Carnitine
Carnitine O-Acetyltransferase
Acetyltransferases
Carnitine O-Palmitoyltransferase
Carnitine Acyltransferases
Histone Acetyltransferases
Choline O-Acetyltransferase
Chloramphenicol O-Acetyltransferase
Acetylcarnitine
p300-CBP Transcription Factors
Malonyl Coenzyme A
gamma-Butyrobetaine Dioxygenase
Organic Cation Transport Proteins
Serine O-Acetyltransferase
Molecular Sequence Data
N-Terminal Acetyltransferase A
N-Terminal Acetyltransferase E
Acetyl Coenzyme A
Acyltransferases
Palmitoyl Coenzyme A
Palmitoylcarnitine
Dihydrolipoyllysine-Residue Acetyltransferase
Promoter Regions, Genetic
Base Sequence
Escherichia coli O157
Transcription, Genetic
Acyl Coenzyme A
Betaine
Amino Acid Sequence
Histones
Mitochondria, Liver
Liver
Plasmids
Pyruvate Dehydrogenase Complex
CREB-Binding Protein
Transfection
Saccharomyces cerevisiae Proteins
Gene Expression Regulation
Transcription Factors
Cloning, Molecular
Fatty Acids
O(6)-Methylguanine-DNA Methyltransferase
E1A-Associated p300 Protein
RNA, Messenger
Vitamin B Deficiency
N-Terminal Acetyltransferases
N-Terminal Acetyltransferase B
Epoxy Compounds
Spermine
Binding Sites
Ketone Bodies
Nuclear Proteins
Oxidation-Reduction
Vesicular Acetylcholine Transport Proteins
Gene Expression Regulation, Enzymologic
Transcriptional Activation
Regulatory Sequences, Nucleic Acid
Spermidine
Mutation
Choline
DNA-Binding Proteins
Protein Binding
Substrate Specificity
Restriction Mapping
Cysteine Synthase
Rats, Inbred Strains
Microbodies
Recombinant Fusion Proteins
Trans-Activators
Acetyl-CoA C-Acetyltransferase
Saccharomyces cerevisiae
Sequence Homology, Amino Acid
3-Hydroxybutyric Acid
Chromatin
Enhancer Elements, Genetic
Cells, Cultured
Lipid Metabolism, Inborn Errors
Reye Syndrome
Escherichia coli
HeLa Cells
DNA
Acetylcholinesterase
Chloramphenicol Resistance
Anacardic Acids
Clofibrate
Genes, Reporter
Glucosamine 6-Phosphate N-Acetyltransferase
Gene Expression
Myocardium
Protein Structure, Tertiary
Genes, Regulator
Carrier Proteins
Mitochondria
Tumor Cells, Cultured
Chloramphenicol
Mutagenesis, Site-Directed
Hyperammonemia
Platelet Activating Factor
Enzyme Induction
Histone Deacetylases
DNA Primers
Amino-Acid N-Acetyltransferase
Biological Transport
Genes
Mersalyl
Caprylates
Mitochondria, Muscle
Oxygen Consumption
Biogenic Polyamines
Lipid Metabolism
DNA, Complementary
Cell Nucleus
Isoenzymes
Blotting, Western
Blotting, Northern
Tissue Distribution
Nucleosomes
Sequence Alignment
Cell Cycle Proteins
Acyl-CoA Dehydrogenase
Substantia Innominata
Putrescine
Cattle
Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. (1/91)
The activities of beta-oxidation enzymes were measured in extracts of glucose- and triolein-grown cells of Aspergillus niger. Growth on triolein stimulated increased enzyme activity, especially for acyl-CoA dehydrogenase. No acyl-CoA oxidase activity was detected. HPLC analysis after incubation of triolein-grown cell extracts with decanoyl-CoA showed that beta-oxidation was limited to one cycle. Octanoyl-CoA accumulated as the decanoyl-CoA was oxidized. Beta-oxidation enzymes in isolated mitochondrial fractions were also studied. The results are discussed in the context of methyl ketone production by fungi. (+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. (2/91)
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)Pea chloroplast carnitine acetyltransferase. (3/91)
The purpose of this study was to resolve the controversy as to whether or not chloroplasts possess the enzyme carnitine acetyltransferase (CAT) and whether the activity of this enzyme is sufficient to support previously reported rates of fatty acid synthesis from acetylcarnitine. CAT catalyses the freely reversible reaction: carnitine + short-chain acylCoA <--> short-chain acylcarnitine + CoASH. CAT activity was detected in thc chloroplasts of Pisum sativum L. With membrane-impermeable acetyl CoA as a substrate. activity was only detected in ruptured chloroplasts and not with intact chloroplasts, indicating that the enzyme was located on the stromal side of the envelope. In crude preparations, CAT could only be detected using a sensitive radioenzymatic assay due to competing reactions from other enzymes using acetyl CoA and large amounts of ultraviolet-absorbing materials. After partial purification of the enzyme, CAT was detected in both the forward and reverse directions using spectrophotometric assays. Rates of 100 nmol of product formed per minute per milligram of protein were obtained, which is sufficient to support reported fatty acid synthesis rates from acetylcarnitine. Chloroplastic CAT showed optimal activity at pH 8.5 and had a high substrate specificity, handling C2-C4 acyl CoAs only. We believe that CAT has been satisfactorily demonstrated in pea chloroplasts. (+info)Evidence that the rate-limiting step for the biosynthesis of arachidonic acid in Mortierella alpina is at the level of the 18:3 to 20:3 elongase. (4/91)
Mortierella alpina, a fungus used commercially as a source of arachidonic acid, 20:4(n-6), has been examined to see if growth on lipid-based carbon sources leads to repression of either fatty acid biosynthesis and/or fatty acid desaturation and elongation. Changes in the activities of ATP:citrate lyase, isocitrate lyase, carnitine acetyltransferase, malic enzyme, glucose-6-phosphate dehydrogenase and pyruvate kinase when the fungus was grown on fatty-acid-based (Tween) carbon sources were consistent with (i) the cells using the fatty acyl portion of the substrate as the sole carbon source, (ii) pyruvate kinase being the source of pyruvate for biosynthesis under these conditions and (iii) malic enzyme's major function being as a provider of NADPH for lipid biosynthesis. The abolition of fatty acid synthase activity when cells were grown on Tweens indicated the cessation of de novo fatty acid biosynthesis under these conditions. The fatty acyl composition of the lipid accumulated by the fungus grown on Tweens 20, 40 and 80 showed that desaturation and elongation of the substrate lipid still occurred. The absolute amount of arachidonic acid synthesized by Tween-grown cells was the same as for cells grown on glucose. The transformation of incorporated fatty acids into 20:4(n-6) was, it appeared, limited at the elongation of 18:3(n-6) to 20:3(n-6) as, in every case, 18:1, 18:2 and 18:3(n-6) increased in amount in the Tween-grown cells. These data show for the first time that fatty acid synthesis is regulated separately from fatty acid desaturation/elongation and that the latter reactions are not repressed by growth of the fungus on simple fatty acids. Furthermore, the data strongly implicate the elongation of 18:3(n-6) to 20:3(n-6) as the limiting step in arachidonic acid biosynthesis by Mort. alpina. (+info)Hormonal control of ketogenesis. Rapid activation of hepatic ketogenic capacity in fed rats by anti-insulin serum and glucagon. (5/91)
The enhanced capacity for long-chain fatty acid oxidation and ketogenesis that develops in the rat liver between 6 and 9 h after the onset of starvation was shown to be inducible much more rapidly by administration of anti-insulin serum or glucagon to fed rats. After only 1 h of treatment with either agent, the liver had clearly switched from a "nonketogenic" to a "ketogenic" profile, as determined by rates of acetoacetate and b-hydroxybutyrate production on perfusion with oleic acid. As was the case after starvation, the administration of insulin antibodies or glucagon resulted in depletion of hepatic glycogen stores and a proportional increase in the ability of the liver to oxidize long-chain fatty acids and (-)-octanoylcarnitine, suggesting that all three treatment schedules activated the carnitine acyltransferase system of enzymes. In contrast to anti-insulin serum, which produced marked elevations in plasma glucose, free fatty acid, and ketone body concentrations, glucagon treatment had little effect on any of these parameters, presumably due to enhanced insulin secretion after the initial stimulation of glycogenolysis. Thus, after treatment with glucagon alone, it was possible to obtain a "ketogenic" liver from a nonketotic animal. The results are consistent with the possibility that the activity of carnitine acyltransferase, and thus ketogenic capacity, is subject to bihormonal control through the relative blood concentrations of insulin and glucagon, as also appears to be the case with hepatic carbohydrate metabolism. (+info)Age-associated mitochondrial oxidative decay: improvement of carnitine acetyltransferase substrate-binding affinity and activity in brain by feeding old rats acetyl-L- carnitine and/or R-alpha -lipoic acid. (6/91)
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 CAT were analyzed by using the brains of young and old rats and of old rats supplemented for 7 weeks with the CAT substrate acetyl-l-carnitine (ALCAR) and/or the mitochondrial antioxidant precursor R-alpha-lipoic acid (LA). Old rats, compared with young rats, showed a decrease in CAT activity and in CAT-binding affinity for both substrates, ALCAR and CoA. Feeding ALCAR or ALCAR plus LA to old rats significantly restored CAT-binding affinity for ALCAR and CoA, and CAT activity. To explore the underlying mechanism, lipid peroxidation and total iron and copper levels were assayed; all increased in old rats. Feeding old rats LA or LA plus ALCAR inhibited lipid peroxidation but did not decrease iron and copper levels. Ex vivo oxidation of young-rat brain with Fe(II) caused loss of CAT activity and binding affinity. In vitro oxidation of purified CAT with Fe(II) inactivated the enzyme but did not alter binding affinity. However, in vitro treatment of CAT with the lipid peroxidation products malondialdehyde or 4-hydroxy-nonenal caused a decrease in CAT-binding affinity and activity, thus mimicking age-related change. Preincubation of CAT with ALCAR or CoA prevented malondialdehyde-induced dysfunction. Thus, feeding old rats high levels of key mitochondrial metabolites can ameliorate oxidative damage, enzyme activity, substrate-binding affinity, and mitochondrial dysfunction. (+info)Acetyl-coenzyme A hydrolase, an artifact? The conversion of acetyl-coenzyme A into acetate by the combined action of carnitine acetyltransferase and acetylcarnitine hydrolase. (7/91)
1. The nature of the acetyl-CoA hydrolase (EC 3.1.2.1) reaction in rat and sheep liver homogenates was investigated. 2. The activity determined in an incubated system was 5.10 and 3.28nmol/min per mg of protein for rat and sheep liver homogenate respectively. This activity was not affected by the addition of l-carnitine, but was decreased by the addition of d-carnitine. 3. No acetyl-CoA hydrolase activity could be detected in rat or sheep liver homogenates first treated with Sephadex G-25. This treatment decreased the carnitine concentrations of the homogenates to about one-twentieth. Subsequent addition of l-carnitine, but not d-carnitine, restored the apparent acetyl-CoA hydrolase activity. 4. Sephadex treatment did not affect acetyl-carnitine hydrolase activity of the homogenates, which was 5.8 and 8.1nmol/min per mg of protein respectively for rat and sheep liver. 5. Direct spectrophotometric assay of acetyl-CoA hydrolase, based on the reaction of CoA released with 5,5'-dithiobis-(2-nitrobenzoic acid), clearly demonstrated that after Sephadex treatment no activity could be measured. 6. Carnitine acetyltransferase (EC 2.3.1.7) activity measured in the same assay system in response to added l-carnitine was very low in normal rat liver homogenates, owing to the apparent high acetyl-CoA hydrolase activity, but was increased markedly after Sephadex treatment. The V(max.) for this enzyme in rat liver homogenates was increased from 3.4 to 14.8nmol/min per mg of protein whereas the K(m) for l-carnitine was decreased from 936 to 32mum after Sephadex treatment. 7. Acetyl-CoA hydrolase activity could be demonstrated in disrupted rat liver mitochondria but not in separated outer or inner mitochondrial membrane fractions. Activity could be demonstrated after recombination of outer and inner mitochondrial membrane fractions. The outer mitochondrial membrane fraction showed acetylcarnitine hydrolase activity and the inner mitochondrial membrane fraction showed carnitine acetyltransferase activity. 8. The results presented here demonstrate that acetyl-CoA hydrolase activity in rat and sheep liver is an artifact and the activity is due to the combined activity of carnitine acetyltransferase and acetylcarnitine hydrolase. (+info)Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. (8/91)
Carnitine acyltransferases have crucial roles in the transport of fatty acids for beta-oxidation. Dysregulation of these enzymes can lead to serious diseases in humans, and they are targets for therapeutic development against diabetes. We report the crystal structures of murine carnitine acetyltransferase (CRAT), alone and in complex with its substrate carnitine or CoA. The structure contains two domains. Surprisingly, these two domains share the same backbone fold, which is also similar to that of chloramphenicol acetyltransferase and dihydrolipoyl transacetylase. The active site is located at the interface between the two domains. Carnitine and CoA are bound in deep channels in the enzyme, on opposite sides of the catalytic His343 residue. The structural information provides a molecular basis for understanding the catalysis by carnitine acyltransferases and for designing their inhibitors. Specifically, our structural information suggests that the substrate carnitine may assist the catalysis by stabilizing the oxyanion in the reaction intermediate. (+info)1. Vitamin B1 (Thiamine): necessary for converting carbohydrates into energy
2. Vitamin B2 (Riboflavin): important for vision health and immune system function
3. Vitamin B3 (Niacin): crucial for energy production and skin health
4. Vitamin B5 (Pantothenic acid): involved in energy production, hormone production, and blood cell formation
5. Vitamin B6: essential for brain function, immune system function, and the synthesis of neurotransmitters
6. Vitamin B7 (Biotin): important for hair, skin, and nail health, as well as energy production
7. Vitamin B9 (Folic acid): crucial for fetal development during pregnancy
8. Vitamin B12: necessary for the production of red blood cells, nerve function, and DNA synthesis.
Vitamin B deficiencies can occur due to several factors, including:
* Poor diet or malnutrition
* Gastrointestinal disorders that impair nutrient absorption (e.g., celiac disease, Crohn's disease)
* Increased demand for vitamins during pregnancy and lactation
* Certain medications (e.g., antacids, proton pump inhibitors) that interfere with nutrient absorption
* Malabsorption due to pancreas or small intestine disorders
* Inherited disorders (e.g., vitamin B12 deficiency due to pernicious anemia)
Symptoms of vitamin B deficiencies can vary depending on the specific vitamin and the severity of the deficiency. Some common symptoms include fatigue, weakness, irritability, depression, skin problems, and impaired cognitive function. Treatment typically involves dietary modifications and supplementation with the appropriate vitamin. In severe cases, hospitalization may be necessary to address any underlying conditions or complications.
The following are some of the most common vitamin B deficiencies:
1. Vitamin B12 deficiency: This is one of the most common vitamin B deficiencies and can cause fatigue, weakness, pale skin, and neurological problems such as numbness or tingling in the hands and feet.
2. Vitamin B6 deficiency: This can cause skin problems, such as acne-like rashes, and neurological symptoms like confusion, convulsions, and weakness in the arms and legs.
3. Folate deficiency: This can cause fatigue, weakness, pale skin, and neurological problems such as memory loss and confusion.
4. Vitamin B2 (riboflavin) deficiency: This can cause cracked lips, skin around the mouth, and tongue, and eyes.
5. Niacin (vitamin B3) deficiency: This can cause pellagra, a condition characterized by diarrhea, dermatitis, and dementia.
6. Vitamin B5 (pantothenic acid) deficiency: This can cause fatigue, weakness, and neurological symptoms like headaches and dizziness.
7. Vitamin B1 (thiamine) deficiency: This can cause beriberi, a condition characterized by weakness, fatigue, and neurological problems such as confusion and memory loss.
8. Biotin deficiency: This is rare but can cause skin problems, such as seborrhea, and neurological symptoms like numbness and tingling in the hands and feet.
9. Vitamin B12 (cobalamin) deficiency: This is common in vegetarians and vegans who do not consume enough animal products, and can cause fatigue, weakness, and neurological problems such as numbness and tingling in the hands and feet.
It's important to note that these deficiencies can have a significant impact on your overall health and well-being, so it's essential to be aware of the signs and symptoms and take steps to ensure you are getting enough of these vitamins in your diet.
Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.
Types of Starvation:
There are several types of starvation, each with different causes and effects. These include:
1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.
Effects of Starvation on the Body:
Starvation can have severe effects on the body, including:
1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.
It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.
There are several types of inborn errors of lipid metabolism, each with its own unique set of symptoms and characteristics. Some of the most common include:
* Familial hypercholesterolemia: A condition that causes high levels of low-density lipoprotein (LDL) cholesterol in the blood, which can lead to heart disease and other health problems.
* Fabry disease: A rare genetic disorder that affects the body's ability to break down certain fats, leading to a buildup of toxic substances in the body.
* Gaucher disease: Another rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.
* Lipoid cerebral degeneration: A condition that causes fatty deposits to accumulate in the brain, leading to cognitive decline and other neurological problems.
* Tangier disease: A rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.
Inborn errors of lipid metabolism can be diagnosed through a variety of tests, including blood tests and genetic analysis. Treatment options vary depending on the specific disorder and its severity, but may include dietary changes, medication, and other therapies. With proper treatment and management, many individuals with inborn errors of lipid metabolism can lead active and fulfilling lives.
Symptoms of Reye Syndrome can include:
* Headache
* Confusion
* Vomiting
* Seizures
* Loss of consciousness
* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Abdominal pain
If you suspect that your child may have Reye Syndrome, it is important to seek medical attention immediately. The condition can be difficult to diagnose, as it can resemble other conditions such as meningitis or encephalitis. A healthcare provider will typically perform a physical examination, take a medical history, and order laboratory tests to confirm the diagnosis.
There is no specific treatment for Reye Syndrome, but the condition is usually managed with supportive care in a hospital setting. Treatment may include:
* Medication to control seizures
* Intravenous fluids and nutrition
* Monitoring of vital signs and liver function
* Antiviral medication in some cases
Reye Syndrome can be fatal if left untreated, so early diagnosis and aggressive management are crucial. The condition is rare, but it is important for parents and healthcare providers to be aware of the signs and symptoms in order to provide prompt and appropriate care.
Causes of Hyperammonemia:
1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.
Symptoms of Hyperammonemia:
1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting
Diagnosis of Hyperammonemia:
1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.
Treatment of Hyperammonemia:
1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.
Complications of Hyperammonemia:
1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.
In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.
Carnitine O-acetyltransferase
Gamma-butyrobetaine dioxygenase
Meldonium
Carnitine palmitoyltransferase II deficiency
Carnitine palmitoyltransferase I
Carnitine O-palmitoyltransferase
Beta-Hydroxybutyric acid
CATC
Inner mitochondrial membrane
Leucine
List of EC numbers (EC 2)
List of MeSH codes (D08)
Beta-Hydroxy beta-methylbutyryl-CoA
CAT I
CAT II
CDP-choline pathway
Transferase
Acetyl group
Chromosome 11
Choline
List of enzymes
List of EC numbers (EC 4)
List of EC numbers (EC 1)
Amphetamine
Methamphetamine
Epigenetics of neurodegenerative diseases
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Carnitine acetyltransferase activity in oleaginous yeasts - Nuffield Department of Medicine
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Choline acetyltransferase2
- The urothelium of various species has been shown to express choline acetyltransferase (ChAT) and/or carnitine acetyltransferase (CarAT), enzymes that synthesize the neurotransmitter acetylcholine (Ach) [5], [6]. (bioerc-iend.org)
- gene provides instructions for making a protein called choline acetyltransferase. (nih.gov)
Mitochondrial5
- Acetyl-L-carnitine is a mitochondrial metabolite that facilitates the movement of fatty acids into the mitochondria for energy and is also used to generate acetyl coenzyme A. '-Lipoic acid is a coenzyme involved in mitochondrial ATP production and its reduced form can recycle other antioxidants. (nih.gov)
- This decay, a major contributor to aging, can be ameliorated by feeding old rats the normal mitochondrial metabolites acetyl carnitine (ALCAR) and lipoic acid (LA) at high levels. (nih.gov)
- TGF-β1 attenuates mitochondrial bioenergetics in pulmonary arterial endothelial cells via the disruption of carnitine homeostasis. (nih.gov)
- TGF-β1 induced mitochondrial dysfunction was linked to a nitration-mediated activation of Akt1 and the subsequent mitochondrial translocation of endothelial NO synthase (eNOS) resulting in the nitration of carnitine acetyl transferase (CrAT) and the disruption of carnitine homeostasis. (nih.gov)
- shunt), we have recently shown a disruption in carnitine homeostasis, associated with mitochondrial dysfunction and decreased endothelial nitric oxide synthase (eNOS)/heat shock protein (Hsp)90 interactions that contribute to eNOS uncoupling, increased superoxide levels, and decreased bioavailable nitric oxide (NO). Therefore, we undertook this study to test the hypothesis that L-carnitine therapy would maintain mitochondrial function and NO signaling. (arizona.edu)
Transferase1
- These changes correlated with increased carnitine acetyl transferase (CrAT) protein and enzyme activity and decreased levels of nitrated CrAT. (arizona.edu)
Lipoic acid6
- Thus, acetyl carnitine/'-lipoic acid dietary supplements have a potential market of tens of millions of middle-aged and elderly Americans who desire to improve their general health. (nih.gov)
- Virtually no information on the potential toxicity of acetyl-L-carnitine/'-lipoic acid combinations was found in the available literature. (nih.gov)
- Approximately one year following the presentation of acetyl-L-carnitine/'-lipoic acid at the CSWG meeting on July 1, 2003, a search of PubMed was conducted to identify new published information. (nih.gov)
- Although no new studies of acetyl-L-carnitine/'-lipoic acid combinations were identified in the literature search, several studies describing protective effects for lipoic acid were published in the last year. (nih.gov)
- Oxidation: Partial Reversal by Feeding Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
- Improvement of Carnitine Acetyltransferase Substrate Binding Affinity and Activity in Brain by Feeding Old Rats Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
Protein1
- Together with carnitine palmitoyltransferase I, the encoded protein oxidizes long-chain fatty acids in the mitochondria. (nih.gov)
Acetylcarnitine1
- An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. (nih.gov)
Gene1
- 7. The leucine twenty homeobox (LEUTX) gene, which lacks a histone acetyltransferase domain, is fused to KAT6A in therapy-related acute myeloid leukemia with t(8;19)(p11;q13). (nih.gov)
Endothelial1
- Conclusion: L-Carnitine therapy may improve the endothelial dysfunction noted in children with CHDs and has important clinical implications that warrant further investigation. (arizona.edu)
Pulmonary1
- Furthermore, acetylcholine significantly decreased left pulmonary vascular resistance only in L-carnitine-treated lambs. (arizona.edu)
Activity1
- In this formulation, acetyl-L-carnitine hydrochloride is thought to increase general metabolic activity and to improve cognitive function. (nih.gov)
Treatment1
- Immediately after delivery, lambs received daily treatment with oral L-carnitine or its vehicle. (arizona.edu)
Levels1
- Results: L-Carnitine-treated lambs had decreased levels of acylcarnitine and a reduced acylcarnitine:free carnitine ratio as compared with vehicle-treated shunt lambs. (arizona.edu)
Acetyl-L-carniti8
- In this formulation, acetyl-L-carnitine hydrochloride is thought to increase general metabolic activity and to improve cognitive function. (nih.gov)
- Acetyl-L-carnitine is a mitochondrial metabolite that facilitates the movement of fatty acids into the mitochondria for energy and is also used to generate acetyl coenzyme A. '-Lipoic acid is a coenzyme involved in mitochondrial ATP production and its reduced form can recycle other antioxidants. (nih.gov)
- Virtually no information on the potential toxicity of acetyl-L-carnitine/'-lipoic acid combinations was found in the available literature. (nih.gov)
- Approximately one year following the presentation of acetyl-L-carnitine/'-lipoic acid at the CSWG meeting on July 1, 2003, a search of PubMed was conducted to identify new published information. (nih.gov)
- Although no new studies of acetyl-L-carnitine/'-lipoic acid combinations were identified in the literature search, several studies describing protective effects for lipoic acid were published in the last year. (nih.gov)
- A report indicating that acetyl-L-carnitine had beneficial effects in animal models of Parkinson's disease (Beal, 2004). (nih.gov)
- Oxidation: Partial Reversal by Feeding Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
- Improvement of Carnitine Acetyltransferase Substrate Binding Affinity and Activity in Brain by Feeding Old Rats Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
Organic cation1
- 10. Oxaliplatin transport mediated by organic cation/carnitine transporters OCTN1 and OCTN2 in overexpressing human embryonic kidney 293 cells and rat dorsal root ganglion neurons. (nih.gov)
Oxidation1
- L-Carnitine Improves Skeletal Muscle Fat Oxidation in Primary Carnitine Deficiency. (nih.gov)
Enzyme1
- An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. (nih.gov)
Human1
- 12. Combination effects of platinum drugs and N1, N11 diethylnorspermine on spermidine/spermine N1-acetyltransferase, polyamines and growth inhibition in A2780 human ovarian carcinoma cells and their oxaliplatin and cisplatin-resistant variants. (nih.gov)
Effects1
- The effects of adjunctive treatment with L-carnitine on monitoring laboratory variables in ICU patients: a double-blinded randomized controlled clinical trial. (nih.gov)