High impact information on Mte1

• High expression of MTE-I was found in liver from peroxisome proliferator treated rats and in heart and brown fat from control and induced rats [1].
• A 40-kDa enzyme was purified and characterized as a very long chain acyl-CoA thioesterase (MTE-I) [1].
• MTE-I was inhibited by p-chloromercuribenzoic acid, which implicates the importance of a cysteine residue in, or close, to the active site [1].
• Comparison of physical and catalytical characteristics of the enzymes studied here and previously purified acyl-CoA thioesterases suggest that MTE-I and MTE-II are novel enzymes [1].
• In this study, we investigated the tissue distribution of this multigene family of enzymes, focusing on cytosolic (CTE-I) and mitochondrial acyl-CoA thioesterases (MTE-I) in adult rats, using an anti-CTE-I antibody which recognizes both the isoforms [2].

Biological context of Mte1

• Western and Northern blot analyses showed that MTE-I is constitutively expressed in heart and is strongly induced in liver by feeding rats with di(2-ethylhexyl)phthalate, a peroxisome proliferator, suggesting a role for the enzyme in lipid metabolism [3].
• The ingestion of sesamin also resulted in an increase in the gene expression of acyl-CoA thioesterase involved in acyl-CoA hydrolase and very-long-chain acyl-CoA thioesterase [4].
• The protein is homologous to a family of novel acyl-CoA thioesterases and identical to a peroxisome proliferator-inducible mitochondrial acyl-CoA thioesterase that shows highest substrate specificity for very-long-chain fatty acids such as arachidoyl- and palmitoyl-CoA [5].

Anatomical context of Mte1

• CTE-I mRNA was strongly expressed in kidney and brown adipose tissue and MTE-I mRNA was expressed mainly in brown adipose tissue and heart but was also expressed in kidney and white adipose tissue [6].
• The sparsity of endoplasmic reticulum and the lack of detection of mitochondrial acyl CoA thioesterase, MTE-I, led to the conclusion that the increase in tumour acyl CoA thioesterase activity may be due to an increase in the activity of the peroxisomal enzyme [7].

Associations of Mte1 with chemical compounds

• As expected, both CTE-I and MTE-I were strongly upregulated (> 50-fold) by clofibrate treatment [6].
• They were identified as carnitine palmitoyltransferase 2, mitochondrial acyl-CoA thioesterase 1, isocitrate dehydrogenase 3 (NAD+) alpha, fumarate hydratase 1 and pyruvate dehydrogenase beta [8].

Other interactions of Mte1

• These results demonstrated the distribution of CTE-I and MTE-I in a wide variety of rat tissues, primarily characterized by an epithelial localization, being consistent with their involvement in fatty acid metabolism [2].

Analytical, diagnostic and therapeutic context of Mte1

• Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase [9].
• Western blot analysis showed that enzymes in the 40-kDa peak of the peroxisomal and cytosolic fractions were structurally related, but not identical, to a 40-kDa mitochondrial very-long-chain acyl-CoA thioesterase [10].
• In situ hybridization suggested colocalization of CTE-I and MTE-I in the kidney [2].

References