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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥50 units/mg protein
Biological source:
pigeon breast
Concentration:
≥0.4 mg/mL
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
Quality Level
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 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.
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.
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.
Other Notes
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.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
动植物源性产品
低风险生物材料
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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)
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
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
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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
以硫酸铵悬浮液形式提供的酶的使用指南
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