The Identification of a Succinyl-CoA Thioesterase Suggests a Novel Pathway for Succinate Production in Peroxisomes

Dicarboxylic acids are formed by ω-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via β-oxidation in peroxisomes. Both synthesis and degradation of dicarboxylic acids occur mainly in kidney and liver, and the chain-shortened dicarboxylic acids are excreted in the...

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Published inThe Journal of biological chemistry Vol. 280; no. 46; pp. 38125 - 38132
Main Authors Westin, Maria A.K., Hunt, Mary C., Alexson, Stefan E.H.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 18.11.2005
American Society for Biochemistry and Molecular Biology
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Abstract Dicarboxylic acids are formed by ω-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via β-oxidation in peroxisomes. Both synthesis and degradation of dicarboxylic acids occur mainly in kidney and liver, and the chain-shortened dicarboxylic acids are excreted in the urine as the free acids, implying that acyl-CoA thioesterases (ACOTs), which hydrolyze CoA esters to the free acid and CoASH, are needed for the release of the free acids. Recent studies show that peroxisomes contain several acyl-CoA thioesterases with different functions. We have now expressed a peroxisomal acyl-CoA thioesterase with a previously unknown function, ACOT4, which we show is active on dicarboxylyl-CoA esters. We also expressed ACOT8, another peroxisomal acyl-CoA thioesterase that was previously shown to hydrolyze a large variety of CoA esters. Acot4 and Acot8 are both strongly expressed in kidney and liver and are also target genes for the peroxisome proliferator-activated receptor α. Enzyme activity measurements with expressed ACOT4 and ACOT8 show that both enzymes hydrolyze CoA esters of dicarboxylic acids with high activity but with strikingly different specificities. Whereas ACOT4 mainly hydrolyzes succinyl-CoA, ACOT8 preferentially hydrolyzes longer dicarboxylyl-CoA esters (glutaryl-CoA, adipyl-CoA, suberyl-CoA, sebacyl-CoA, and dodecanedioyl-CoA). The identification of a highly specific succinyl-CoA thioesterase in peroxisomes strongly suggests that peroxisomal β-oxidation of dicarboxylic acids leads to formation of succinate, at least under certain conditions, and that ACOT4 and ACOT8 are responsible for the termination of β-oxidation of dicarboxylic acids of medium-chain length with the concomitant release of the corresponding free acids.
AbstractList Dicarboxylic acids are formed by ω-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via β-oxidation in peroxisomes. Both synthesis and degradation of dicarboxylic acids occur mainly in kidney and liver, and the chain-shortened dicarboxylic acids are excreted in the urine as the free acids, implying that acyl-CoA thioesterases (ACOTs), which hydrolyze CoA esters to the free acid and CoASH, are needed for the release of the free acids. Recent studies show that peroxisomes contain several acyl-CoA thioesterases with different functions. We have now expressed a peroxisomal acyl-CoA thioesterase with a previously unknown function, ACOT4, which we show is active on dicarboxylyl-CoA esters. We also expressed ACOT8, another peroxisomal acyl-CoA thioesterase that was previously shown to hydrolyze a large variety of CoA esters. Acot4 and Acot8 are both strongly expressed in kidney and liver and are also target genes for the peroxisome proliferator-activated receptor α. Enzyme activity measurements with expressed ACOT4 and ACOT8 show that both enzymes hydrolyze CoA esters of dicarboxylic acids with high activity but with strikingly different specificities. Whereas ACOT4 mainly hydrolyzes succinyl-CoA, ACOT8 preferentially hydrolyzes longer dicarboxylyl-CoA esters (glutaryl-CoA, adipyl-CoA, suberyl-CoA, sebacyl-CoA, and dodecanedioyl-CoA). The identification of a highly specific succinyl-CoA thioesterase in peroxisomes strongly suggests that peroxisomal β-oxidation of dicarboxylic acids leads to formation of succinate, at least under certain conditions, and that ACOT4 and ACOT8 are responsible for the termination of β-oxidation of dicarboxylic acids of medium-chain length with the concomitant release of the corresponding free acids.
Dicarboxylic acids are formed by omega-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via beta-oxidation in peroxisomes. Both synthesis and degradation of dicarboxylic acids occur mainly in kidney and liver, and the chain-shortened dicarboxylic acids are excreted in the urine as the free acids, implying that acyl-CoA thioesterases (ACOTs), which hydrolyze CoA esters to the free acid and CoASH, are needed for the release of the free acids. Recent studies show that peroxisomes contain several acyl-CoA thioesterases with different functions. We have now expressed a peroxisomal acyl-CoA thioesterase with a previously unknown function, ACOT4, which we show is active on dicarboxylyl-CoA esters. We also expressed ACOT8, another peroxisomal acyl-CoA thioesterase that was previously shown to hydrolyze a large variety of CoA esters. Acot4 and Acot8 are both strongly expressed in kidney and liver and are also target genes for the peroxisome proliferator-activated receptor alpha. Enzyme activity measurements with expressed ACOT4 and ACOT8 show that both enzymes hydrolyze CoA esters of dicarboxylic acids with high activity but with strikingly different specificities. Whereas ACOT4 mainly hydrolyzes succinyl-CoA, ACOT8 preferentially hydrolyzes longer dicarboxylyl-CoA esters (glutaryl-CoA, adipyl-CoA, suberyl-CoA, sebacyl-CoA, and dodecanedioyl-CoA). The identification of a highly specific succinyl-CoA thioesterase in peroxisomes strongly suggests that peroxisomal beta-oxidation of dicarboxylic acids leads to formation of succinate, at least under certain conditions, and that ACOT4 and ACOT8 are responsible for the termination of beta-oxidation of dicarboxylic acids of medium-chain length with the concomitant release of the corresponding free acids.
Dicarboxylic acids are formed by ω-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via β-oxidation in peroxisomes. Both synthesis and degradation of dicarboxylic acids occur mainly in kidney and liver, and the chain-shortened dicarboxylic acids are excreted in the urine as the free acids, implying that acyl-CoA thioesterases (ACOTs), which hydrolyze CoA esters to the free acid and CoASH, are needed for the release of the free acids. Recent studies show that peroxisomes contain several acyl-CoA thioesterases with different functions. We have now expressed a peroxisomal acyl-CoA thioesterase with a previously unknown function, ACOT4, which we show is active on dicarboxylyl-CoA esters. We also expressed ACOT8, another peroxisomal acyl-CoA thioesterase that was previously shown to hydrolyze a large variety of CoA esters. Acot4 and Acot8 are both strongly expressed in kidney and liver and are also target genes for the peroxisome proliferator-activated receptor α. Enzyme activity measurements with expressed ACOT4 and ACOT8 show that both enzymes hydrolyze CoA esters of dicarboxylic acids with high activity but with strikingly different specificities. Whereas ACOT4 mainly hydrolyzes succinyl-CoA, ACOT8 preferentially hydrolyzes longer dicarboxylyl-CoA esters (glutaryl-CoA, adipyl-CoA, suberyl-CoA, sebacyl-CoA, and dodecanedioyl-CoA). The identification of a highly specific succinyl-CoA thioesterase in peroxisomes strongly suggests that peroxisomal β-oxidation of dicarboxylic acids leads to formation of succinate, at least under certain conditions, and that ACOT4 and ACOT8 are responsible for the termination of β-oxidation of dicarboxylic acids of medium-chain length with the concomitant release of the corresponding free acids.
Author Alexson, Stefan E.H.
Westin, Maria A.K.
Hunt, Mary C.
Author_xml – sequence: 1
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  surname: Westin
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  givenname: Stefan E.H.
  surname: Alexson
  fullname: Alexson, Stefan E.H.
  email: stefan.alexson@ki.se
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Snippet Dicarboxylic acids are formed by ω-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via β-oxidation in peroxisomes. Both...
Dicarboxylic acids are formed by ω-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via β-oxidation in peroxisomes. Both...
Dicarboxylic acids are formed by omega-oxidation of fatty acids in the endoplasmic reticulum and degraded as the CoA ester via beta-oxidation in peroxisomes....
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SubjectTerms Animals
Blotting, Western
Cloning, Molecular
Dicarboxylic Acids - chemistry
Dicarboxylic Acids - metabolism
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum - metabolism
Fatty Acids - metabolism
Fibroblasts - metabolism
Gene Expression Regulation
Green Fluorescent Proteins - metabolism
Humans
Hydrolysis
Kidney - metabolism
Kinetics
Liver - metabolism
Male
Medicin och hälsovetenskap
Mice
Mice, Transgenic
Models, Biological
Palmitoyl-CoA Hydrolase - chemistry
Palmitoyl-CoA Hydrolase - physiology
Peroxisomes - metabolism
PPAR alpha - metabolism
Pyrimidines - pharmacology
Recombinant Proteins - chemistry
Reverse Transcriptase Polymerase Chain Reaction
RNA, Messenger - metabolism
Substrate Specificity
Succinic Acid - chemistry
Thiolester Hydrolases - chemistry
Thiolester Hydrolases - metabolism
Thiolester Hydrolases - physiology
Time Factors
Tissue Distribution
Up-Regulation
Title The Identification of a Succinyl-CoA Thioesterase Suggests a Novel Pathway for Succinate Production in Peroxisomes
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