Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.
An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
An enzyme that catalyses the last step of the TRIACYLGLYCEROL synthesis reaction in which diacylglycerol is covalently joined to LONG-CHAIN ACYL COA to form triglyceride. It was formerly categorized as EC 2.3.1.124.
The addition of an organic acid radical into a molecule.

Submitochondrial and subcellular distributions of the carnitine-acylcarnitine carrier. (1/96)

The submitochondrial and subcellular distributions of the carnitine-acylcarnitine translocase (CAC) have been studied. CAC is enriched to a much lesser extent than the carnitine palmitoyltransferases within the contact sites of mitochondria. A high-abundance protein of identical molecular size as the mitochondrial CAC that is immunoreactive with an anti-peptide antibody raised against a linear epitope of mitochondrial CAC is present in peroxisomes but not in microsomes. This suggests that CAC is targeted to at least two different locations within the liver cell and that acylcarnitine transport into peroxisomes is CAC mediated.  (+info)

Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p. (2/96)

In Saccharomyces cerevisiae, beta-oxidation of fatty acids is confined to peroxisomes. The acetyl-CoA produced has to be transported from the peroxisomes via the cytoplasm to the mitochondrial matrix in order to be degraded to CO(2) and H(2)O. Two pathways for the transport of acetyl-CoA to the mitochondria have been proposed. The first involves peroxisomal conversion of acetyl-CoA into glyoxylate cycle intermediates followed by transport of these intermediates to the mitochondria. The second pathway involves peroxisomal conversion of acetyl-CoA into acetylcarnitine, which is subsequently transported to the mitochondria. Using a selective screen, we have isolated several mutants that are specifically affected in the second pathway, the carnitine-dependent acetyl-CoA transport from the peroxisomes to the mitochondria, and assigned these CDAT mutants to three different complementation groups. The corresponding genes were identified using functional complementation of the mutants with a genomic DNA library. In addition to the previously reported carnitine acetyl-CoA transferase (CAT2), we identified the genes for the yeast orthologue of the human mitochondrial carnitine acylcarnitine translocase (YOR100C or CAC) and for a transport protein (AGP2) required for carnitine transport across the plasma membrane.  (+info)

Arrhythmias and conduction defects as presenting symptoms of fatty acid oxidation disorders in children. (3/96)

BACKGROUND: The clinical manifestations of inherited disorders of fatty acid oxidation vary according to the enzymatic defect. They may present as isolated cardiomyopathy, sudden death, progressive skeletal myopathy, or hepatic failure. Arrhythmia is an unusual presenting symptom of fatty acid oxidation deficiencies. METHODS AND RESULTS: Over a period of 25 years, 107 patients were diagnosed with an inherited fatty acid oxidation disorder. Arrhythmia was the predominant presenting symptom in 24 cases. These 24 cases included 15 ventricular tachycardias, 4 atrial tachycardias, 4 sinus node dysfunctions with episodes of atrial tachycardia, 6 atrioventricular blocks, and 4 left bundle-branch blocks in newborn infants. Conduction disorders and atrial tachycardias were observed in patients with defects of long-chain fatty acid transport across the inner mitochondrial membrane (carnitine palmitoyl transferase type II deficiency and carnitine acylcarnitine translocase deficiency) and in patients with trifunctional protein deficiency. Ventricular tachycardias were observed in patients with any type of fatty acid oxidation deficiency. Arrhythmias were absent in patients with primary carnitine carrier, carnitine palmitoyl transferase I, and medium chain acyl coenzyme A dehydrogenase deficiencies. CONCLUSIONS: The accumulation of arrhythmogenic intermediary metabolites of fatty acids, such as long-chain acylcarnitines, may be responsible for arrhythmias. Inborn errors of fatty acid oxidation should be considered in unexplained sudden death or near-miss in infants and in infants with conduction defects or ventricular tachycardia. Diagnosis can be easily ascertained by an acylcarnitine profile from blood spots on filter paper.  (+info)

Evidence for triacylglycerol synthesis in the lumen of microsomes via a lipolysis-esterification pathway involving carnitine acyltransferases. (4/96)

In this study a pathway for the synthesis of triacylglycerol (TAG) within the lumen of the endoplasmic reticulum has been identified, using microsomes that had been preconditioned by depleting their endogenous substrates and then fusing them with biotinylated phosphatidylserine liposomes containing CoASH and Mg(2+). Incubating these fused microsomes with tri[(3)H] oleoylglycerol and [(14)C]oleoyl-CoA yielded microsome-associated triacylglycerol, which resisted extensive washing and had a [(3)H]:[(14)C] ratio close to 2:1. The data suggest that the precursor tri[(3)H]oleoylglycerol was hydrolyzed by microsomal lipase to membrane-bound di[(3)H]oleoylglycerol and subsequently re-esterified with luminal [(14)C]oleoyl-CoA. The accumulation of TAG within the microsomes, even when overt diacylglycerol acyltransferase (DGAT I) was inactive, is consistent with the existence of a latent diacylglycerol acyltransferase (DGAT II) within the microsomal lumen. Moreover, because luminal synthesis of TAG was carnitine-dependent and markedly reduced by glybenclamide, a potent carnitine acyltransferase inhibitor, microsomal carnitine acyltransferase appears to be essential for trafficking the [(14)C]oleoyl-CoA into the microsomal lumen for subsequent incorporation into newly synthesized TAG. This study thus provides the first direct demonstration of an enzymatic process leading to the synthesis of luminal triacylglycerol, which is a major component of very low density lipoproteins.  (+info)

Identification of the two histidine residues responsible for the inhibition by malonyl-CoA in peroxisomal carnitine octanoyltransferase from rat liver. (5/96)

Carnitine octanoyltransferase (COT), an enzyme that facilitates the transport of medium chain fatty acids through peroxisomal membranes, is inhibited by malonyl-CoA. cDNAs encoding full-length wild-type COT and one double mutant variant from rat peroxisomal COT were expressed in Saccharomyces cerevisiae. Both expressed forms were expressed similarly in quantitative terms and exhibited full enzyme activity. The wild-type-expressed COT was inhibited by malonyl-CoA like the liver enzyme. The activity of the enzyme encoded by the double mutant H131A/H340A was completely insensitive to malonyl-CoA in the range assayed (2-200 microM). These results indicate that the two histidine residues, H131 and H340, are the sites responsible for inhibition by malonyl-CoA. Another mutant variant, H327A, abolishes the enzyme activity, from which it is concluded that it plays an important role in catalysis.  (+info)

Identification and functions of new transporters in yeast mitochondria. (6/96)

The genome of Saccharomyces cerevisiae encodes 35 putative members of the mitochondrial carrier family. Known members of this family transport substrates and products across the inner membranes of mitochondria. We are attempting to identify the functions of the yeast mitochondrial transporters via high-yield expression in Escherichia coli and/or S. cerevisiae, purification and reconstitution of their protein products into liposomes, where their transport properties are investigated. With this strategy, we have already identified the functions of seven S. cerevisiae gene products, whose structural and functional properties assigned them to the mitochondrial carrier family. The functional information obtained in the reconstituted system and the use of knock-out yeast strains can be usefully exploited for the investigation of the physiological role of individual transporters. Furthermore, the yeast carrier sequences can be used to identify the orthologous proteins in other organisms, including man.  (+info)

Inhibition by etomoxir of rat liver carnitine octanoyltransferase is produced through the co-ordinate interaction with two histidine residues. (7/96)

Rat peroxisomal carnitine octanoyltransferase (COT), which facilitates the transport of medium-chain fatty acids through the peroxisomal membrane, is irreversibly inhibited by the hypoglycaemia-inducing drug etomoxir. To identify the molecular basis of this inhibition, cDNAs encoding full-length wild-type COT, two different variant point mutants and one variant double mutant from rat peroxisomal COT were expressed in Saccharomyces cerevisiae, an organism devoid of endogenous COT activity. The recombinant mutated enzymes showed activity towards both carnitine and decanoyl-CoA in the same range as the wild type. Whereas the wild-type version expressed in yeast was inhibited by etomoxir in an identical manner to COT from rat liver peroxisomes, the activity of the enzyme containing the double mutation H131A/H340A was completely insensitive to etomoxir. Individual point mutations H131A and H340A also drastically reduced sensitivity to etomoxir. Taken together, these results indicate that the two histidine residues, H131 and H340, are the sites responsible for inhibition by etomoxir and that the full inhibitory properties of the drug will be shown only if both histidines are intact at the same time. Our data demonstrate that both etomoxir and malonyl-CoA inhibit COT by interacting with the same sites.  (+info)

Molecular enzymology of carnitine transfer and transport. (8/96)

Carnitine (L-3-hydroxy-4-N-trimethylaminobutyric acid) forms esters with a wide range of acyl groups and functions to transport and excrete these groups. It is found in most cells at millimolar levels after uptake via the sodium-dependent carrier, OCTN2. The acylation state of the mobile carnitine pool is linked to that of the limited and compartmentalised coenzyme A pools by the action of the family of carnitine acyltransferases and the mitochondrial membrane transporter, CACT. The genes and sequences of the carriers and the acyltransferases are reviewed along with mutations that affect activity. After summarising the accepted enzymatic background, recent molecular studies on the carnitine acyltransferases are described to provide a picture of the role and function of these freely reversible enzymes. The kinetic and chemical mechanisms are also discussed in relation to the different inhibitors under study for their potential to control diseases of lipid metabolism.  (+info)

Carnitine acyltransferases are a group of enzymes that play a crucial role in the transport and metabolism of fatty acids within cells. These enzymes are responsible for transferring acyl groups from acyl-CoAs to carnitine, forming acylcarnitines, which can then be transported across the mitochondrial membrane and into the mitochondrial matrix.

Once inside the matrix, the acyl groups can be released from carnitine and oxidized in the beta-oxidation pathway to produce energy in the form of ATP. There are three main types of carnitine acyltransferases: Carnitine palmitoyltransferase I (CPT I), located on the outer mitochondrial membrane, which activates long-chain fatty acids for transport into the mitochondria; Carnitine palmitoyltransferase II (CPT II), located on the inner mitochondrial membrane, which reconverts acylcarnitines back to acyl-CoAs for oxidation; and carnitine octanoyltransferase (CRAT), which is involved in the metabolism of medium-chain fatty acids.

Deficiencies in these enzymes can lead to various metabolic disorders, such as CPT II deficiency, which can cause muscle weakness, hypoglycemia, and cardiomyopathy. Proper regulation of carnitine acyltransferases is essential for maintaining healthy fatty acid metabolism and overall cellular function.

Carnitine O-acetyltransferase (COAT) is an enzyme that plays a crucial role in the transport and metabolism of fatty acids within cells. It is also known as carnitine palmitoyltransferase I (CPT I).

The primary function of COAT is to catalyze the transfer of an acetyl group from acetyl-CoA to carnitine, forming acetylcarnitine and free CoA. This reaction is essential for the entry of long-chain fatty acids into the mitochondrial matrix, where they undergo beta-oxidation to produce energy in the form of ATP.

COAT is located on the outer membrane of the mitochondria and functions as a rate-limiting enzyme in fatty acid oxidation. Its activity can be inhibited by malonyl-CoA, which is an intermediate in fatty acid synthesis. This inhibition helps regulate the balance between fatty acid oxidation and synthesis, ensuring that cells have enough energy while preventing excessive accumulation of lipids.

Deficiencies or mutations in COAT can lead to various metabolic disorders, such as carnitine palmitoyltransferase I deficiency (CPT I deficiency), which may cause symptoms like muscle weakness, hypoglycemia, and cardiomyopathy. Proper diagnosis and management of these conditions often involve dietary modifications, supplementation with carnitine, and avoidance of fasting to prevent metabolic crises.

Carnitine is a naturally occurring substance in the body that plays a crucial role in energy production. It transports long-chain fatty acids into the mitochondria, where they can be broken down to produce energy. Carnitine is also available as a dietary supplement and is often used to treat or prevent carnitine deficiency.

The medical definition of Carnitine is:

"A quaternary ammonium compound that occurs naturally in animal tissues, especially in muscle, heart, brain, and liver. It is essential for the transport of long-chain fatty acids into the mitochondria, where they can be oxidized to produce energy. Carnitine also functions as an antioxidant and has been studied as a potential treatment for various conditions, including heart disease, diabetes, and kidney disease."

Carnitine is also known as L-carnitine or levocarnitine. It can be found in foods such as red meat, dairy products, fish, poultry, and tempeh. In the body, carnitine is synthesized from the amino acids lysine and methionine with the help of vitamin C and iron. Some people may have a deficiency in carnitine due to genetic factors, malnutrition, or certain medical conditions, such as kidney disease or liver disease. In these cases, supplementation may be necessary to prevent or treat symptoms of carnitine deficiency.

Acyltransferases are a group of enzymes that catalyze the transfer of an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydrogen atom) from one molecule to another. This transfer involves the formation of an ester bond between the acyl group donor and the acyl group acceptor.

Acyltransferases play important roles in various biological processes, including the biosynthesis of lipids, fatty acids, and other metabolites. They are also involved in the detoxification of xenobiotics (foreign substances) by catalyzing the addition of an acyl group to these compounds, making them more water-soluble and easier to excrete from the body.

Examples of acyltransferases include serine palmitoyltransferase, which is involved in the biosynthesis of sphingolipids, and cholesteryl ester transfer protein (CETP), which facilitates the transfer of cholesteryl esters between lipoproteins.

Acyltransferases are classified based on the type of acyl group they transfer and the nature of the acyl group donor and acceptor molecules. They can be further categorized into subclasses based on their sequence similarities, three-dimensional structures, and evolutionary relationships.

Carnitine O-palmitoyltransferase (CPT) is an enzyme that plays a crucial role in the transport of long-chain fatty acids into the mitochondrial matrix, where they undergo beta-oxidation to produce energy. There are two main forms of this enzyme: CPT1 and CPT2.

CPT1 is located on the outer mitochondrial membrane and catalyzes the transfer of a long-chain fatty acyl group from coenzyme A (CoA) to carnitine, forming acylcarnitine. This reaction is reversible and allows for the regulation of fatty acid oxidation in response to changes in energy demand.

CPT2 is located on the inner mitochondrial membrane and catalyzes the reverse reaction, transferring the long-chain fatty acyl group from carnitine back to CoA, allowing for the entry of the fatty acid into the beta-oxidation pathway.

Deficiencies in CPT1 or CPT2 can lead to serious metabolic disorders, such as carnitine deficiency and mitochondrial myopathies, which can cause muscle weakness, cardiomyopathy, and other symptoms. Treatment may involve dietary modifications, supplementation with carnitine or medium-chain fatty acids, and in some cases, enzyme replacement therapy.

1-Acylglycerophosphocholine O-Acyltransferase is an enzyme that belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. It is responsible for catalyzing the reaction that transfers an acyl group from an acyl-CoA to the sn-2 position of 1-acylglycerophosphocholine, resulting in the formation of phosphatidylcholine, which is a major component of biological membranes. This enzyme plays a crucial role in lipid metabolism and has been implicated in various diseases, including atherosclerosis, non-alcoholic fatty liver disease, and cancer.

Glycerol-3-Phosphate O-Acyltransferase (GPAT) is an enzyme that plays a crucial role in the biosynthesis of triacylglycerols and phospholipids, which are major components of cellular membranes and energy storage molecules. The GPAT enzyme catalyzes the initial and rate-limiting step in the glycerolipid synthesis pathway, specifically the transfer of an acyl group from an acyl-CoA donor to the sn-1 position of glycerol-3-phosphate, forming lysophosphatidic acid (LPA). This reaction is essential for the production of various glycerolipids, including phosphatidic acid, diacylglycerol, and triacylglycerol. There are four isoforms of GPAT (GPAT1-4) in humans, each with distinct subcellular localizations and functions. Dysregulation of GPAT activity has been implicated in several pathological conditions, such as metabolic disorders, cardiovascular diseases, and cancers.

Acyl Coenzyme A (often abbreviated as Acetyl-CoA or Acyl-CoA) is a crucial molecule in metabolism, particularly in the breakdown and oxidation of fats and carbohydrates to produce energy. It is a thioester compound that consists of a fatty acid or an acetate group linked to coenzyme A through a sulfur atom.

Acyl CoA plays a central role in several metabolic pathways, including:

1. The citric acid cycle (Krebs cycle): In the mitochondria, Acyl-CoA is formed from the oxidation of fatty acids or the breakdown of certain amino acids. This Acyl-CoA then enters the citric acid cycle to produce high-energy electrons, which are used in the electron transport chain to generate ATP (adenosine triphosphate), the main energy currency of the cell.
2. Beta-oxidation: The breakdown of fatty acids occurs in the mitochondria through a process called beta-oxidation, where Acyl-CoA is sequentially broken down into smaller units, releasing acetyl-CoA, which then enters the citric acid cycle.
3. Ketogenesis: In times of low carbohydrate availability or during prolonged fasting, the liver can produce ketone bodies from acetyl-CoA to supply energy to other organs, such as the brain and heart.
4. Protein synthesis: Acyl-CoA is also involved in the modification of proteins by attaching fatty acid chains to them (a process called acetylation), which can influence protein function and stability.

In summary, Acyl Coenzyme A is a vital molecule in metabolism that connects various pathways related to energy production, fatty acid breakdown, and protein modification.

Diacylglycerol O-Acyltransferase (DGAT) is an enzyme that catalyzes the final step in triacylglycerol synthesis, which is the formation of diacylglycerol and fatty acyl-CoA into triacylglycerol. This enzyme plays a crucial role in lipid metabolism and energy storage in cells. There are two main types of DGAT enzymes, DGAT1 and DGAT2, which share limited sequence similarity but have similar functions. Inhibition of DGAT has been explored as a potential therapeutic strategy for the treatment of obesity and related metabolic disorders.

Acylation is a medical and biological term that refers to the process of introducing an acyl group (-CO-) into a molecule. This process can occur naturally or it can be induced through chemical reactions. In the context of medicine and biology, acylation often occurs during post-translational modifications of proteins, where an acyl group is added to specific amino acid residues, altering the protein's function, stability, or localization.

An example of acylation in medicine is the administration of neuraminidase inhibitors, such as oseltamivir (Tamiflu), for the treatment and prevention of influenza. These drugs work by inhibiting the activity of the viral neuraminidase enzyme, which is essential for the release of newly formed virus particles from infected cells. Oseltamivir is administered orally as an ethyl ester prodrug, which is then hydrolyzed in the body to form the active acylated metabolite that inhibits the viral neuraminidase.

In summary, acylation is a vital process in medicine and biology, with implications for drug design, protein function, and post-translational modifications.

Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, ... Farrell, S. O.; Fiol, C. J.; Reddy, J. K.; Bieber, L. L. (1984-11-10). "Properties of purified carnitine acyltransferases of ... In the absence of carnitine acetyltransferase (CRAT), acyltransferases such as CROT can catalyze the acetyl group transfer from ... The significant catalytic residue within all carnitine acyltransferases, including CROT, has been found to be a histidine ...
Cronin CN (Sep 1997). "The conserved serine-threonine-serine motif of the carnitine acyltransferases is involved in carnitine ... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... "Carnitine acyltransferase enzymic catalysis requires a positive charge on the carnitine cofactor". Archives of Biochemistry and ... Jogl G, Hsiao YS, Tong L (Nov 2004). "Structure and function of carnitine acyltransferases". Annals of the New York Academy of ...
... (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase ( ... It is part of a family of enzymes called carnitine acyltransferases. This "preparation" allows for subsequent movement of the ... van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes ... Carnitine palmitoyltransferase I is the first component and rate-limiting step of the carnitine palmitoyltransferase system, ...
van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes ... Carnitine O-palmitoyltransferase 2, mitochondrial is an enzyme that in humans is encoded by the CPT2 gene. Carnitine ... CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. Defects in this gene ... Verderio E, Cavadini P, Montermini L, Wang H, Lamantea E, Finocchiaro G, DiDonato S, Gellera C, Taroni F (1995). "Carnitine ...
PDOC00402 - Acyltransferases ChoActase / COT / CPT family in PROSITE Choline/Carnitine o-acyltransferase family[permanent dead ... A related transferase is carnitine acyltransferase. Palmitoylcarnitine Palmitoyl CoA There are four different forms of CPT in ... Carnitine O-palmitoyltransferase (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3. ... humans: CPT1A - associated with Carnitine palmitoyltransferase I deficiency CPT1B CPT1C CPT2 - associated with carnitine ...
CPT II shares structural elements with other members of the carnitine acyltransferase protein family. The crystal structure of ... Carnitine O-palmitoyltransferase Carnitine palmitoyltransferase I deficiency Fasciculation Myokymia Primary carnitine ... 1993). "Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a ... The "carnitine shuttle" is composed of three enzymes that utilize carnitine to facilitate the import of hydrophobic long-chain ...
Carnitine octanoyltransferase (EC 2.3.1.137) is a carnitine acyltransferase that catalyzes the reversible transfer of fatty ... 2000). "Genomics of the human carnitine acyltransferase genes". Mol. Genet. Metab. 71 (1-2): 139-53. doi:10.1006/mgme.2000.3055 ... 2000) reviewed the function, structural features, and phylogenetics of human carnitine acyltransferase genes, including CROT.[ ... 2002). "Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: ...
There carnitine acyltransferase II reverses the process, producing fatty acyl-CoA and carnitine. This shuttle mechanism is ... They are converted to fatty acyl carnitine by carnitine acyltransferase I, an enzyme of the inner leaflet of the outer ... Fatty acyl carnitine is then transported by an antiport in exchange for free carnitine to the inner surface of the inner ...
This reaction takes place in the mitochondrial matrix and is catalyzed by carnitine acyltransferase 2 (also called carnitine ... L-Carnitine, acetyl-l-carnitine, and propionyl-l-carnitine are available in dietary supplement pills or powders, with a daily ... Carnitine exists as one of two stereoisomers (the two enantiomers d-carnitine (S-(+)-) and l-carnitine (R-(−)-)). Both are ... Two types of carnitine deficiency states exist. Primary carnitine deficiency is a genetic disorder of the cellular carnitine- ...
... carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal β-oxidation and palmitoyl-CoA ...
... carnitine acyltransferase, AMP-activated protein kinase, and others. These enzymes are important targets for drug discovery ...
... but not as a protease or a carnitine acyltransferase". Archives of Biochemistry and Biophysics. 323 (2): 397-403. doi:10.1006/ ...
... inhibits fatty acids from associating with carnitine by regulating the enzyme carnitine acyltransferase, thereby ...
... carnitine and carnitine acyltransferase I and II, reducing their bioavailability and consequently inhibiting beta oxidation of ...
... new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to carnitine with carnitine acyltransferase ...
... carnitine acyltransferases MeSH D08.811.913.050.350.170 - carnitine O-acetyltransferase MeSH D08.811.913.050.350.200 - ... diacylglycerol o-acyltransferase MeSH D08.811.913.050.425 - glycerol-3-phosphate O-acyltransferase MeSH D08.811.913.050.600 - ... phosphatidylcholine-sterol O-acyltransferase MeSH D08.811.913.050.646 - retinol O-fatty-acyltransferase MeSH D08.811.913.050. ... 1-acylglycerol-3-phosphate O-acyltransferase MeSH D08.811.913.050.175 - 1-acylglycerophosphocholine O-acyltransferase MeSH ...
The liberated carnitine returns to the cytosol. It is important to note that carnitine acyltransferase I undergoes allosteric ... This occurs via a series of similar steps: Acyl CoA is conjugated to carnitine by carnitine acyltransferase I ( ... is converted to acyl CoA by carnitine acyltransferase (palmitoyltransferase) II located on the inner mitochondrial membrane. ... I located on the outer mitochondrial membrane Acyl carnitine is shuttled inside by a translocase Acyl carnitine (such as ...
Family 4.C.2 The Carnitine O-Acyl Transferase (CrAT) Family 4.C.3 The Acyl-CoA Thioesterase (AcoT) Family 4.D.1 The Putative ... Family 2.A.14 Lactate Permease Family 2.A.15 The Betaine/Carnitine/Choline Transporter (BCCT) Family 2.A.16 Tellurite- ...
... diacylglycerol O-acyltransferase EC 2.3.1.21: carnitine O-palmitoyltransferase EC 2.3.1.22: 2-acylglycerol O-acyltransferase EC ... phosphatidylcholine-retinol O-acyltransferase EC 2.3.1.136: polysialic-acid O-acetyltransferase EC 2.3.1.137: carnitine O- ... dolichol O-acyltransferase EC 2.3.1.124: Already listed as EC 2.3.1.20 EC 2.3.1.125: 1-alkyl-2-acetylglycerol O-acyltransferase ... sphingosine N-acyltransferase EC 2.3.1.25: plasmalogen synthase EC 2.3.1.26: sterol O-acyltransferase EC 2.3.1.27: cortisol O- ...
Glycine-N-acyltransferase GLYATL2 encoding protein Glycine-N-acyltransferase like 2 GPHA2: Glycoprotein hormone alpha-2 GYLTL1B ... carnitine palmitoyltransferase 1A (liver) CREBZF encoding protein CREB/ATF bZIP transcription factor DAK: Triokinase/FMN ... monoacylglycerol O-acyltransferase 2 MTRNR2L8: encoding protein MT-RNR2-like 8 NADSYN1: NAD synthetase 1 NAP1L4: nucleosome ... DGAT2 encoding protein Diacylglycerol O-acyltransferase 2 DHCR7: 7-dehydrocholesterol reductase DKK3: Dickkopf-related protein ...
"Downregulation of carnitine acyltransferases and organic cation transporter OCTN2 in mononuclear cells in healthy elderly and ... an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency". Human ... characterized by impaired carnitine transport, urinary carnitine wasting, low serum carnitine levels, reduced intracellular ... "Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter". ...
β-oxidation in the peroxisome requires the use of a peroxisomal carnitine acyltransferase (instead of carnitine acyltransferase ... Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, as a carnitine is shuttled outside. Acyl-carnitine ... The liberated carnitine is shuttled back to the cytosol, as an acyl-carnitine is shuttled into the matrix. If the fatty acyl- ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ...
However, no formal assessment of the utility of carnitine and arginine supplementation has been published, and its uses have ... Neuwald AF (August 1997). "Barth syndrome may be due to an acyltransferase deficiency". Current Biology. 7 (8): R465-6. doi: ... Metabolic deficiencies have been treated by oral arginine and carnitine supplementation, which has been shown to ameliorate ... CL remodeling in mammals requires additional enzymes, such as monolysocardiolipin acyltransferase (MLCLAT), acyl-CoA: ...
SLC22A3 is an extraneuronal monoamine transporter that is present in astrocytes, and SLC22A5 is a high-affinity carnitine ... CYP2D6, dopamine β-hydroxylase, flavin-containing monooxygenase 3, butyrate-CoA ligase, and glycine N-acyltransferase are the ... cite encyclopedia}}: ,work= ignored (help) "Substrate/Product". glycine N-acyltransferase. Archived from the original on 23 ...
... : diacylglycerol acyltransferase (DGAT) plays an important role in energy metabolism on account of key enzyme in ... Transport of acyl-CoA into the mitochondria requires carnitine palmitoyltransferase 1 (CPT1), which converts acyl-CoA into ... Yu, Yi‐Hao; Ginsberg, Henry (8 July 2009). "The role of acyl‐CoA:diacylglycerol acyltransferase (DGAT) in energy metabolism". ...
Lysophosphatidylcholine acyltransferase 1 LYRM7: encoding protein LYR motif containing 7 LYSMD3: LysM and putative ... carboxylase deficiency Myelodysplastic syndrome Netherton syndrome Nicotine dependency Parkinson's disease Primary carnitine ...
Chen S, Ogawa A, Ohneda M, Unger RH, Foster DW, McGarry JD (July 1994). "More direct evidence for a malonyl-CoA-carnitine ... It works by inhibiting the enzyme Carnityl Acyl Transferase I (CAT-I) indirectly which is present in the mitochondria. This ... Lehtihet M, Welsh N, Berggren PO, Cook GA, Sjoholm A (August 2003). "Glibenclamide inhibits islet carnitine ...
... carnitine dehydratase - carrier - carveol dehydrogenase - CAT assay - CAT RNA-binding domain - catalase-related immune- ... palmitoyl acyltransferase - Parkinson's disease - pBR322 - PCR - pedigree - peptide - peptide-transporting ATPase - peptide ... phospholipid acyltransferase - phosphonate-transporting ATPase - phosphorylation - physical map - plant calmodulin-binding ...
Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, as a carnitine is shuttled outside. Acyl-carnitine ... Enzymes, acyltransferases and transacylases, incorporate fatty acids in phospholipids, triacylglycerols, etc. by transferring ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ... The liberated carnitine is shuttled back to the cytosol, as an acyl-CoA is shuttled into the mitochondrial matrix. Beta ...
Rytting E, Audus KL (January 2005). "Novel organic cation transporter 2-mediated carnitine uptake in placental choriocarcinoma ... and glycine N-acyltransferase (GLYAT) are the enzymes known to metabolize amphetamine or its metabolites in humans. Amphetamine ... and SLC22A5 is a high-affinity carnitine transporter. Amphetamine is known to strongly induce cocaine- and amphetamine- ... the role of glycine N-acyltransferase, and factors that influence interindividual variation". Expert Opinion on Drug Metabolism ...
The role of carnitine via the action of carnitine acyltransferase in buffering CoA availability in the mitochondrial matrix is ... N2 - The role of carnitine via the action of carnitine acyltransferase in buffering CoA availability in the mitochondrial ... AB - The role of carnitine via the action of carnitine acyltransferase in buffering CoA availability in the mitochondrial ... abstract = "The role of carnitine via the action of carnitine acyltransferase in buffering CoA availability in the ...
Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, ... Farrell, S. O.; Fiol, C. J.; Reddy, J. K.; Bieber, L. L. (1984-11-10). "Properties of purified carnitine acyltransferases of ... In the absence of carnitine acetyltransferase (CRAT), acyltransferases such as CROT can catalyze the acetyl group transfer from ... The significant catalytic residue within all carnitine acyltransferases, including CROT, has been found to be a histidine ...
... are catalyzed by the enzyme carnitine acyl transferase. Defects in this enzyme or in the carnitine carrier are inborn errors of ... are catalyzed by the enzyme carnitine acyl transferase. Defects in this enzyme or in the carnitine carrier are inborn errors of ... carnitine acyl transferase (enzyme). metabolism: Formation of fatty acyl coenzyme A molecules: … ... carnitine acyltransferase (enzyme). metabolism: Formation of fatty acyl coenzyme A molecules: … ...
Carnitine acyltransferase (CAT) transports free fatty acids into the mitochondria and therefore regulates their entry into the ...
HIV-1 Vpr enhances PPARbeta/delta-induced PDK4, carnitine palmitoyltransferase I (CPT1), and acetyl-coenzyme A acyltransferase ...
PDK4, Pyruvate dehydrogenase kinase 4; SLC25A20, carnitine-acylcarnitine translocase; ACAA2, acetyl-Coenzyme A acyltransferase ... carnitine-acylcarnitine translocase; ACAA2, acetyl-Coenzyme A acyltransferase 2. ... 2; CPT1, Carnitine palmitoyltransferase 1; ABCA1, ATP binding cassette transporter 1; TLR4, Toll-like receptor-4; PPARγ, ...
Acylethanolamines can be found in the mitochondria in vitro [191] and palmitoyl requires carnitine to enter mitochondria. When ... phosphatidylethanolamine can serve as a substrate for acyltransferases and indeed N-acylphosphoethanolamine (NAPE) is produced ... A. Augustyniak and E. Skrzydlewska, "The influence of L-carnitine suplementation on the antioxidative abilities of serum and ... cells or animals receive carnitine it acts as a neuroprotective agent, preventing ethanol-induced damage [147]. Furthermore, ϖ ...
Carmovirus Carmustine Carney Complex Carnitine Carnitine Acyltransferases Carnitine O-Acetyltransferase Carnitine O- .... ...
Carnitine acyltransferase (CAT) transports free fatty acids into the mitochondria and therefore regulates their entry into the ...
... which activates the carnitine acyltransferase system [6, 7]. This increases fatty acid oxidation and ketogenesis [6, 7]. In ...
There carnitine acyl transferase II reverses the process, producing fatty acyl-CoA and carnitine. This shuttle mechanism is ... They are converted to fatty acyl carnitine by carnitine acyl transferase I, an enzyme of the inner leaflet of the outer ... Fatty acyl carnitine is then transported by an antiport in exchange for free carnitine to the inner surface of the inner ...
There carnitine acyl transferase II reverses the process, producing fatty acyl-CoA and carnitine. This shuttle mechanism is ... They are converted to fatty acyl carnitine by carnitine acyl transferase I, an enzyme of the inner leaflet of the outer ... Fatty acyl carnitine is then transported by an antiport in exchange for free carnitine to the inner surface of the inner ...
This occurs enzymatically via carnitine acyltransferases. Specific acylcarnitines accumulate as a result of various organic ... Plasma samples revealed low levels of free carnitine (C0), long-chain acyl-carnitines and total carnitine. In particular, C0 ... To measure total carnitine, samples are spiked with deuterated carnitine (internal standard) and hydrolyzed with potassium ... Abnormal levels of free carnitine, total carnitine, and acylcarnitines in serum can be indicative of a metabolic disorder ...
In the cells treated with PA and HG, expressions of glucose transporter 4 (Glut4) and carnitine acyltransferase I (CPT1) for ß- ... Moreover, carnitine palmitoyltransferase 1A, a central regulator of fatty acid oxidation, was downregulated and its expression ... acyl-coenzyme A oxidase 1 carnitine palmitoyl transferase 1α and peroxisome proliferator-activated receptor α) expression was ...
... from the cytoplasm to the mitochondrial ICA-110381 matrix mediated by successive carnitine acyltransferases (6). Carnitine ... acyl-CoAs to carnitine on the outer mitochondrial membrane generating acylcarnitines that can traverse through the Carnitine- ...
Results:: Genes associated with β-oxidation (peroxisome proliferator-activated receptor α, carnitine palmitoyltransferase 1A, ... cholesterol acyltransferase 2), fatty acid transport (fatty acid-binding protein), construction of triglycerides in the ... Results:: Genes associated with β-oxidation (peroxisome proliferator-activated receptor α, carnitine palmitoyltransferase 1A, ... Results:: Genes associated with β-oxidation (peroxisome proliferator-activated receptor α, carnitine palmitoyltransferase 1A, ...
... and choline/carnitine O-acyltransferase, compared. ...
Carnitine acyl transferase-I (CAT-I) is associated with the outer surface of the inner mitochondrial membrane - Carnitine ... Carnitine-acyl transferase II (CAT-II) is associated with the inner surface of the inner mitochondrial membrane and catalyzes ... Lecithin cholesterol acyltransferase (LCAT)- found in the plasma and participates in reverse cholesterol transport by HDL - ... translocase trnasports fatty acyl carnitine into the mitochondria and transports free carnitine back out of the mitochondria - ...
"Choline/carnitine acyltransferase domain [Interproscan].","protein_coding" "PTI_16G00930.1","No alias","Phaeodactylum ... ","Biotin/lipoyl attachment; 2-oxoacid dehydrogenase acyltransferase, catalytic domain [Interproscan].","protein_coding" "OT_ ...
Carnitine Acyltransferases. *Citrate (si)-Synthase. *Diacylglycerol O-Acyltransferase. *Glycerol-3-Phosphate O-Acyltransferase ...
Fold c.43: CoA-dependent acyltransferases [52776] (1 superfamily). core: 2 layers, a/b; mixed beta-sheet of 6 strands, order ... PDB Compounds: (A:) Carnitine O-palmitoyltransferase 2. SCOPe Domain Sequences for d2rcua1:. Sequence; same for both SEQRES and ... Superfamily c.43.1: CoA-dependent acyltransferases [52777] (5 families) *. Family c.43.1.0: automated matches [191456] (1 ... PDB Description: crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-( ...
You are searching for: Acyltransferase T76369. Target Name. Liver carboxylesterase (CES1). Target Type. Successful Target ...
Carnitine Acyltransferases. *Citrate (si)-Synthase. *Diacylglycerol O-Acyltransferase. *Glycerol-3-Phosphate O-Acyltransferase ... "Diacylglycerol O-Acyltransferase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Diacylglycerol O-Acyltransferase" by people in this website by ... Below are the most recent publications written about "Diacylglycerol O-Acyltransferase" by people in Profiles. ...
Choline/Carnitine o-acyltransferase hsa mmu rno Chondroitin N-acetylgalactosaminyltransferase hsa mmu rno ...
Bruce CR; Brolin C; Turner N; Cleasby M; van der Leij F; Cooney GJ; Kraegen EW, 2007, Overexpression of carnitine ... Xu Y; Du X; Turner N; Brown AJ; Yang H, 2019, Enhanced acyl-CoA:cholesterol acyltransferase activity increases cholesterol ... 2008, The role of mitochondrial alycerol-3-phosphate acyltransferase-1 in regluating lipid and glucose homeostasis in high-fat ... 2009, Overexpression of carnitine palmitoyltransferase-1 in skeletal muscle is sufficient to enhance fatty acid oxidation and ...
Carnitine Acyltransferases [D08.811.913.050.350] * Citrate (si)-Synthase [D08.811.913.050.368] * Diacylglycerol O- ... Acyltransferases [D08.811.913.050] * Acetyl-CoA C-Acyltransferase [D08.811.913.050.080] * Acetyltransferases [D08.811.913.050. ... Sphingosine Acyltransferase Registry Number. EC 2.3.1.24. Public MeSH Note. 2006; SPHINGOSINE N-ACYLTRANSFERASE was indexed ... 1-Acylglycerol-3-Phosphate O-Acyltransferase [D08.811.913.050.173] * 1-Acylglycerophosphocholine O-Acyltransferase [D08.811. ...
5B, PFOA upregulated hexose metabolism-related genes (fucosyltransferase 1 [FUT1], PDK4, and carnitine palmitoyltransferase 1A ... glycine-N-acyltransferase, aldehyde dehydrogenase 7A1, HNF4Α, carbamoyl phosphate synthetase 1, cystathionine beta-synthase, ... and carnitine palmitoyltransferase 1A; and down-regulated OMA1 zinc metallopeptidase, aldolase B (ALDOB), ALDOC, lactate ... bile acid-CoA amino acid N-acyltransferase) and most genes in the second cluster, most of which were related to branched chain ...
Mouse CPT1A(Carnitine Palmitoyltransferase 1A, Liver) ELISA Kit. *Guinea pig SP(Substance P) ELISA Kit ... Mouse LPCAT1(Lysophosphatidylcholine Acyltransferase 1) ELISA Kit. *Mouse LPCAT2(Lysophosphatidylcholine Acyltransferase 2) ... Mouse LPCAT3(Lysophosphatidylcholine Acyltransferase 3) ELISA Kit. *Mouse LPCAT4(Lysophosphatidylcholine Acyltransferase 4) ... Mouse Lysophosphatidylcholine Acyltransferase 3 (LPCAT3) ELISA Kit. SEG531Mu-10x96wellstestplate Cloud-Clone 10x96-wells test ...
Article 쥐 간의 마이크로소옴에서 분리한 Medium-Chain/Long-Chain Carnitine Acyltransferase의 특성에 관한 연구 Loran L. Bieber 1992-12 ...
  • Adipose triglyceride lipase (ATGL), peroxisome proliferator-activated receptor γ (PPARγ), sterol regulatory element-binding protein 1 (SREBP1), diacylglycerol O-acyltransferase 1 (DGAT1) and 2 were decreased by vimentin treatment. (e-dmj.org)
  • Carnitine can buffer the acylation state of the CoA pool for any type of acyl group that is a substrate for the carnitine acyltransferase family of enzymes. (st-andrews.ac.uk)
  • As may be expected from members of the same enzymatic family, there is strong similarity between the structures of carnitine acetyltransferase (CRAT) and CROT, as these enzymes have 36% sequence homology. (wikipedia.org)
  • This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. (wikipedia.org)
  • The role of carnitine via the action of carnitine acyltransferase in buffering CoA availability in the mitochondrial matrix is well known. (st-andrews.ac.uk)
  • Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase. (wikipedia.org)
  • Carnitine O-octanoyltransferase (CROT or COT) is a member of the transferase family, more specifically a carnitine acyltransferase, a type of enzyme which catalyzes the transfer of acyl groups from acyl-CoAs to carnitine, generating CoA and an acyl-carnitine. (wikipedia.org)
  • EC 2.3.1.137) The systematic name of this enzyme is octanoyl-CoA:L-carnitine O-octanoyltransferase. (wikipedia.org)
  • Specifically, CROT catalyzes the chemical reaction: octanoyl-CoA + L-carnitine ⇌ {\displaystyle \rightleftharpoons } CoA + L-octanoylcarnitine Thus, the two substrates of this enzyme are octanoyl-CoA and L-carnitine and its two products are CoA and L-octanoylcarnitine. (wikipedia.org)
  • Interestingly, the trend for a related enzyme, carnitine palmitoyl transferase (CPT), the opposite trend was found. (wikipedia.org)
  • An enzyme that catalyzes the acyltransferase of SPHINGOSINE to N-acylsphingosine using acyl-COENZYME A as donor and COENZYME A as acceptor. (nih.gov)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Lysophosphatidylcholine Acyltransferase 4 (LPCAT4) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids. (myelisakit.com)
  • Specific carnitine acyltransferases in each organelle or membrane can modulate the reserves of free CoA and acyl-CoA in ways specific to the local metabolic demands. (st-andrews.ac.uk)
  • Exogenous LCACs, especially palmitoyl-carnitine and stearoyl-carnitine, inhibited iNKT cell expansion and promoted senescence. (bvsalud.org)
  • Description: A sandwich ELISA kit for detection of Lysophosphatidylcholine Acyltransferase 4 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (myelisakit.com)
  • High-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) and next-generation sequencing (NGS) were used to detect the concentrations of carnitine in the blood spots and for diagnosis. (bvsalud.org)
  • 15. Inhibition of carnitine palmitoyl transferase 1A-induced fatty acid oxidation suppresses cell progression in gastric cancer. (nih.gov)
  • Integrated transcriptome and metabolome network analysis showed 2 major gene-metabolite clusters, 1 centered on the transcript for the bidirectional glucose transporter 2 (Glut2) and the other centered on the transcripts for carnitine-palmitoyl transferase 2 (Cpt2) and acetyl-CoA acyltransferase (Acaa1). (nih.gov)
  • The CPT1A gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver. (medlineplus.gov)
  • Carnitine palmitoyltransferase 1A connects carnitine to long-chain fatty acids so they can cross the inner membrane of mitochondria. (medlineplus.gov)
  • Most of these mutations change single protein building blocks (amino acids) within carnitine palmitoyltransferase 1A. (medlineplus.gov)
  • Akkaoui M, Cohen I, Esnous C, Lenoir V, Sournac M, Girard J, Prip-Buus C. Modulation of the hepatic malonyl-CoA-carnitine palmitoyltransferase 1A partnership creates a metabolic switch allowing oxidation of de novo fatty acids. (medlineplus.gov)
  • Carnitine Palmitoyltransferase 1A Deficiency. (medlineplus.gov)
  • 14. Carnitine palmitoyltransferase 1A functions to repress FoxO transcription factors to allow cell cycle progression in ovarian cancer. (nih.gov)
  • The protection of free CoA pools in disease states is achieved by excretion of acyl-carnitine so that carnitine supplementation is required where unwanted acyl groups build up, such as in some inherited disorders of fatty acid oxidation. (nih.gov)
  • Recent evidence for sequestered pools of activated acetate for synthesis of malonyl-CoA, for the synthesis of polyunsaturated fatty acids and for the inhibition of carnitine palmitoyltransferase 1 to regulate fatty acid oxidation is reviewed. (nih.gov)
  • Supports fat burning by increasing carnitine biosynthesis (molecule required for mitochondrial fatty acid oxidation) (97,98). (gmawarriorsupplements.com)
  • 9. Carnitine-acyltransferase system inhibition, cancer cell death, and prevention of myc-induced lymphomagenesis. (nih.gov)
  • A group of fats called long-chain fatty acids cannot enter mitochondria unless they are attached to a substance known as carnitine. (medlineplus.gov)
  • Without enough of this enzyme, carnitine is not attached to long-chain fatty acids. (medlineplus.gov)
  • Together with carnitine palmitoyltransferase I, the encoded protein oxidizes long-chain fatty acids in the mitochondria. (nih.gov)
  • Once these fatty acids are inside mitochondria, carnitine is removed and they can be metabolized to produce energy. (medlineplus.gov)
  • Carnitine acyltransferase (CAT) transports free fatty acids into the mitochondria and therefore regulates their entry into the oxidative pathway. (medscape.com)
  • Acetyl CoA is further converted into malonyl CoA, a compound that may block the actions of carnitine acyltransferase in shuttling fatty acids into the mitochondria to be burned (and cause HCA to promote fat burning). (bodybuilding-wizard.com)
  • Catalysis of the transfer of an acyl group to an oxygen atom on the carnitine molecule. (systemsbiology.net)
  • Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. (bvsalud.org)
  • This and transfer of the activated acyl moieties between cell compartments without wasting energy on futile cycles of hydrolysis and resynthesis is achieved through the carnitine system. (nih.gov)
  • The therapeutic effects of carnitine and its esters are discussed in relation to the integrative influence of the carnitine system across CoA pools. (nih.gov)