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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:
9029-90-7
Enzyme Commission number:
2.3.1.7 (BRENDA, IUBMB)
MDL number:
MFCD00130725
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.

AAA80570.1

UniProt accession no.

P52826

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

C4899-BULK:
C4899-5MG:
C4899-VAR-N:
C4899-BULK-N:
C4899-1MG:
C4899-VAR:
C4899-10MG:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Marilou Ramos-Pamplona et al.
Molecular microbiology, 61(1), 61-75 (2006-07-11)
In lower eukaryotes, beta-oxidation of fatty acids is restricted primarily to the peroxisomes and the resultant acetyl-CoA molecules (and the chain-shortened fatty acids) are transported via the cytosol into the mitochondria for further breakdown and usage. Using a loss-of-function mutation
Huaijin Zhou et al.
Microbiology (Reading, England), 154(Pt 2), 500-509 (2008-01-30)
Carbon starvation is a significant stress encountered by the opportunistic fungal pathogen Candida albicans, and mutations in several pathways required to assimilate non-fermentable carbon sources attenuate virulence. These pathways -- beta-oxidation, the glyoxylate cycle and gluconeogenesis -- are compartmentalized in
Ida J van der Klei et al.
Biochimica et biophysica acta, 1763(12), 1794-1800 (2006-09-29)
Most peroxisomal matrix proteins contain a peroxisomal targeting signal 1 (PTS1) for sorting to the correct organelle. This signal is located at the extreme C-terminus and generally consists of only three amino acids. The PTS1 is recognized by the receptor
Antonio G Cordente et al.
FEMS microbiology letters, 267(2), 159-166 (2006-12-13)
The wine yeast Saccharomyces cerevisiae is central in the production of aroma compounds during fermentation. Some of the most important yeast-derived aroma compounds produced are esters. The esters ethyl acetate and isoamyl acetate are formed from alcohols and acetyl-CoA in
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