Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism

• Published in: Progress in lipid research Vol. 47; no. 6; pp. 405 - 421
• Main Authors: Hunt, Mary C., Alexson, Stefan E.H.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.11.2008
• Subjects: Acyl-CoA; Acyl-CoA thioesterases; Acyltransferases; Acyltransferases - physiology; Alpha-oxidation; Animals; Beta-oxidation; Bile Acids and Salts - metabolism; Coenzyme A; Coenzyme A - metabolism; Dicarboxylic Acids - metabolism; Fatty Acid-Binding Proteins - physiology; Fatty Acids - metabolism; Humans; Lipid Metabolism - physiology; Medicin och hälsovetenskap; Mice; Omega-oxidation; Oxidation-Reduction; Peroxisomes; Peroxisomes - metabolism; Thiolester Hydrolases - physiology; Acyltransferases; Peroxisomes; Coenzyme A; Acyl-CoA; Acyl-CoA thioesterases; Alpha-oxidation; Beta-oxidation; Omega-oxidation
• ISSN: 0163-7827; 1873-2194; 1873-2194
• DOI: 10.1016/j.plipres.2008.05.001

Peroxisomes are single membrane bound organelles present in almost all eukaryotic cells, and to date have been shown to contain approximately 60 identified enzymes involved in various metabolic pathways, including the oxidation of a variety of lipids. These lipids include very long-chain fatty acids, methyl branched fatty acids, prostaglandins, bile-acid precursors and xenobiotics that are either β-oxidized or α-oxidized in peroxisomes. The recent identification of several acyl-CoA thioesterases and acyltransferases in peroxisomes has revealed their various functions in acting as auxiliary enzymes in α- and β-oxidation in this organelle. To date, 9 functional acyl-CoA thioesterases and acyltransferases have been identified in mouse and 4 functional acyl-CoA thioesterases and acyltransferases in human, thus these enzymes make up a substantial portion of peroxisomal proteins. This review will therefore focus on new and emerging roles for these enzymes in assisting with the oxidation of various lipids, amidation of lipids for excretion from peroxisomes, and in controlling coenzyme A levels in peroxisomes.