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Biochemistry

Technological University Dublin

Acyl-CoA thioesterase

Publication Year

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Full-Text Articles in Life Sciences

The Nudix Hydrolase 7 Is An Acyl-Coa Diphosphatase Involved In Regulating Peroxisomal Coenzyme A Homeostasis., Sarah-Jayne Reilly, Veronica Tillander, Rob Ofman, Stefan Alexson, Mary Hunt Jan 2008

The Nudix Hydrolase 7 Is An Acyl-Coa Diphosphatase Involved In Regulating Peroxisomal Coenzyme A Homeostasis., Sarah-Jayne Reilly, Veronica Tillander, Rob Ofman, Stefan Alexson, Mary Hunt

Articles

Coenzyme A (CoASH) is an obligate cofactor for lipids undergoing β-oxidation in peroxisomes. Although the peroxisomal membrane appears to be impermeable to CoASH, peroxisomes contain their own pool of CoASH. It is believed that CoASH enters peroxisomes as acyl-CoAs, but it is not known how this pool is regulated. The mouse nudix hydrolase 7 (NUDT7α) was previously identified in peroxisomes as a CoAdiphosphatase, and therefore suggested to be involved in regulation of peroxisomal CoASH levels. Here we show that mouse NUDT7α mainly acts as an acyl-CoA diphosphatase, with highest activity towards medium chain acyl-CoAs, and much lower activity with CoASH. …


Molecular Cloning And Characterization Of Two Mouse Peroxisome Proliferator-Activated Receptor Alpha (Ppara) Regulated Peroxisomal Acyl-Coa Thioesterases., Maria Westin, Mary Hunt, Stefan Alexson Jan 2004

Molecular Cloning And Characterization Of Two Mouse Peroxisome Proliferator-Activated Receptor Alpha (Ppara) Regulated Peroxisomal Acyl-Coa Thioesterases., Maria Westin, Mary Hunt, Stefan Alexson

Articles

Peroxisomes are organelles that function in the b-oxidation of very-long and long-chain acyl-CoAs, bile acid-CoA intermediates, prostaglandins, leukotrienes, thromboxanes, dicarboxylic fatty acids, pristanic acid and xenobiotic carboxylic acids. The very long- and long-chain acyl-CoAs are mainly chain-shortened and then transported to mitochondria for further metabolism. We have now identified and characterized two peroxisomal acyl- CoA thioesterases, named PTE-Ia and PTE-Ic, which hydrolyze acyl-CoAs to the free fatty acid and coenzyme A. PTE-Ia and PTE-Ic show 82% sequence identity at amino acid level and a putative peroxisomal type 1 targeting signal of –AKL was identified at the carboxy-terminal end of both …