoA thiolase by a triyne carbonate (L-660, 631)
Biochem. Biophys. Res. Commun.
163
548-553
1989
Rattus norvegicus
Manually annotated by BRENDA team
Honda, A.; Salen, G.; Nguyen, L.B.; Xu, G.; Tint, G.S.; Batta, A.K.; Shefer, S.
Regulation of early cholesterol biosynthesis in rat liver: effects of sterols, bile acids, lovastatin, and BM 15.766 on 3-hydroxy-3-methylglutaryl coenzyme A synthase and acetoacetyl coenzyme A thiolase activities
Hepatology
27
154-159
1998
Rattus norvegicus
Manually annotated by BRENDA team
Antonenkov, V.D.; Croes, K.; Waelkens, E.; Van Veldhoven, P.P.; Mannaerts, G.P.
Identification, purification and characterization of an acetoacetyl-CoA thiolase from rat liver peroxisomes
Eur. J. Biochem.
267
2981-2990
2000
Rattus norvegicus
Manually annotated by BRENDA team