CRAT: Key Enzyme in Body's Energy Metabolism (G1384)

Target Name: CRAT

NCBI ID: G1384

CRAT

CRAT: Key Enzyme in Body's Energy Metabolism

CRAT (Carnitine O-acetyltransferase precursor) is a protein that plays a crucial role in the body's energy metabolism. It is involved in the transfer of acetyl groups from the amino acid L-carnitine to the carbon chain of the long-chain fatty acids, which are the primary energy sources for the body.

CRAT is a key enzyme in the citric acid cycle (also known as the Krebs cycle or tricarboxylic acid (TCA) cycle), a process that generates energy in the form of ATP from the breakdown of fatty acids. The citric acid cycle is a vital part of the body's energy metabolism and is responsible for producing the majority of the ATP that the body uses to power its daily activities.

In addition to its role in the citric acid cycle, CRAT is also involved in the production of the amino acid L-carnitine, which is a critical fuel source for the body's muscles and other tissues. L-carnitine is synthesized in the body from the amino acids L-carnitine and L-histidine, but it can also be obtained from dietary sources such as red meat, organ meats, and fish.

CRAT is a protein that is expressed in most tissues of the body and is highly conserved across species. It is a 23-kDa protein that consists of 216 amino acids. It has a characteristic Rossmann-fold structure, which is a type of beta-sheet, and is located in the mitochondria.

CRAT is involved in the transfer of acetyl groups from L-carnitine to the carbon chain of long-chain fatty acids.

The role of CRAT in energy metabolism is supported by several studies. In one study published in the journal Nature Communications, researchers found that CRAT was significantly increased in the muscle tissue of obese individuals compared to lean individuals. The study suggested that the increased CRAT levels in obese individuals may contribute to the muscle atrophy and decreased muscle mass that is observed in this population.

Another study published in the journal Biochimica et Biophysica Acta found that CRAT was decreased in the livers of individuals with non-alcoholic steatohepatitis (NASH), a type of liver disease that is characterized by the accumulation of fat in the liver. The study suggested that the decreased CRAT levels in NASH individuals may contribute to the liver damage and the development of other health conditions associated with this disease.

In addition to its role in energy metabolism, CRAT is also involved in the production of L-carnitine. L-carnitine is a critical fuel source for the body's muscles and other tissues and is synthesized in the body from the amino acids L-carnitine and L-histidine. However, it can also be obtained from dietary sources such as red meat, organ meats, and fish.

The production of L-carnitine by CRAT is a well-established process that has been studied extensively. CRAT catalyzes the transfer of the acetyl group from L-carnitine to the carbon chain of long-chain fatty acids, such as acyl-CoA. This transfer of the acetyl group allows the fatty acids to be broken down into energy-carrying molecules, such as carbon dioxide and water, which are then exported from the cell.

CRAT is a protein that is highly conserved across species and is expressed in most tissues of the body. It is a 23-kDa protein that consists of 216 amino acids and has a characteristic Rossmann-fold structure.

The role of CRAT in energy metabolism is supported by several studies, including the one

Protein Name: Carnitine O-acetyltransferase

Functions: Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation (PubMed:15099582, PubMed:29395073). Responsible for the synthesis of short- and branched-chain acylcarnitines (PubMed:23485643). Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates (PubMed:23485643). Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates (PubMed:23485643)

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