C4899
Carnitine Acetyltransferase from pigeon breast muscle
ammonium sulfate suspension, ≥50 units/mg protein
Synonyme(s) :
CrAT
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
pigeon breast
Niveau de qualité
Forme
ammonium sulfate suspension
Activité spécifique
≥50 units/mg protein
Concentration
≥0.4 mg/mL
Technique(s)
cell based assay: suitable
Numéro d'accès Protein ID
Numéro d'accès UniProt
Température de stockage
2-8°C
Informations sur le gène
pigeon ... CRAT(102084317)
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Description générale
Research area: Cell Signaling
Application
Carnitine Acetyltransferase from pigeon breast muscle has been used in enzymatic assays.
Actions biochimiques/physiologiques
Carnitine acyltransferases (CrAT) are enzymes that contribute to the reversible conversion of acetyl-CoA and carnitine into acetylcarnitine and free CoA. This enzymatic process plays a vital role in the energy metabolism of eukaryotes by promoting the β-oxidation of fatty acids. CrAT-mediated acetyl carnitine production and efflux help maintain a balance between acetyl-CoA and acetyl carnitine in the mitochondria, regenerate free CoA, and alleviate the product inhibition of pyruvate dehydrogenase (PDH), which is a key enzyme in glucose oxidation. This process promotes glucose homeostasis and helps maintain optimal cellular energy metabolism. Carnitine acetyltransferase activity also aids in the progression of the cell cycle from G1 to S phase. carnitine acetyltransferase deficiency also leads to the development of various neurological disorders including Alzheimer′s disease, ataxic encephalopathy, and several vascular diseases.
Carnitine acetyltransferase maintains the cellular and mitochondrial levels of acetyl-CoA, a key cofactor required for oxidative metabolism, by catalyzing an equilibrium between acetyl-CoA and acetyl-L-carnitine, a storage form of activated acetate. Carnitine acetyltransferase also maintains the pool of acetyl-CoA required for neuronal and nonneuronal acetylcholine production.
Définition de l'unité
One unit will convert 1.0 μmole of acetyl-L-carnitine and CoA to L-carnitine and acetyl-CoA per min at pH 8.0 at 25 °C.
Forme physique
Crystalline suspension in 3.2 M (NH4)2SO4 solution, 50 mM potassium phosphate, 1 mM dithiothreitol, pH 7.0
Remarque sur l'analyse
Protein determined by biuret.
Inhibiteur
Réf. du produit
Description
Tarif
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
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Proceedings of the National Academy of Sciences of the United States of America, 109(9), 3259-3263 (2012-02-14)
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Increased plasma free fatty acid (FFA) levels are a feature of insulin resistance and type 2 diabetes. The aim of the present study was to assess the effect of L-carnitine supplementation on plasma lipids and the expression of enzymes in
Marie A Schroeder et al.
Circulation. Cardiovascular imaging, 5(2), 201-209 (2012-01-13)
Carnitine acetyltransferase catalyzes the reversible conversion of acetyl-coenzyme A (CoA) into acetylcarnitine. The aim of this study was to use the metabolic tracer hyperpolarized [2-(13)C]pyruvate with magnetic resonance spectroscopy to determine whether carnitine acetyltransferase facilitates carbohydrate oxidation in the heart.
Ann T Hanna-Mitchell et al.
Life sciences, 80(24-25), 2298-2302 (2007-03-17)
Non-neuronal release of acetylcholine (ACh) has been proposed to play a role in urinary bladder function. These studies investigated the expression and function of the non-neuronal cholinergic system in cultured urothelial cells isolated from the rat urinary bladder. Our findings
Kristaps Jaudzems et al.
Journal of enzyme inhibition and medicinal chemistry, 24(6), 1269-1275 (2009-11-17)
Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups. In this study, biochemical measurements, saturation transfer
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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