Regulation of peroxisomal lipid metabolism: The role of acyl-CoA and coenzyme A metabolizing enzymes
Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in mammals is the partial degradation of various (di)carboxylic acids via α- and β-oxidation. While only a small number of enzymes catalyze the...
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Published in | Biochimie Vol. 98; pp. 45 - 55 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
France
Elsevier B.V
01.03.2014
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Subjects | |
Online Access | Get full text |
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Summary: | Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in mammals is the partial degradation of various (di)carboxylic acids via α- and β-oxidation. While only a small number of enzymes catalyze the reactions of β-oxidation, numerous auxiliary enzymes have been identified to be involved in uptake of fatty acids and cofactors required for β-oxidation, regulation of β-oxidation and transport of metabolites across the membrane. These proteins include membrane transporters/channels, acyl-CoA thioesterases, acyl-CoA:amino acid N-acyltransferases, carnitine acyltransferases and nudix hydrolases. Here we review the current view of the role of these auxiliary enzymes in peroxisomal lipid metabolism and propose that they function in concert to provide a means to regulate fatty acid metabolism and transport of products across the peroxisomal membrane.
•ACOTs, NUDTs and N-acyltransferases regulate peroxisomal coenzyme A metabolism.•Auxiliary enzymes produce metabolites for export out of peroxisomes.•Peroxisomal β-oxidation requires auxiliary enzymes for optimal function.•N-acyl taurines can be synthesized in peroxisomes. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0300-9084 1638-6183 1638-6183 |
DOI: | 10.1016/j.biochi.2013.12.018 |