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C4899

Sigma-Aldrich

Carnitine Acetyltransferase from pigeon breast muscle

ammonium sulfate suspension, ≥50 units/mg protein

Synonym(s):

CATC, Carnitine acetyltransferase, Acetyl-Co-A:carnitine-O-acetyltransferase, CrAT

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

pigeon breast

form

ammonium sulfate suspension

specific activity

≥50 units/mg protein

concentration

≥0.4 mg/mL

technique(s)

cell based assay: suitable

Protein ID accession no.

UniProt accession no.

storage temp.

2-8°C

Gene Information

pigeon ... CRAT(102084317)

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General description

Research area: Cell Signaling

Application

Carnitine Acetyltransferase from pigeon breast muscle has been used in enzymatic assays.

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

Crystalline suspension in 3.2 M (NH4)2SO4 solution, 50 mM potassium phosphate, 1 mM dithiothreitol, pH 7.0

Analysis Note

Protein determined by biuret.

inhibitor

Product No.
Description
Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Redesign of carnitine acetyltransferase specificity by protein engineering
Cordente AG, et al.
The Journal of Biological Chemistry, 279(32), 33899-33908 (2004)
Structure-based virtual screening to identify novel carnitine acetyltransferase activators
Ombrato R, et al.
Journal of Molecular Graphics & Modelling (2020)
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
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.
Rui Wu et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(9), 3259-3263 (2012-02-14)
Phenotypic plasticity occurs prevalently and plays a vital role in adaptive evolution. However, the underlying molecular mechanisms responsible for the expression of alternate phenotypes remain unknown. Here, a density-dependent phase polyphenism of Locusta migratoria was used as the study model

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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