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EC Tree
IUBMB Comments The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
The taxonomic range for the selected organisms is: Rattus norvegicus The enzyme appears in selected viruses and cellular organisms
Synonyms
elovl6, elovl5, 3-ketoacyl-coa thiolase, beta-ketothiolase, 3-oxoacyl-coa thiolase, acaa2, 3-ketothiolase, elovl-6, thiolase i, thiolase a,
more
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3-ketoacyl CoA thiolase
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3-ketoacyl coenzyme A thiolase
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3-ketoacyl thiolase
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3-oxoacyl-CoA thiolase
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3-oxoacyl-coenzyme A thiolase
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6-oxoacyl-CoA thiolase
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acetoacetyl-CoA beta-ketothiolase
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acetyl-CoA acyltransferase
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acyltransferase, acetyl coenzyme A
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beta-ketoacyl coenzyme A thiolase
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beta-ketoacyl-CoA thiolase
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beta-ketoadipyl coenzyme A thiolase
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beta-ketoadipyl-CoA thiolase
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beta-ketothiolase
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enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
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ketoacyl-CoA acyltransferase
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ketoacyl-coenzyme A thiolase
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long-chain 3-oxoacyl-CoA thiolase
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oxoacyl-coenzyme A thiolase
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pro-3-ketoacyl-CoA thiolase
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SCP2/3-oxoacyl-CoA thiolase
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3-ketoacyl-CoA thiolase
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3-ketoacyl-CoA thiolase
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acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
ping-pong mechanism
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acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
sterol carrier protein X is a 3-oxoacyl CoA thiolase with intrinsic sterol carrier and lipid transfer activity
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Acyl group transfer
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KEGG
alpha-Linolenic acid metabolism , Benzoate degradation , Biosynthesis of secondary metabolites , Biosynthesis of unsaturated fatty acids , Ethylbenzene degradation , Fatty acid degradation , Fatty acid elongation , Geraniol degradation , Microbial metabolism in diverse environments , Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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acyl-CoA:acetyl-CoA C-acyltransferase
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
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acetyl-CoA + H2O
acetate + CoA
butyryl-CoA + H2O
butanoate + CoA
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acetyl-CoA hydrolase activity
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
CoA + 3-oxodecanoyl-CoA
acetyl-CoA + octanoyl-CoA
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CoA + 3-oxododecanoyl-CoA
acetyl-CoA + decanoyl-CoA
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CoA + 3-oxohexadecanoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
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CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
CoA + 3-oxolauryl-CoA
acetyl-CoA + decanoyl-CoA
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CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
CoA + 3-oxopalmitoyl-CoA
acetyl-CoA + tetradecanoyl-CoA
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CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
dodecanoyl-CoA + H2O
dodecanoate + CoA
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acetyl-CoA hydrolase activity
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hexanoyl-CoA + H2O
hexanoate + CoA
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acetyl-CoA hydrolase activity
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?
palmitoyl-CoA + H2O
palmitate + CoA
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acetyl-CoA hydrolase activity
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propionyl-CoA + H2O
propionate + CoA
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acetyl-CoA hydrolase activity
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?
additional information
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acetyl-CoA + H2O
acetate + CoA
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3-ketoacyl-CoA thiolase activity
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acetyl-CoA + H2O
acetate + CoA
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best acyl-CoA substrate, acetyl-CoA hydrolase activity
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acetyl-CoA + H2O
acetate + CoA
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preferred substrate, 3-ketoacyl-CoA thiolase activity
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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r
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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enzyme catalyses the last step in the beta-oxidation cycle
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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enzyme plays important role in peroxisomal beta-oxidation, in addition the enzyme may facilitate the intraperoxysomal movement of sterols and certain other lipids
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CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
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CoA + 3-oxohexanoyl-CoA
acetyl-CoA + butanoyl-CoA
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highest activity with 3-oxohexanoyl-CoA
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r
CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
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CoA + 3-oxooctanoyl-CoA
acetyl-CoA + hexanoyl-CoA
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CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
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CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
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r
additional information
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additional information
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3-oxoacyl-CoA homologues from acetoacetyl to 3-oxopalmitoyl-CoA
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additional information
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thiolase A and B possess virtually the same substrate specificity
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additional information
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key enzyme involved in fatty acid oxidation
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additional information
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the enzyme is involved in fatty acid beta-oxidation
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additional information
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analysis of the substrate chain length specificity of the enzyme, high preference for acetyl-CoA
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acetyl-CoA + H2O
acetate + CoA
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3-ketoacyl-CoA thiolase activity
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
additional information
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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enzyme catalyses the last step in the beta-oxidation cycle
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CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
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enzyme plays important role in peroxisomal beta-oxidation, in addition the enzyme may facilitate the intraperoxysomal movement of sterols and certain other lipids
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additional information
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key enzyme involved in fatty acid oxidation
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additional information
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the enzyme is involved in fatty acid beta-oxidation
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4-Bromo-2-octenoic acid
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acetoacetyl-CoA
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competitive inhibition of the acetyl-CoA hydrolase activity
acetyl-CoA
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competitive inhibition of the 3-ketoacyl-CoA thiolase activity
Mg2+
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25 mM, 20% inhibition
CoA
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CoA
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at concentrations above 0.025 mM
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additional information
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di-(2-ethylhexyl)phthalate induces the enzyme
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0.01 - 0.079
acetoacetyl-CoA
additional information
additional information
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0.01
acetoacetyl-CoA
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0.0114
acetoacetyl-CoA
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pH 7.4
0.021
acetoacetyl-CoA
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pH 8.2, wild-type enzyme
0.058
acetoacetyl-CoA
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pH 8.2, mutant enzyme H352E
0.065
acetoacetyl-CoA
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pH 8.2, mutant enzyme H352Y
0.07
acetoacetyl-CoA
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pH 8.2, mutant enzyme H352A
0.079
acetoacetyl-CoA
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pH 8.2, mutant enzyme H352K
additional information
additional information
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additional information
additional information
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additional information
additional information
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kinetics
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additional information
additional information
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overview: Km of peroxisomal and mitochondrial enzyme with various substrates
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additional information
additional information
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overview: Km of peroxisomal and mitochondrial enzyme with various substrates
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0.029
3-oxooctanoyl-CoA
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sterol carrier protein X-547
0.0022
acetoacetyl-CoA
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pH 7.4, competitive versus acetyl-CoA hydrolysis
0.24
acetyl-CoA
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pH 7.4, competitive versus 3-ketoacyl-CoA thiolase activity
0.02
CoA
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sterol carrier protein X-547
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0.543
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purified enzyme, acetyl-CoA hydrolase activity
119
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thiolase A, substrate: 3-oxooctanoyl-CoA
123
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thiolase B, substrate: 3-oxooctanoyl-CoA
additional information
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additional information
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additional information
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thiolase A pI: 8.45, thiolase B pI: 8.7
additional information
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higher activity in phosphate than in Tris buffer
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brenda
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SwissProt
brenda
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brenda
male Wistar rats
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brenda
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brenda
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di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
brenda
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brenda
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di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
brenda
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brenda
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di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
brenda
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brenda
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di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
brenda
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brenda
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brenda
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di-(2-ethylhexyl)phthalate-inducible acetyl-CoA hydrolase activity
brenda
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enzyme is synthesized in the cytosol and subsequently imported into the peroxisome
brenda
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brenda
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brenda
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brenda
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thiolase A from normal rat liver peroxisomes and thiolase B from livers of clofibrate-treated rats
brenda
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physiological function
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Elovl-5 knockdown decreases elongation of 16:1,n-7. Elovl-5 over-expression increases synthesis of 18:1,n-7, however, this is dependent on stearoyl-CoA desaturase driven 16:1,n-7 availability
physiological function
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knockdown of Elovl-6 decreases elongation of 16:0 and 16:1,n-7, resulting in accumulation of 16:1,n-7. Elovl-6 over-expression preferentially drives synthesis of 16:0 elongation products 18:0 and 18:1,n-9 but not 18:1,n-7
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THIM_RAT
397
0
41871
Swiss-Prot
Mitochondrion (Reliability: 4 )
SCP2_RAT
547
0
58813
Swiss-Prot
Mitochondrion (Reliability: 5 )
THIKA_RAT
434
0
44839
Swiss-Prot
Mitochondrion (Reliability: 3 )
THIKB_RAT
424
0
43820
Swiss-Prot
Mitochondrion (Reliability: 3 )
ECHB_RAT
475
0
51414
Swiss-Prot
Mitochondrion (Reliability: 2 )
A0A8I6G9S8_RAT
577
0
62311
TrEMBL
Mitochondrion (Reliability: 4 )
A0A0G2KAC1_RAT
542
0
58599
TrEMBL
Mitochondrion (Reliability: 4 )
F1LQ55_RAT
548
0
59112
TrEMBL
Mitochondrion (Reliability: 3 )
ECHA_RAT
763
0
82665
Swiss-Prot
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154000
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mitochondrial enzyme, sedimentation equilibrium
40000
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2 * 40000, peroxisomal enzyme, SDS-PAGE
51000
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
79000
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
85000
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thiolase A and B, gel filtration
89000
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peroxisomal enzyme, sedimentation equilibrium
41000
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2 * 41000, mitochondrial enzyme, SDS-PAGE
41000
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2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure
41000
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mitochondrial enzyme, 4 * 41000
460000
gel filtration
460000
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase, gel filtration
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octamer
alpha4beta4, 4 * 79000 + 4 * 51000, SDS-PAGE
tetramer
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mitochondrial enzyme, 4 * 41000
dimer
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2 * 40000, peroxisomal enzyme, SDS-PAGE
dimer
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2 * 41000, mitochondrial enzyme, SDS-PAGE
dimer
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2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure
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H352A
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3.3fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 1154 times
H352E
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2.7fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 1250 times
H352K
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3.7fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 526 times
H352Y
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3.1fold increase in KM-value for acetoacetyl-CoA compared to wild-type value, Vmax is decreased 429 times
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additional information
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thiolase B exhibits cold-lability: loss of acitvity is more pronounced at 4°C than at 30°C, in the presence of KCl, thiolase A is stable under the same conditions, thiolase A exhibits higher stabiliy than thiolase B at 46°C, lability of the thiolase B might be compensated for by the formation of a more stable multienzyme complex
additional information
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enzyme exhibits reversible cold-lability: loss of acitvity at 4°C in the presence of NaCl, half-maximal inactivation in ice in 4 min
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-80°C, wild-type and mutant enzymes H352E, H352A, H352K and H352Y, stable for at least 3 months
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native enzyme 27.2fold from liver mitochondria preparation by 5 steps of ion exchange and hydrophobic interaction chromatography
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expression in Escherichia coli
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His-tagged wild-type and His352 mutant proteins overexpressed in Escherichia coli
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Seedorf, U.; Brysch, P.; Engel, T.; Schrage, K.; Assmann, G.
Sterol carrier protein x is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity
J. Biol. Chem.
269
21277-21283
1994
Rattus norvegicus
brenda
Miyazawa, S.; Osumi, T.; Hashimoto, T.
The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes
Eur. J. Biochem.
103
589-596
1980
Rattus norvegicus
brenda
Miyazawa, S.; Furuta, S.; Osumi, T.; Hashimoto, T.; Ui, N.
Properties of peroxisomal 3-ketoacyl-CoA thiolase from rat liver
J. Biochem.
90
511-519
1981
Rattus norvegicus
brenda
Uchida, Y.; Izai, K.; Orii, T.; Hashimoto, T.
Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
J. Biol. Chem.
267
1034-1041
1992
Rattus norvegicus, Rattus norvegicus (Q64428)
brenda
Middleton, B.
3-Ketoacyl-CoA thiolase of mammalian tissues
Methods Enzymol.
35 B
128-136
1975
Bos taurus, Ovis aries, Rattus norvegicus, Sus scrofa
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brenda
Li, J.; Schulz, H.
4-Bromo-2-octenoic acid specifically inactivates 3-ketoacyl-CoA thiolase and thereby fatty acid oxidation in rat liver mitochondria
Biochemistry
27
5995-6000
1988
Rattus norvegicus
brenda
Arakawa, H.; Takiguchi, M.; Amaya, Y.; Nagata, S.; Hayashi, H.; Mori, M.
cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme
EMBO J.
6
1361-1366
1987
Rattus norvegicus
brenda
Krahling, J.B.; Tolbert, N.E.
Peroxisomal beta-ketothiolase
Arch. Biochem. Biophys.
209
100-110
1981
Rattus norvegicus
brenda
Antonenkov, V.D.; Van Veldhoven, P.P.; Waelkens, E.; Mannaerts, G.P.
Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver
Biochim. Biophys. Acta
1437
136-141
1999
Rattus norvegicus
brenda
Latruffe, N.; Nicolas-Frances, V.; Dasari, V.K.; Osumi, T.
Studies on regulation of the peroxisomal beta-oxidation at the 3-ketothiolase step: Dissection of the rat liver thiolase B gene promoter
Adv. Exp. Med. Biol.
466
253-259
1999
Rattus norvegicus
brenda
Zeng, J.; Li, D.
Expression and purification of His-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins
Protein Expr. Purif.
35
320-326
2004
Rattus norvegicus
brenda
Yamashita, H.; Itsuki, A.; Kimoto, M.; Hiemori, M.; Tsuji, H.
Acetate generation in rat liver mitochondria: acetyl-CoA hydrolase activity is demonstrated by 3-ketoacyl-CoA thiolase
Biochim. Biophys. Acta
1761
17-23
2006
Rattus norvegicus
brenda
Green, C.D.; Ozguden-Akkoc, C.G.; Wang, Y.; Jump, D.B.; Olson, L.K.
Role of fatty acid elongases in determination of de novo synthesized monounsaturated fatty acid species
J. Lipid Res.
51
1871-1877
2010
Rattus norvegicus
brenda