Acyl-coenzyme A synthetases in metabolic control
| Autor: | Jessica M. Ellis, Jennifer L. Frahm, Rosalind A. Coleman, Lei O. Li |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Acyl Coenzyme A Synthetases
Endocrinology Diabetes and Metabolism Very long chain AMP-Activated Protein Kinases Article AMP-activated protein kinase Coenzyme A Ligases Genetics Animals Humans Disease adipocyte protein 2 Molecular Biology chemistry.chemical_classification Nutrition and Dietetics biology Fatty Acids Fatty acid Biological Transport Cell Biology Transport protein Biochemistry chemistry Metabolic control analysis biology.protein lipids (amino acids peptides and proteins) Cardiology and Cardiovascular Medicine |
| Popis: | The 11 long-chain (ACSL) and very long chain acyl-coenzyme A (acyl-CoA) synthetases [(ACSVL)/fatty acid transport protein] are receiving considerable attention because it has become apparent that their individual functions are not redundant.Recent studies have focused on the structure of the acyl-CoA synthetases, their post-translational modification, their ability to activate fatty acids of varying chain lengths, and their role in directing fatty acids into different metabolic pathways. An unsettled controversy focuses on the ACSVL isoforms and whether these have both enzymatic and transport functions. Another issue is whether conversion of a fatty acid to an acyl-CoA produces an increase in the AMP/ATP ratio that is sufficient to activate AMP-activated kinase.Future studies are required to determine the subcellular location of each ACSL and ACSVL isoform and the functional importance of phosphorylation and acetylation. Purification and crystallization of mammalian ACSL and ACSVL isoforms is needed to confirm the mechanism of action and discover how these enzymes differ in their affinity for fatty acids of different chain lengths. Functionally, it will be important to learn how the ACSL isoforms can direct their acyl-CoA products toward independent downstream pathways. |
| Databáze: | OpenAIRE |
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