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Key Documents

10103241001

Roche

Carnitine Acetyltransferase

from pigeon breast muscle

Synonym(s):

acetylcarnitine transferase

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204

biological source

pigeon breast

Quality Level

form

suspension

specific activity

~80 units/mg protein (At 25 °C with CoA and acetyl-D,L-carnitine as the substrates.)

packaging

pkg of 1 mL (5 mg)

manufacturer/tradename

Roche

technique(s)

analytical sample preparation: suitable

color

white

optimum pH

7.3-8.0

solubility

water: miscible

NCBI accession no.

UniProt accession no.

application(s)

life science and biopharma

foreign activity

Acetyl-CoA-deacylase 0.01%

storage temp.

2-8°C

Gene Information

pigeon ... CRAT(102084317)

General description

Acetyl-CoA:carnitine O-acetyltransferase
Carnitine acetyltransferase is a mitochondrial enzyme essential for fuel utilization. It is present in the mitochondrial matrix and peroxisome. It is involved in the fatty acid metabolism. It facilitates conversion of acetyl-CoA and carnitine to acetylcarnitine and CoA respectively. This conversion facilitates peroxisomal β-oxidation by importing acetyl group for mitochondrial oxidation.

Quality

Contaminants: <0.01% acetyl-CoA-deacylase ion in storage buffer.

Physical form

Suspension in 2.9 M ammonium sulfate solution, 50 mM K-phosphate, 1 mM EDTA, pH approximately 7.5

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

No data available

flash_point_c

No data available


Certificates of Analysis (COA)

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Y Elgersma et al.
The EMBO journal, 14(14), 3472-3479 (1995-07-17)
Carnitine acetyltransferase (CAT) is present in mitochondria and peroxisomes of oleate-grown Saccharomyces cerevisiae. Both proteins are encoded by the same gene, YCAT, which encodes a protein with a mitochondrial targeting signal (MTS) at the N-terminus, and a peroxisomal targeting signal
Jiankang Liu et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(4), 1876-1881 (2002-02-21)
We test whether the dysfunction with age of carnitine acetyltransferase (CAT), a key mitochondrial enzyme for fuel utilization, is due to decreased binding affinity for substrate and whether this substrate, fed to old rats, restores CAT activity. The kinetics of

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