Anti-ACAT1 Antibody Picoband® Fluoro647 Conjugated

Acetyl-CoA acetyltransferase, mitochondrial, also known as acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by the ACAT1 (Acetyl-Coenzyme A acetyltransferase 1) gene. This gene encodes a mitochondrially localized enzyme that catalyzes the reversible formation of acetoacetyl-CoA from two molecules of acetyl-CoA. Defects in this gene are associated with 3-ketothiolase deficiency, an inborn error of isoleucine catabolism characterized by urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, tiglylglycine, and butanone.

Bifunctional epoxide hydrolase 2; Cytosolic epoxide hydrolase 2; CEH;3.3.2.10; Epoxide hydratase; Soluble epoxide hydrolase; SEH; Lipid-phosphate phosphatase;3.1.3.76; EPHX2

Cancer Metabolism, Cardiovascular, Cell Biology, Cholesterol Metabolism, Drug Metabolism, Fatty Acid Oxidation, Fatty Acids, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Redox Metabolism, Signal Transduction, Vasculature

Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo- 9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro- 9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy- octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate. .

1. Daum, R. S., Scriver, C. R., Mamer, O. A., Delvin, E., Lamm, P. H., Goldman, H. An inherited disorder of isoleucine catabolism causing accumulation of alpha-methylacetoacetate and alpha-methyl-beta-hydroxybutyrate and intermittent metabolic acidosis. Pediat. Res. 7: 149-160, 1973. 2. Fukao, T., Matsuo, N., Zhang, G. X., Urasawa, R., Kubo, T., Kohno, Y., Kondo, N. Single base substitutions at the initiator codon in the mitochondrial acetoacetyl-CoA thiolase (ACAT1/T2) gene result in production of varying amounts of wild-type T2 polypeptide. Hum. Mutat. 21: 587-592, 2003. 3. Fukao, T., Nakamura, H., Nakamura, K., Perez-Cerda, C., Baldellou, A., Barrionuevo, C. R., Castello, F. G., Kohno, Y., Ugarte, M., Kondo, N. Characterization of six mutations in five Spanish patients with mitochondrial acetoacetyl-CoA thiolase deficiency: effects of amino acid substitutions on tertiary structure. Molec. Genet. Metab. 75: 235-243, 2002.