C4899
Carnitine Acetyltransferase from pigeon breast muscle
ammonium sulfate suspension, ≥50 units/mg protein
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Synonym(s):
CATC, Carnitine acetyltransferase, Acetyl-Co-A:carnitine-O-acetyltransferase, CrAT
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
pigeon breast
Quality Level
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
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
动植物源性产品
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)
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
In vivo clinical measures of intermediary metabolism are inadequate: can a new magnetic resonance spectroscopy technology do better?
James A Balschi
Circulation. Cardiovascular imaging, 5(2), 171-174 (2012-03-23)
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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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