Identification of PTE2, a human peroxisomal long-chain Acyl-CoA thioesterase

Jacob M. Jones; Stephen J. Gould

doi:10.1006/bbrc.2000.3285

Identification of PTE2, a human peroxisomal long-chain Acyl-CoA thioesterase

Jacob M. Jones, Stephen J. Gould

School of Medicine

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

Computer-based approaches identified PTE2 as a candidate human peroxisomal acyl-CoA thioesterase gene. The PTE2 gene product is highly similar to the rat cytosolic and mitochondrial thioesterases, CTE1 and MTE1, respectively, and terminates in a tripeptide sequence, serine-lysine-valine(COOH), that resembles the consensus sequence for type-1 peroxisomal targeting signals. PTE2 was targeted to peroxisomes and recombinant PTE2 showed intrinsic acyl-CoA thioesterase activity with a pH optimum of 8.5. A comparison of PTE2 and PTE1 thioesterase activities across multiple acyl-CoA substrates indicated that while PTE1 was most active on medium-chain acyl-CoAs, with little activity on long-chain acyl-CoAs, PTE2 displayed high activity on medium- and long-chain acyl-CoAs. The identification of PTE2 therefore offers an explanation for the observed long-chain acyl-CoA thioesterase activity of mammalian peroxisomes. (C) 2000 Academic Press.

Original language	English (US)
Pages (from-to)	233-240
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	275
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.2000.3285
State	Published - Aug 18 2000

Keywords

Coenzyme A
Fatty acid metabolism
Peroxisomes
Thioesterase
α-oxidation
β-oxidation

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Identification of PTE2, a human peroxisomal long-chain Acyl-CoA thioesterase",

abstract = "Computer-based approaches identified PTE2 as a candidate human peroxisomal acyl-CoA thioesterase gene. The PTE2 gene product is highly similar to the rat cytosolic and mitochondrial thioesterases, CTE1 and MTE1, respectively, and terminates in a tripeptide sequence, serine-lysine-valine(COOH), that resembles the consensus sequence for type-1 peroxisomal targeting signals. PTE2 was targeted to peroxisomes and recombinant PTE2 showed intrinsic acyl-CoA thioesterase activity with a pH optimum of 8.5. A comparison of PTE2 and PTE1 thioesterase activities across multiple acyl-CoA substrates indicated that while PTE1 was most active on medium-chain acyl-CoAs, with little activity on long-chain acyl-CoAs, PTE2 displayed high activity on medium- and long-chain acyl-CoAs. The identification of PTE2 therefore offers an explanation for the observed long-chain acyl-CoA thioesterase activity of mammalian peroxisomes. (C) 2000 Academic Press.",

keywords = "Coenzyme A, Fatty acid metabolism, Peroxisomes, Thioesterase, α-oxidation, β-oxidation",

author = "Jones, {Jacob M.} and Gould, {Stephen J.}",

note = "Funding Information: We thank Katherine Sacksteder and Brian Geisbrecht for their helpful comments and James Morrell for his expert technical assistance during the course of these studies. This work was supported by grants from the NIH to S.J.G. (DK45787 and HD10981).",

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doi = "10.1006/bbrc.2000.3285",

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N1 - Funding Information: We thank Katherine Sacksteder and Brian Geisbrecht for their helpful comments and James Morrell for his expert technical assistance during the course of these studies. This work was supported by grants from the NIH to S.J.G. (DK45787 and HD10981).

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Y1 - 2000/8/18

N2 - Computer-based approaches identified PTE2 as a candidate human peroxisomal acyl-CoA thioesterase gene. The PTE2 gene product is highly similar to the rat cytosolic and mitochondrial thioesterases, CTE1 and MTE1, respectively, and terminates in a tripeptide sequence, serine-lysine-valine(COOH), that resembles the consensus sequence for type-1 peroxisomal targeting signals. PTE2 was targeted to peroxisomes and recombinant PTE2 showed intrinsic acyl-CoA thioesterase activity with a pH optimum of 8.5. A comparison of PTE2 and PTE1 thioesterase activities across multiple acyl-CoA substrates indicated that while PTE1 was most active on medium-chain acyl-CoAs, with little activity on long-chain acyl-CoAs, PTE2 displayed high activity on medium- and long-chain acyl-CoAs. The identification of PTE2 therefore offers an explanation for the observed long-chain acyl-CoA thioesterase activity of mammalian peroxisomes. (C) 2000 Academic Press.

AB - Computer-based approaches identified PTE2 as a candidate human peroxisomal acyl-CoA thioesterase gene. The PTE2 gene product is highly similar to the rat cytosolic and mitochondrial thioesterases, CTE1 and MTE1, respectively, and terminates in a tripeptide sequence, serine-lysine-valine(COOH), that resembles the consensus sequence for type-1 peroxisomal targeting signals. PTE2 was targeted to peroxisomes and recombinant PTE2 showed intrinsic acyl-CoA thioesterase activity with a pH optimum of 8.5. A comparison of PTE2 and PTE1 thioesterase activities across multiple acyl-CoA substrates indicated that while PTE1 was most active on medium-chain acyl-CoAs, with little activity on long-chain acyl-CoAs, PTE2 displayed high activity on medium- and long-chain acyl-CoAs. The identification of PTE2 therefore offers an explanation for the observed long-chain acyl-CoA thioesterase activity of mammalian peroxisomes. (C) 2000 Academic Press.

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KW - Fatty acid metabolism

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KW - Thioesterase

KW - α-oxidation

KW - β-oxidation

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Identification of PTE2, a human peroxisomal long-chain Acyl-CoA thioesterase

Abstract

Keywords

ASJC Scopus subject areas

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