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

被引：21

作者：

Jones, JM ^{[1
]}

Gould, SJ ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 275卷 / 01期

关键词：

peroxisomes; fatty acid metabolism; thioesterase; coenzyme A; beta-oxidation; alpha-oxidation;

D O I：

10.1006/bbrc.2000.3285

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：233 / 240

页数：8

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