An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor.
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
An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC
A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.
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.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
The state of being deprived of sleep under experimental conditions, due to life events, or from a wide variety of pathophysiologic causes such as medication effect, chronic illness, psychiatric illness, or sleep disorder.
Clinical or subclinical disturbances of cortical function due to a sudden, abnormal, excessive, and disorganized discharge of brain cells. Clinical manifestations include abnormal motor, sensory and psychic phenomena. Recurrent seizures are usually referred to as EPILEPSY or "seizure disorder."
Solid dosage forms, of varying weight, size, and shape, which may be molded or compressed, and which contain a medicinal substance in pure or diluted form. (Dorland, 28th ed)
Recording of electric currents developed in the brain by means of electrodes applied to the scalp, to the surface of the brain, or placed within the substance of the brain.
A childhood seizure disorder characterized by rhythmic electrical brain discharges of generalized onset. Clinical features include a sudden cessation of ongoing activity usually without loss of postural tone. Rhythmic blinking of the eyelids or lip smacking frequently accompanies the SEIZURES. The usual duration is 5-10 seconds, and multiple episodes may occur daily. Juvenile absence epilepsy is characterized by the juvenile onset of absence seizures and an increased incidence of myoclonus and tonic-clonic seizures. (Menkes, Textbook of Child Neurology, 5th ed, p736)
Printed publications usually having a format with no binding and no cover and having fewer than some set number of pages. They are often devoted to a single subject.
A medical specialty concerned with the study of the structures, functions, and diseases of the nervous system.

The peroxisome proliferator (PP) response element upstream of the human acyl CoA oxidase gene is inactive among a sample human population: significance for species differences in response to PPs. (1/269)

Peroxisome proliferators (PP) cause peroxisome proliferation, associated with rodent hepatocyte growth perturbation and hepatocarcinogenesis. However, in humans this class of non-genotoxic carcinogens does not appear to have the same adverse effects. The peroxisome proliferator-activated receptor alpha (PPARalpha) mediates the effects of PPs in rodents via peroxisome proliferator response elements (PPREs) upstream of PP-responsive genes such as acyl coenzyme A oxidase (ACO). When the human ACO promoter was cloned previously, it was found to be active and to contain a consensus PPRE (-1918 AGGTCA C TGGTCA -1906). To confirm and extend those original findings, we isolated a 2 kb genomic fragment of the ACO gene promoter from a human liver biopsy and used it to create a beta-galactosidase reporter gene plasmid. The human ACO promoter reporter plasmid was added to both Hepalclc7 and NIH 3T3 cells together with a plasmid expressing mPPARa and assessed for its ability to drive PP-mediated gene transcription. The human ACO promoter fragment was inactive, unlike the equivalent rat ACO promoter fragment used as a positive control. The PPRE within our cloned fragment of the human ACO promoter differed at three positions (5'-AGGTCA G CTGTCA-3') from the previously published active human ACO promoter. Next, we studied the frequency of the inactive versus the active human PPRE within the human population. Using a PCR strategy, we isolated and analysed genomic DNA fragments from 22 unrelated human individuals and from the human hepatoma cell line HepG2. In each case, the PPRE contained the inactive sequence. These data show that the human ACO gene promoter found in a sample human population is inactive. This may explain at the genomic level the lack of response of humans to some of the adverse effects of the PP class of non-genotoxic hepatocarcinogens.  (+info)

Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. (2/269)

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)

Beneficial effects of fibrates on apolipoprotein A-I metabolism occur independently of any peroxisome proliferative response. (3/269)

BACKGROUND: In humans, fibrates are frequently used normolipidemic drugs. Fibrates act by regulating genes involved in lipoprotein metabolism via activation of the peroxisome proliferator-activated receptor-alpha (PPARalpha) in liver. In rodents, however, fibrates induce a peroxisome proliferation, leading to hepatomegaly and possibly hepatocarcinogenesis. Although this peroxisome proliferative response appears not to occur in humans, it remains controversial whether the beneficial effects of fibrates on lipoprotein metabolism can occur dissociated from such undesirable peroxisomal response. Here, we assessed the influence of fenofibrate on lipoprotein metabolism and peroxisome proliferation in the rabbit, an animal that, contrary to rodents and similar to humans, is less sensitive to peroxisome proliferators. METHODS AND RESULTS: First, we demonstrate that in normal rabbits, fenofibrate given at a high dose for 2 weeks does not influence serum concentrations or intestinal mRNA levels of the HDL apolipoprotein apoA-I. Therefore, the study was continued with human apoA-I transgenic rabbits that overexpress the human apoA-I gene under control of its homologous promoter, including its PPAR-response elements. In these animals, fenofibrate increases serum human apoA-I concentrations via an increased expression of the human apoA-I gene in liver. Interestingly, liver weight or mRNA levels and activity of fatty acyl-CoA oxidase, a rate-limiting and marker enzyme of peroxisomal beta-oxidation, remain unchanged after fenofibrate. CONCLUSIONS: Expression of the human apoA-I transgene in rabbit liver suffices to confer fibrate-mediated induction of serum apoA-I. Furthermore, these data provide in vivo evidence that the beneficial effects of fibrates on lipoprotein metabolism occur mechanistically dissociated from any deleterious activity on peroxisome proliferation and possibly hepatocarcinogenesis.  (+info)

Absence of spontaneous peroxisome proliferation in enoyl-CoA Hydratase/L-3-hydroxyacyl-CoA dehydrogenase-deficient mouse liver. Further support for the role of fatty acyl CoA oxidase in PPARalpha ligand metabolism. (4/269)

Peroxisomes contain a classical L-hydroxy-specific peroxisome proliferator-inducible beta-oxidation system and also a second noninducible D-hydroxy-specific beta-oxidation system. We previously generated mice lacking fatty acyl-CoA oxidase (AOX), the first enzyme of the L-hydroxy-specific classical beta-oxidation system; these AOX-/- mice exhibited sustained activation of peroxisome proliferator-activated receptor alpha (PPARalpha), resulting in profound spontaneous peroxisome proliferation in liver cells. These observations implied that AOX is responsible for the metabolic degradation of PPARalpha ligands. In this study, the function of enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase (L-PBE), the second enzyme of this peroxisomal beta-oxidation system, was investigated by disrupting its gene. Mutant mice (L-PBE-/-) were viable and fertile and exhibited no detectable gross phenotypic defects. L-PBE-/- mice showed no hepatic steatosis and manifested no spontaneous peroxisome proliferation, unlike that encountered in livers of mice deficient in AOX. These results indicate that disruption of classical peroxisomal fatty acid beta-oxidation system distal to AOX step does not interfere with the inactivation of endogenous ligands of PPARalpha, further confirming that the AOX gene is indispensable for the physiological regulation of this receptor. The absence of appreciable changes in lipid metabolism also indicates that enoyl-CoAs, generated in the classical system in L-PBE-/- mice are diverted to D-hydroxy-specific system for metabolism by D-PBE. When challenged with a peroxisome proliferator, L-PBE-/- mice showed increases in the levels of hepatic mRNAs and proteins that are regulated by PPARalpha except for appreciable blunting of peroxisome proliferative response as compared with that observed in hepatocytes of wild type mice similarly treated. This blunting of peroxisome proliferative response is attributed to the absence of L-PBE protein in L-PBE-/- mouse liver, because all other proteins are induced essentially to the same extent in both wild type and L-PBE-/- mice.  (+info)

Activation of flavin-containing oxidases underlies light-induced production of H2O2 in mammalian cells. (5/269)

Violet-blue light is toxic to mammalian cells, and this toxicity has been linked with cellular production of H2O2. In this report, we show that violet-blue light, as well as UVA, stimulated H2O2 production in cultured mouse, monkey, and human cells. We found that H2O2 originated in peroxisomes and mitochondria, and it was enhanced in cells overexpressing flavin-containing oxidases. These results support the hypothesis that photoreduction of flavoproteins underlies light-induced production of H2O2 in cells. Because H2O2 and its metabolite, hydroxyl radicals, can cause cellular damage, these reactive oxygen species may contribute to pathologies associated with exposure to UVA, violet, and blue light. They may also contribute to phototoxicity often encountered during light microscopy. Because multiphoton excitation imaging with 1,047-nm wavelength prevented light-induced H2O2 production in cells, possibly by minimizing photoreduction of flavoproteins, this technique may be useful for decreasing phototoxicity during fluorescence microscopy.  (+info)

Impairment of peroxisomal biogenesis in human colon carcinoma. (6/269)

Peroxisomes and the activities of their enzymes have been reported to be significantly reduced in various types of tumors including the colon carcinoma. Therefore, the present study was designed to investigate the gene expression of several peroxisomal proteins in human colon carcinoma and additionally those of the peroxisome proliferator activated receptor alpha (PPARalpha) and PEX5, a receptor protein involved in the import of most peroxisomal matrix proteins. Samples from adenocarcinomas and adjacent normal colon were analyzed by immunohistochemistry and western blotting. The mRNA content was assessed by a novel sensitive dot blot RNase protection assay and northern blotting. By immunohistochemistry, peroxisomes were distinctly visualized in normal colonocytes but were not detected in colon carcinoma cells. The protein levels of catalase (CAT), acyl-CoA oxidase as well as the 22 and 70 kDa peroxisomal membrane proteins (PMP22 and PMP70) were all significantly decreased in carcinomas. The corresponding mRNAs for CAT and PMP70, however, were unchanged. In contrast, the mRNA of PEX5 was significantly increased. The expression of PPARalpha was not altered in tumors, neither at protein nor mRNA levels. These observations show that the reduction of peroxisomes and their proteins in colon carcinoma is not due to a generalized reduction of transcription of their genes. It seems more likely that this phenomenon is regulated at a post-transcriptional or translational level. Alternatively, and more likely, an impairment of the biogenesis of the organelle could account for the paucity of peroxisomes in colon carcinoma.  (+info)

Arachidonic acid and PGE2 regulation of hepatic lipogenic gene expression. (7/269)

N-6 polyunsaturated fatty acids (PUFA) suppress hepatic and adipocyte de novo lipogenesis by inhibiting the transcription of genes encoding key lipogenic proteins. In cultured 3T3-L1 adipocytes, arachidonic acid (20:4,n-6) suppression of lipogenic gene expression requires cyclooxygenase (COX) activity. In this study, we found no evidence to support a role for COX-1 or -2 in the 20:4,n-6 inhibition of hepatocyte lipogenic gene expression. In contrast to L1 preadipocytes, adipocytes and rat liver, RT-PCR and Western analyses did not detect COX-1 or COX-2 expression in cultured primary hepatocytes. Moreover, the COX inhibitor, flurbiprofen, did not affect the 20:4,n-6 regulation of lipogenic gene expression in primary hepatocytes. Despite the absence of COX-1 and -2 expression in primary hepatocytes, prostaglandins (PGE2 and PGF2alpha) suppressed fatty acid synthase, l-pyruvate kinase, and the S14 protein mRNA, while having no effect on acyl-CoA oxidase or CYP4A2 mRNA. Using PGE2 receptor agonist, the PGE2 effect on lipogenic gene expression was linked to EP3 receptors. PGE2 inhibited S14CAT activity in transfected primary hepatocytes and targeted the S14 PUFA-response region located -220 to -80 bp upstream from the transcription start site. Taken together, these studies show that COX-1 and COX-2 do not contribute to the n-6 PUFA suppression of hepatocyte lipogenic gene expression. However, cyclooxygenase products from non-parenchymal cells can act on parenchymal cells through a paracrine process and mimic the effects of n-6 PUFA on lipogenic gene expression.  (+info)

Novel form of lipolysis induced by leptin. (8/269)

Hyperleptinemia causes disappearance of body fat without a rise in free fatty acids (FFA) or ketones, suggesting that leptin can deplete adipocytes of fat without releasing FFA. To test this, we measured FFA and glycerol released from adipocytes obtained from normal lean Zucker diabetic fatty rats (+/+) and incubated for 0, 3, 6, or 24 h in either 20 ng/ml recombinant leptin or 100 nM norepinephrine (NE). Whereas NE increased both FFA and glycerol release from adipocytes of +/+ rats, leptin increased glycerol release in +/+ adipocytes without a parallel increase in FFA release. In adipocytes of obese Zucker diabetic fatty rats (fa/fa) with defective leptin receptors, NE increased both FFA and glycerol release, but leptin had no effect on either. Leptin significantly lowered the mRNA of leptin and fatty acid synthase of adipocytes (FAS) (p < 0.05), and up-regulated the mRNA of peroxisome proliferator-activated receptor (PPAR)-alpha, carnitine palmitoyl transferase-1, (CPT-1), and acyl CoA oxidase (ACO) (p < 0.05). NE (100 nM) also lowered leptin mRNA (p < 0.05) but did not affect FAS, PPARalpha, ACO, or CPT-1 expression. We conclude that in normal adipocytes leptin directly decreases FAS expression, increases PPARalpha and the enzymes of FFA oxidation, and stimulates a novel form of lipolysis in which glycerol is released without a proportional release of FFA.  (+info)

Acyl-CoA oxidase is an enzyme that plays a crucial role in the breakdown of fatty acids within the body. It is located in the peroxisomes, which are small organelles found in the cells of living organisms. The primary function of acyl-CoA oxidase is to catalyze the initial step in the beta-oxidation of fatty acids, a process that involves the sequential removal of two-carbon units from fatty acid molecules in the form of acetyl-CoA.

The reaction catalyzed by acyl-CoA oxidase is as follows:

acyl-CoA + FAD → trans-2,3-dehydroacyl-CoA + FADH2 + H+

In this reaction, the enzyme removes a hydrogen atom from the fatty acyl-CoA molecule and transfers it to its cofactor, flavin adenine dinucleotide (FAD). This results in the formation of trans-2,3-dehydroacyl-CoA, FADH2, and a proton. The FADH2 produced during this reaction can then be used to generate ATP through the electron transport chain, while the trans-2,3-dehydroacyl-CoA undergoes further reactions in the beta-oxidation pathway.

There are two main isoforms of acyl-CoA oxidase found in humans: ACOX1 and ACOX2. ACOX1 is primarily responsible for oxidizing straight-chain fatty acids, while ACOX2 specializes in the breakdown of branched-chain fatty acids. Mutations in the genes encoding these enzymes can lead to various metabolic disorders, such as peroxisomal biogenesis disorders and Refsum disease.

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.

Sterol O-Acyltransferase (SOAT, also known as ACAT for Acyl-CoA:cholesterol acyltransferase) is an enzyme that plays a crucial role in cholesterol homeostasis within cells. Specifically, it catalyzes the reaction of esterifying free cholesterol with fatty acyl-coenzyme A (fatty acyl-CoA) to form cholesteryl esters. This enzymatic activity allows for the intracellular storage of excess cholesterol in lipid droplets, reducing the levels of free cholesterol in the cell and thus preventing its potential toxic effects on membranes and proteins. There are two isoforms of SOAT, SOAT1 and SOAT2, which exhibit distinct subcellular localization and functions. Dysregulation of SOAT activity has been implicated in various pathological conditions, including atherosclerosis and neurodegenerative disorders.

NADPH oxidase is an enzyme complex that plays a crucial role in the production of reactive oxygen species (ROS) in various cell types. The primary function of NADPH oxidase is to catalyze the transfer of electrons from NADPH to molecular oxygen, resulting in the formation of superoxide radicals. This enzyme complex consists of several subunits, including two membrane-bound components (gp91phox and p22phox) and several cytosolic components (p47phox, p67phox, p40phox, and rac1 or rac2). Upon activation, these subunits assemble to form a functional enzyme complex that generates ROS, which serve as important signaling molecules in various cellular processes. However, excessive or uncontrolled production of ROS by NADPH oxidase has been implicated in the pathogenesis of several diseases, such as cardiovascular disorders, neurodegenerative diseases, and cancer.

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.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

Coenzyme A (CoA) ligases, also known as CoA synthetases, are a class of enzymes that activate acyl groups, such as fatty acids and amino acids, by forming a thioester bond with coenzyme A. This activation is an essential step in various metabolic pathways, including fatty acid oxidation, amino acid catabolism, and the synthesis of several important compounds like steroids and acetylcholine.

CoA ligases catalyze the following reaction:

acyl group + ATP + CoA ↔ acyl-CoA + AMP + PP~i~

In this reaction, an acyl group (R-) from a carboxylic acid is linked to the thiol (-SH) group of coenzyme A through a high-energy thioester bond. The energy required for this activation is provided by the hydrolysis of ATP to AMP and inorganic pyrophosphate (PP~i~).

CoA ligases are classified into three main types based on the nature of the acyl group they activate:

1. Acyl-CoA synthetases (or long-chain fatty acid CoA ligases) activate long-chain fatty acids, typically containing 12 or more carbon atoms.
2. Aminoacyl-CoA synthetases activate amino acids to form aminoacyl-CoAs, which are essential intermediates in the catabolism of certain amino acids.
3. Short-chain specific CoA ligases activate short-chain fatty acids (up to 6 carbon atoms) and other acyl groups like acetate or propionate.

These enzymes play a crucial role in maintaining cellular energy homeostasis, metabolism, and the synthesis of various essential biomolecules.

Sleep deprivation is a condition that occurs when an individual fails to get sufficient quality sleep or the recommended amount of sleep, typically 7-9 hours for adults. This can lead to various physical and mental health issues. It can be acute, lasting for one night or a few days, or chronic, persisting over a longer period.

The consequences of sleep deprivation include:

1. Fatigue and lack of energy
2. Difficulty concentrating or remembering things
3. Mood changes, such as irritability or depression
4. Weakened immune system
5. Increased appetite and potential weight gain
6. Higher risk of accidents due to decreased reaction time
7. Health problems like high blood pressure, diabetes, and heart disease over time

Sleep deprivation can be caused by various factors, including stress, shift work, sleep disorders like insomnia or sleep apnea, poor sleep hygiene, and certain medications. It's essential to address the underlying causes of sleep deprivation to ensure proper rest and overall well-being.

A seizure is an uncontrolled, abnormal firing of neurons (brain cells) that can cause various symptoms such as convulsions, loss of consciousness, altered awareness, or changes in behavior. Seizures can be caused by a variety of factors including epilepsy, brain injury, infection, toxic substances, or genetic disorders. They can also occur without any identifiable cause, known as idiopathic seizures. Seizures are a medical emergency and require immediate attention.

In the context of medical terminology, tablets refer to pharmaceutical dosage forms that contain various active ingredients. They are often manufactured in a solid, compressed form and can be administered orally. Tablets may come in different shapes, sizes, colors, and flavors, depending on their intended use and the manufacturer's specifications.

Some tablets are designed to disintegrate or dissolve quickly in the mouth, making them easier to swallow, while others are formulated to release their active ingredients slowly over time, allowing for extended drug delivery. These types of tablets are known as sustained-release or controlled-release tablets.

Tablets may contain a single active ingredient or a combination of several ingredients, depending on the intended therapeutic effect. They are typically manufactured using a variety of excipients, such as binders, fillers, and disintegrants, which help to hold the tablet together and ensure that it breaks down properly when ingested.

Overall, tablets are a convenient and widely used dosage form for administering medications, offering patients an easy-to-use and often palatable option for receiving their prescribed treatments.

Electroencephalography (EEG) is a medical procedure that records electrical activity in the brain. It uses small, metal discs called electrodes, which are attached to the scalp with paste or a specialized cap. These electrodes detect tiny electrical charges that result from the activity of brain cells, and the EEG machine then amplifies and records these signals.

EEG is used to diagnose various conditions related to the brain, such as seizures, sleep disorders, head injuries, infections, and degenerative diseases like Alzheimer's or Parkinson's. It can also be used during surgery to monitor brain activity and ensure that surgical procedures do not interfere with vital functions.

EEG is a safe and non-invasive procedure that typically takes about 30 minutes to an hour to complete, although longer recordings may be necessary in some cases. Patients are usually asked to relax and remain still during the test, as movement can affect the quality of the recording.

Absence epilepsy is a type of epilepsy characterized by recurrent brief episodes of "absences," or staring spells, that can last from a few seconds to several minutes. These episodes are often accompanied by subtle body movements such as lip smacking or eyelid flutters. Absence epilepsy is most commonly diagnosed in children and adolescents, and it is more common in girls than boys.

The seizures in absence epilepsy are caused by abnormal electrical activity in the brain, specifically in a part of the brain called the cortex. These abnormal electrical discharges occur in a pattern that involves both sides of the brain simultaneously. This differs from other types of epilepsy, which may involve only one side of the brain or specific areas within a single hemisphere.

Absence seizures are typically brief and do not cause confusion or disorientation after they end. However, if they occur frequently, they can interfere with learning and social development. In some cases, absence epilepsy may be associated with other types of seizures, such as generalized tonic-clonic (grand mal) seizures or myoclonic jerks.

The diagnosis of absence epilepsy is usually made based on the characteristic symptoms and the results of an electroencephalogram (EEG), which can detect the abnormal electrical activity in the brain during a seizure. Treatment typically involves medication to control the seizures, such as ethosuximide or valproic acid. In some cases, a ketogenic diet may also be recommended as an alternative treatment option.

I'm sorry for any confusion, but "pamphlets" is not a medical term. It refers to a small paper booklet or leaflet that can be used to provide information on various topics, including non-medical subjects. If you have any questions about medical terminology or concepts, I'd be happy to help with those!

Neurology is a branch of medicine that deals with the study and treatment of diseases and disorders of the nervous system, which includes the brain, spinal cord, peripheral nerves, muscles, and autonomic nervous system. Neurologists are medical doctors who specialize in this field, diagnosing and treating conditions such as stroke, Alzheimer's disease, epilepsy, Parkinson's disease, multiple sclerosis, and various types of headaches and pain disorders. They use a variety of diagnostic tests, including imaging studies like MRI and CT scans, electrophysiological tests like EEG and EMG, and laboratory tests to evaluate nerve function and identify any underlying conditions or abnormalities. Treatment options may include medication, surgery, rehabilitation, or lifestyle modifications.

Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. This ... In enzymology, an acyl-CoA oxidase (EC is an enzyme that catalyzes the chemical reaction acyl-CoA + O2 ⇌ {\ ... Osumi T, Hashimoto T, Ui N (June 1980). "Purification and properties of acyl-CoA oxidase from rat liver". J. Biochem. 87 (6): ... November 1980). "Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase". J. Biochem. 88 (5): 1481-6. doi:10.1093/ ...
... affects a person from birth, and most newborns affected with this condition will not survive past ... Acyl-CoA oxidase deficiency is an extremely rare condition. Diagnosis can be done both prenatally based on family history and ... Acyl-CoA oxidase deficiency is a rare disorder that leads to significant damage and deterioration of nervous system functions ( ... Acyl-CoA oxidase deficiency is an autosomal recessive disorder that is caused by biallelic pathogenic variants in ACOX1. This ...
ARFGEF2 Peroxisomal acyl-CoA oxidase deficiency; 264470; ACOX1 Perry syndrome; 168605; DCTN1 Persistent Mullerian duct syndrome ... SCARB2 Acyl-CoA dehydrogenase, long chain, deficiency of; 201460; ACADL Acyl-CoA dehydrogenase, medium chain, deficiency of; ... ACADM Acyl-CoA dehydrogenase, short chain, deficiency of; 201470; ACADS Adenocarcinoma of lung, response to tyrosine kinase ... HADHSC 3-hydroxyisobutryl-CoA hydrolase deficiency; 250620; HIBCH 3-M syndrome; 273750; CUL7 3-Methylcrotonyl-CoA carboxylase 1 ...
Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK (May 1994). "Isolation of the human peroxisomal acyl-CoA oxidase gene ... 2002). "Peroxisomal acyl CoA oxidase deficiency". J. Pediatr. 140 (1): 128-30. doi:10.1067/mpd.2002.120511. PMID 11815777. ... ACOX3 Acyl-CoA oxidase GRCh38: Ensembl release 89: ENSG00000161533 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... 1995). "Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells". J. Biol. Chem. 270 (9 ...
An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA ... THC-CoA oxidase, THCA-CoA oxidase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, 3alpha,7alpha,12alpha- ... Schepers L, Van Veldhoven PP, Casteels M, Eyssen HJ, Mannaerts GP (1990). "Presence of three acyl-CoA oxidases in rat liver ... 12alpha-trihydroxy-5beta-chole stanoyl-CoA oxidase from rabbit liver". J. Biol. Chem. 272 (29): 18481-9. doi:10.1074/jbc.272.29 ...
It shows some homology to acyl-CoA oxidases and those containing flavins. Recent observations suggest that AidB may bind to ...
Acyl-Coenzyme A oxidase 3 also known as pristanoyl-CoA oxidase (ACOX3) is involved in the desaturation of 2-methyl branched ... ACOX1 Acyl-CoA oxidase GRCh38: Ensembl release 89: ENSG00000087008 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and ... "Entrez Gene: ACOX3 acyl-Coenzyme A oxidase 3, pristanoyl". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to ...
... and acyl-CoA oxidase. Changes in expression were reportedly due to epigenetic regulation of either the gene promoter itself, or ... Feeding a PR-diet to pregnant and/or lactating mice also increased expression of glucokinase, acetyl-CoA carboxylase, PPARα, ...
... acyl-CoA oxidase (see, e.g., ACOX1, MIM 609751); the 'D-bifunctional enzyme,' with enoyl-CoA hydratase and D-3-hydroxyacyl-CoA ... "Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA ... Jiang LL, Miyazawa S, Souri M, Hashimoto T (February 1997). "Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA ... Itoh M, Suzuki Y, Takashima S (June 1999). "A novel peroxisomal enzyme, D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA ...
... dehydrogenation of fatty acyl-CoA in peroxisomes). Most of the oxidases are flavoproteins. The name "mixed-function oxidase" ... saturated fatty acyl-CoA and NADPH are oxidized by molecular oxygen (O2) to produce monounsaturated fatty acyl-CoA, NADP+ and 2 ... Desaturation of fatty acyl-CoA in vertebrates is an example of the mixed-function oxidase reaction. In the process, ... Mixed-function oxidase is the name of a family of oxidase enzymes that catalyze a reaction in which each of the two atoms of ...
1 with or without hormone resistance Acrofrontofacionasal dysostosis Acromelic frontonasal dysostosis Acyl-CoA oxidase ...
... and branched chain acyl-CoA oxidase. Möller G, van Grunsven EG, Wanders RJ, Adamski J (January 2001). "Molecular basis of D- ... DBP is a stereospecific enzyme; hydratase domain forms only (R)-hydroxy-acyl-CoA intermediates from trans-2-enoyl-CoAs. D-BP is ... D-BP knockout mice show compensatory upregulation of other peroxisomal enzymes in absence of D-BP such as palmitoyl-CoA oxidase ... van Grunsven EG, Mooijer PA, Aubourg P, Wanders RJ (August 1999). "Enoyl-CoA hydratase deficiency: identification of a new type ...
D-amino acid oxidase, glucose oxidase, xanthine oxidase, and acyl CoA dehydrogenase. FADH and FADH2 are reduced forms of FAD. ... Flavin adenine dinucleotide is a group bound to many enzymes including ferredoxin-NADP+ reductase, monoamine oxidase, ...
"Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily". Proc ... a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase". Arch. Biochem. Biophys. 433 (1): 157-65. doi:10.1016/j. ... In enzymology, a nitroalkane oxidase (EC is an enzyme that catalyzes the chemical reaction a nitroalkane + H2O + O2 ... Other names in common use include nitroethane oxidase, NAO, and nitroethane:oxygen oxidoreductase. This enzyme participates in ...
... cytochrome c oxidase, subunit 4, isoform 2) genes with racing performance in Thoroughbred horses". Equine Veterinary Journal. ... Acyl-CoA thioesterase 9 is a protein that is encoded by the human ACOT9 gene. It is a member of the acyl-CoA thioesterase ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ...
... acyl-coa dehydrogenase, long-chain MeSH D08.811.682.660.150.200 - acyl-CoA oxidase MeSH D08.811.682.660.150.300 - butyryl-coa ... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 - acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 - ... sarcosine oxidase MeSH D08.811.682.662.640 - proline oxidase MeSH D08.811.682.662.680 - pyridoxamine-phosphate oxidase MeSH ... acyl-carrier protein) reductase (nadph, b-specific) MeSH D08.811.682.660.425 - Glutaryl-CoA dehydrogenase MeSH D08.811.682.660. ...
... deficiency of Acyl-CoA dehydrogenase, very long chain, deficiency of Acyl-CoA oxidase deficiency Adactylia unilateral dominant ... Acute promyelocytic leukemia Acute renal failure Acute respiratory distress syndrome Acute tubular necrosis Acyl-CoA ... dehydrogenase, medium chain, deficiency of Acyl-CoA dehydrogenase, short chain, ...
It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for ... Other names in common use include long-chain fatty alcohol oxidase, fatty alcohol oxidase, fatty alcohol:oxygen oxidoreductase ... Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. ... Long-chain alcohol oxidase is also used in germinating seedlings of jojoba (Simmondsia chinensis) to degrade esterified long- ...
... deficiency of subtypes of acyl CoA dehydrogenase (LCAD, SCAD, MCAD, VLCAD, 3-hydroxyacyl-coenzyme A dehydrogenase deficiency), ... thiolase deficiency Mitochondrial myopathies: deficiency of succinate dehydrogenase, cytochrome c oxidase and coenzyme Q10 ...
The first oxidation step in the peroxisome is catalyzed by the enzyme acyl-CoA oxidase. The β-ketothiolase used in peroxisomal ... Cn-acyl-CoA + FAD + NAD+ + H 2O + CoA → Cn-2-acyl-CoA + FADH 2 + NADH + H+ + acetyl-CoA Free fatty acids cannot penetrate any ... The final cycle produces two separate acetyl CoAs, instead of one acyl CoA and one acetyl CoA. For every cycle, the Acyl CoA ... is not an appropriate substrate for acyl CoA dehydrogenase, or enoyl CoA hydratase: If the acyl CoA contains a cis-Δ3 bond, ...
... short/branched-chain acyl-CoA dehydrogenase), valine (isobutyryl-CoA dehydrogenase), and lysine (glutaryl-CoA dehydrogenase). ... Glucose oxidase (GOX) catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone with the simultaneous reduction of enzyme- ... such as for multiple acyl-CoA dehydrogenase deficiency. In addition, riboflavin deficiency itself (and the resulting lack of ... Monoamine oxidase (MAO) is an extensively studied flavoenzyme due to its biological importance with the catabolism of ...
... protoporphyrinogen oxidase EC bilirubin oxidase EC acyl-CoA oxidase EC dihydrouracil oxidase EC 1.3. ... medium-chain acyl-CoA dehydrogenase, EC, long-chain acyl-CoA dehydrogenase and EC, very-long-chain acyl-CoA ... medium-chain acyl-CoA dehydrogenase EC long-chain acyl-CoA dehydrogenase EC very-long-chain acyl-CoA ... acyl-lipid (11-3)-desaturase EC acyl-CoA 11-(Z)-desaturase EC acyl-CoA (9+3)-desaturase EC Now ...
... through substrate-level phosphorylation catalyzed by succinyl-CoA synthetase, as succinyl-CoA is converted to succinate, three ... Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain. In oxidative phosphorylation, the ... imply a high amount of reduced cytochrome c and a high level of cytochrome c oxidase activity. An additional level of ... The acetyl-CoA is metabolized by the citric acid cycle to generate ATP, while the NADH and FADH2 are used by oxidative ...
... acyl-carrier-protein) reductase (NADH) - (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase - 3(or 17)a-hydroxysteroid ... 4-hydroxyphenylpyruvate oxidase - 4-Nitrophenol 4-monooxygenase - 4933425L06Rik - 5' end - 5' flanking region - 5-pyridoxate ... myristoyl-CoA 11-(E) desaturase - myristoyl-CoA 11-(Z) desaturase - N terminus - N-acetylhexosamine 1-dehydrogenase - N- ... succinate-citramalate CoA-transferase - suicide gene - sulfate-transporting ATPase - supercoil - SurE, survival protein E - Syb ...
The citric acid cycle involves acyl-CoA, pyruvate, acetyl-CoA, citrate, isocitrate, α-ketoglutarate, succinyl-CoA, fumarate, ... cytochrome c oxidase). The electron transport chain is responsible for establishing a pH and electrochemical gradient that ... β-Oxidation uses pyruvate carboxylase, acyl-CoA dehydrogenase, and β-ketothiolase. Amino acid production is facilitated by ... The production of acetyl-CoA begins the citric acid cycle while the co-enzymes produced are used in the electron transport ...
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 ... NADPH Oxidase Family 5.B.2 The Eukaryotic Cytochrome b561 (Cytb561) Family 5.B.3 The Geobacter Nanowire Electron Transfer (G- ... Superfamily 3.D.4 Proton-translocating Cytochrome Oxidase (COX) Superfamily 3.D.5 The Na+-translocating NADH:Quinone ...
MPS-III-D Muenke syndrome Multiple acyl-CoA dehydrogenase deficiency Multiple congenital anomalies-hypotonia-seizures syndrome ... Sialuria Simpson-Golabi-Behmel syndrome Snijders Blok-Campeau syndrome Sotos syndrome Sturge-Weber syndrome Sulfite oxidase ...
Multiple p Multiple acyl-CoA deficiency Multiple carboxylase deficiency, biotin responsive Multiple carboxylase deficiency, ... Molybdenum cofactor deficiency MOMO syndrome Mondini dysplasia Mondor's disease Monge's disease Monilethrix Monoamine oxidase A ... nodule of the upper lip Mediastinal endodermal sinus tumors Mediastinal syndrome Mediterranean fever Medium-chain Acyl-CoA ... mixed Müllerian tumor Malignant paroxysmal ventricular tachycardia Mallory-Weiss syndrome Malonic aciduria Malonyl-CoA ...
Ikeda Y, Dabrowski C, Tanaka K (25 January 1983). "Separation and properties of five distinct acyl-CoA dehydrogenases from rat ... Cytochrome c oxidase, also known as complex IV, is the final protein complex in the electron transport chain. The mammalian ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066-76. doi:10.1016/S0021- ... The cytochrome c oxidase complex is highly efficient at reducing oxygen to water, and it releases very few partly reduced ...
... oleoyl-CoA + 2 ferricytochrome b5 + H2O EC linoleoyl-CoA 9-desaturase linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 ... sulfite oxidase (EC, plant and fungal nitrate reductases (EC, EC, EC, and plant and fungal ... cytochrome b5/acyl lipid desaturase fusion proteins. 3-D structures of a number of cytochrome b5 and yeast flavocytochrome b2 ... H2O EC stearoyl-CoA 9-desaturase stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ → ...
Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. This ... In enzymology, an acyl-CoA oxidase (EC is an enzyme that catalyzes the chemical reaction acyl-CoA + O2 ⇌ {\ ... Osumi T, Hashimoto T, Ui N (June 1980). "Purification and properties of acyl-CoA oxidase from rat liver". J. Biochem. 87 (6): ... November 1980). "Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase". J. Biochem. 88 (5): 1481-6. doi:10.1093/ ...
Peroxisomal acyl-CoA oxidase deficiency is a disorder that causes deterioration of nervous system functions (neurodegeneration ... Peroxisomal acyl-CoA oxidase deficiency. ... Peroxisomal acyl-CoA oxidase deficiency is caused by mutations in the ACOX1 gene, which provides instructions for making an ... Peroxisomal acyl-CoA oxidase deficiency is a rare disorder. Its prevalence is unknown. Only a few dozen cases have been ...
acyl-CoA oxidase, Activity: , 20 U/mg - 10KU. ...
Acyl-CoA dehydrogenase C-terminal-like. 58. 2. 119535. Acyl-CoA oxidase. C-terminal. - Molecular Function: acyl-CoA oxidase ... Acyl-CoA dehydrogenase C-terminal-like. 14. 5. 129855. Acyl-CoA oxidase. C-terminal. - Molecular Function: acyl-CoA oxidase ... ACX6 (ACYL-COA OXIDASE 6); FAD binding / acyl-CoA dehydrogenase/ acyl-CoA oxidase/ electron car…. ... At1g06310.1 68408.m00606 acyl-CoA oxidase ACX3 -related similar to acyl-CoA oxidase ACX3 GI:816…. ...
At4g16760.1 68411.m02303 acyl-CoA oxidase like protein swissprot. blastx. No significant hits ( or none blast was used over ... gi,15553480,gb,AAL01888.1, acyl-CoA oxidase [Glycine max]. arabidopsis. blastx. At4g16760.1. 515.8. 1e-146. 79.55. 924 bp (88.7 ... Putative Homology: acyl-CoA oxidase. Annotation Keywords: lipid metabolism; fatty acid biosynthesis ...
Nitroalkane oxidase: active site mutant D402N crystallized with 1-nitrooctane ... The flavoenzyme nitroalkane oxidase is a member of the acyl-CoA dehydrogenase superfamily. Nitroalkane oxidase catalyzes the ... Crystal structures of intermediates in the nitroalkane oxidase reaction.. Heroux, A., Bozinovski, D.M., Valley, M.P., ... When nitroalkane oxidase oxidizes nitroalkanes in the presence of cyanide, an electrophilic flavin imine intermediate can be ...
In agreement, there were no significant differences between sites in the peroxisomal acyl CoA oxidase activity. The content of ...
Acyl-CoA oxidase I deficiency. ACOX1. CNV. Combined malonic and methylmalonic aciduria. ACSF3. CNV. ... Short chain acyl-CoA dehydrogenase deficiency. ACADS. CNV. Short/branched chain acyl-CoA dehydrogenase deficiency. ACADSB. CNV ... Medium chain acyl-CoA dehydrogenase deficiency. ACADM. CNV. ... Very long chain acyl-CoA dehydrogenase deficiency. ACADVL. CNV ...
These genes, containing PPAR-response elements, are fatty acyl-CoA oxidase (ACO) and UCP2, which catalyze the limiting steps of ... THE MALONYL-CoA/CPT-1 INTERACTION IN THE CONTROL OF INSULIN SECRETION. The role of acyl-CoA compounds as coupling factors ... ACO, acyl-CoA oxidase; DAG, diacylglycerol; detox, detoxification; G3P, glycerol 3-phosphate; PL, phospholipid; UCP2, ... ACO, acyl-CoA oxidase; DAG, diacylglycerol; detox, detoxification; G3P, glycerol 3-phosphate; PL, phospholipid; UCP2, ...
A new peroxisomal disorder with enlarged peroxisomes and a specific deficiency of acyl-CoA oxidase (pseudo-neonatal ... Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in ... The end result is the formation of acetylcoenzyme A (acetyl-CoA) units, which are degraded in the Krebs cycle to produce energy ... Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat Genet. 1997 Oct. 17(2):190-3. [QxMD MEDLINE ...
Very large peroxisomes in distinct peroxisomal disorders (rhizomelic chondrodysplasia punctata and acyl-CoA oxidase deficiency ...
Peroxisomal acyl-CoA oxidase deficiency. *Phosphoethanolaminuria. *Polyarteritis nodosa. *Porphobilinogen synthase deficiency. ...
... acyl-CoA oxidase [ACO]) FAO enzymes were also induced in the mouse heart during the fast (Figure 2). In contrast to the results ... acyl-CoA oxidase, and muscle-type carnitine palmitoyltransferase I (M-CPT I) probes have been described (23). ... acyl-CoA oxidase [ACO]) FAO enzymes was also assessed. The results shown are representative of three independent experiments. ... medium-chain acyl-CoA dehydrogenase and mitochondrial malate dehydrogenase. J Biol Chem 1989. 264:18921-18925. View this ...
... the acyl-CoA synthetase, the straight-chain acyl-CoA oxidase, the L-bifunctional protein and the 3-ketoacyl-CoA thiolase genes ... In particular, the acyl-CoA synthetase, the carnitine palmitoyl transferase I, the very long-chain acyl-CoA dehydrogenase and ... within the acyl CoA oxidase gene promoter. Toxicol Lett. 1999;110:119-127. [PubMed] [DOI] [Cited in This Article: ] ... flanking sequence of the rat acyl CoA oxidase gene. EMBO J. 1992;11:433-439. [PubMed] [DOI] [Cited in This Article: ] ...
IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal. IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain ... IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily. IPR006091 Acyl-CoA oxidase/dehydrogenase, middle ... Human Disease Modeled: short chain acyl-CoA dehydrogenase deficiency. Allelic Composition. Genetic Background. Reference. ... IPR009075 Acyl-CoA dehydrogenase/oxidase, C-terminal. ... IPR046373 Acyl-CoA oxidase/dehydrogenase, middle domain ...
VK2 enhanced the fatty acid β-oxidation activity in peroxisome to degrade and digest fatty acid-CoA. Our study implies that VK2 ... VK2 enhanced the fatty acid β-oxidation activity in peroxisome to degrade and digest fatty acid-CoA. Our study implies that VK2 ... The human orthologs of acox-1.2 have been implicated in peroxisomal acyl-CoA oxidase activity and are involved in fatty acid β- ... acs-18 is a long-chain fatty acid-CoA ligase, which adds the -CoA onto the fat chains, allowing fatty acid-CoA to be digested ...
2018) Combining Promiscuous Acyl-CoA Oxidase and Enoyl-CoA Carboxylase/Reductases for Atypical Polyketide Extender Unit ... 2021) Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from ... 2019) Four amino acids define the CO2 binding pocket of enoyl-CoA carboxylases/reductases. Proc Natl Acad Sci U S A . 10.1073/ ... 2018) The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite. Nat Chem Biol 14(12), 1127-1132. ...
Olsen, J.A., Huang, A.H.C. (1988) Glyoxysomal acyl CoA synthetase and oxidase from germinating elm, rape and maize seed. ... Rupturing of the mitochondrial membrane allowed rapid access of acyl CoAs to matrix sites. Consequently, in ruptured ... Galliard, T. (1980) Degradation of acyl lipids: hydrolytic and oxidative enzymes. In: The biochemistry of plants, a ... prevents rapid access of acyl-GoA substrates to matrix βoxidation tes. Thus intact mitochondria showed little β-oxidation ...
Peroxisomal Acyl-Coa Oxidase Deficiency. Abnormality of visual evoked potentials, Myopia. ORPHA:2971. ...
acyl-CoA oxidase. -. 7e-39. At4g16760. ACX1 (ACYL-COA OXIDASE 1). O.I.. H.G.. S.X.. Please select. ...
ACX6 (ACYL-COA OXIDASE 6). Encodes a putative acyl-CoA oxidase. However, no transcripts have been detected for this gene and no ... S)-2-hydroxy-acid oxidase, peroxisomal, putative / glycolate oxidase, putative / short chain alpha-hydroxy acid oxidase, ... F:transferase activity, transferring acyl groups other than amino-acyl groups, transferase activity;P:biological_process ... F:glycolate oxidase activity, electron carrier activity, oxidoreductase activity, FMN binding, catalytic activity;P:metabolic ...
Detection of peroxisome proliferators using a reporter construct derived from the rat acyl-CoA oxidase promoter in the rat ... Thiazolidinediones downregulate stearoyl-CoA desaturase 1 gene expression in 3T3-L1 adipocytes. Kurebayashi, S., Hirose, T., ... To understand the molecular source of these radical species, NADPH oxidase-deficient (p47(phox)-null) and PPARalpha-null mice ... untreated), and leptin (-52%), and also muscle triglyceride (-34%) and total long-chain acyl-CoAs (LCACoAs) (-41%) (P , 0.05) [ ...
Growth on triolein stimulated increased enzyme activity, especially for acyl-CoA dehydrogenase. No acyl-CoA oxidase activity ... Octanoyl-CoA accumulated as the decanoyl-CoA was oxidized. β-Oxidation enzymes in isolated mitochondrial fractions were also ... HPLC analysis after incubation of triolein-grown cell extracts with decanoyl-CoA showed that β-oxidation was limited to one ... especially for acyl-CoA dehydrogenase. No acyl-CoA oxidase activity was detected. HPLC analysis after incubation of triolein- ...
But the mRNA level of gene acyl-CoA oxidase (ACO) involved in fatty acid β-oxidation was significantly increased in 5 % ... including acetyl-CoA carboxylase 1 (ACC1). Although the mRNA level of fatty acid synthase (FASN) have no statistical difference ...
acyl-CoA oxidase activity. IEP. Enrichment. MF. GO:0005215. transporter activity. IEP. Enrichment. ...
  • Peroxisomal acyl-CoA oxidase deficiency is a disorder that causes deterioration of nervous system functions (neurodegeneration) beginning in infancy. (
  • Newborns with peroxisomal acyl-CoA oxidase deficiency have weak muscle tone (hypotonia) and seizures. (
  • Most babies with peroxisomal acyl-CoA oxidase deficiency learn to walk and begin speaking, but they experience a gradual loss of these skills (developmental regression), usually beginning between the ages of 1 and 3. (
  • Most children with peroxisomal acyl-CoA oxidase deficiency do not survive past early childhood. (
  • Peroxisomal acyl-CoA oxidase deficiency is a rare disorder. (
  • Peroxisomal acyl-CoA oxidase deficiency is caused by mutations in the ACOX1 gene, which provides instructions for making an enzyme called peroxisomal straight-chain acyl-CoA oxidase. (
  • It is unclear exactly how VLCFA accumulation leads to the specific features of peroxisomal acyl-CoA oxidase deficiency. (
  • Leukodystrophy is likely involved in the development of the neurological abnormalities that occur in peroxisomal acyl-CoA oxidase deficiency. (
  • In enzymology, an acyl-CoA oxidase (EC is an enzyme that catalyzes the chemical reaction acyl-CoA + O2 ⇌ {\displaystyle \rightleftharpoons } trans-2,3-dehydroacyl-CoA + H2O2 Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2,3-dehydroacyl-CoA and H2O2. (
  • The systematic name of this enzyme class is acyl-CoA:oxygen 2-oxidoreductase. (
  • The peroxisomal straight-chain acyl-CoA oxidase enzyme plays a role in the breakdown of certain fat molecules called very long-chain fatty acids (VLCFAs). (
  • ACOX1 gene mutations prevent the peroxisomal straight-chain acyl-CoA oxidase enzyme from breaking down VLCFAs efficiently. (
  • Growth on triolein stimulated increased enzyme activity, especially for acyl-CoA dehydrogenase. (
  • The enzymes include acyl-COA oxidase fat and malic enzyme. (
  • His Endocrinology research includes themes of Enzyme assay, Enzyme, Newborn screening, Myopathy and Acyl CoA dehydrogenase. (
  • Propionic acidemia is an autosomal recessive, inherited, metabolic disorder that is caused by a defective form of the enzyme propionyl-coenzyme A (CoA) carboxylase, which results in the accumulation of propionic acid . (
  • The enzyme propionyl-CoA carboxylase, which requires biotin as a cofactor, catalyzes conversion of propionyl-CoA to methylmalonyl-CoA. (
  • ACL is an enzyme upstream of 3-hydroxy-3-methyl-glutaryl-coenzyme A (HMG-CoA) reductase in the cholesterol biosynthesis pathway. (
  • Methods: Immunohistochemical staining for lipid metabolism-related proteins [fatty acid synthase (FASN), hormone-sensitive lipase (HSL), carnitine palmitoyltransferase IA (CPT-1A), acyl- CoA oxidase 1 (ACOX1), fatty acid binding protein 4 (FABP4,) and perilipin 1 (PLIN1)] was performed using a tissue microarray of 149 cases of metastatic breast cancer (bone metastasis = 39, brain metastasis = 37, liver metastasis = 21, and lung metastasis = 52). (
  • Development of a newborn screening follow-up algorithm for the diagnosis of isobutyryl-CoA dehydrogenase deficiency. (
  • Coordinated and reversible reduction of enzymes involved in terminal oxidative metabolism in skeletal muscle mitochondria from a riboflavin-responsive, multiple acyl-CoA dehydrogenase deficiency patient. (
  • Anesthetic considerations for a patient with compound heterozygous medium-chain Acyl-CoA dehydrogenase deficiency. (
  • Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. (
  • Short-chain acyl-CoA dehydrogenase deficiency: a cause of ophthalmoplegia and multicore myopathy. (
  • Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. (
  • Acyl-coenzyme A oxidase consists of three domains. (
  • VK2 enhanced the fatty acid β-oxidation activity in peroxisome to degrade and digest fatty acid-CoA. (
  • Treatment has up-regulated of mRNA level of the peroxisome proliferator activated receptor-a and acyl-CoA oxidase. (
  • Acyl-CoA dehydrogenase domain-containing protein n=1 Tax=Pseudomonas sp. (
  • Nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to nitrite and the corresponding aldehydes or ketones. (
  • It is apparent that the mitochondrial membrane barrier, which remains intact after sucrose-density-gradient centrifugation, prevents rapid access of acyl-GoA substrates to matrix β oxidation tes. (
  • HPLC analysis after incubation of triolein-grown cell extracts with decanoyl-CoA showed that β-oxidation was limited to one cycle. (
  • Measurement of tissue acyl-CoAs using flow-injection tandem mass spectrometry: acyl-CoA profiles in short-chain fatty acid oxidation defects. (
  • acyl-CoA synthetase medium chain famil. (
  • Bempedoic acid and its active metabolite, ESP15228, require coenzyme A (CoA) activation by very long?chain acyl-CoA synthetase 1 (ACSVL1) to ETC-1002-CoA and ESP15228-CoA, respectively. (
  • Rupturing of the mitochondrial membrane allowed rapid access of acyl CoAs to matrix sites. (
  • 2112\2112\BAE47462.1\Arthrobacter ureafaciens\Arthrobacter ureafaciens aco gene for acyl-CoA oxidase, completecds. (
  • Galliard, T. (1980) Degradation of acyl lipids: hydrolytic and oxidative enzymes. (
  • Several genetic mutations, broadly categorized as defects in 2 subunits of the propionyl-CoA carboxylase gene ( PCCA and PCCB ), may give rise to varying levels of functioning propionyl-CoA carboxylase. (
  • No acyl-CoA oxidase activity was detected. (
  • Antisense morpholino oligonucleotides directed at intronic pseudoexons have been shown to increase propionyl-CoA carboxylase activity to normal levels in fibroblast cell lines derived from patients suffering from propionic acidemia. (
  • To a lesser degree, cholesterol and odd-chain fatty acids also contribute to propionyl-CoA levels. (
  • Accumulation of propionic acid apparently results in an abnormal cytochrome-c oxidase. (
  • NADPH oxidase 4 (NOX4), a source of cellular superoxide anion, has multiple biological functions that may be of importance in inflammation, and in the pathogenesis of human metabolic diseases, including diabetes. (
  • This process shortens the VLCFA molecules by two carbon atoms at a time until the VLCFAs are converted to a molecule called acetyl-CoA, which is transported out of the peroxisomes for reuse by the cell. (
  • The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions. (
  • The flavoenzyme nitroalkane oxidase is a member of the acyl-CoA dehydrogenase superfamily. (
  • Zinc-finger domain of monoamine-oxidase A repressor R1 [Interproscan]. (
  • the E-value for the Acyl-CoA_ox_N domain shown below is 4.1e-30. (
  • Cytochrome c oxidase subunit IV family [Interproscan]. (
  • Consequently, these results provide important structural descriptions of several steps along the nitroalkane oxidase reaction cycle. (
  • Dietary \alpha -18:3 also increased the activity of fatty acid oxidation enzymes except for 3-hydroxyacyl-CoA dehydrogenase. (
  • Unexpectedly, dietary \alpha -18:3 caused great reduction in the activity of 3-hydroxyacyl-CoA dehydrogenase measured with short- and medium-chain substrates but not with long-chain substrate. (
  • Dietary fats rich in \alpha -18:3-CoA relative to safflower oil did not affect the hepatic activity of fatty acid synthase and glucose 6-phosphate dehydrogenase. (
  • acyl-CoA dehydrogenase long chain [So. (
  • and increased acyl-CoA oxidase activity. (
  • An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. (
  • 5. Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene. (
  • 7. Acyl-coenzyme A oxidases 1 and 3 in brown trout (Salmo trutta f. fario): Can peroxisomal fatty acid β-oxidation be regulated by estrogen signaling? (
  • In this study, to produce adipic acid, mutant strains of Candida tropicalis KCTC 7212 deficient of AOX genes encoding acyl-CoA oxidases which are important in the β-oxidation pathway were constructed. (
  • Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. (
  • The nudix hydrolase 7 is an Acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis. (
  • 11. Long-chain acyl-CoA oxidases of Arabidopsis. (
  • 14. AoxA is a major peroxisomal long chain fatty acyl-CoA oxidase required for beta-oxidation in A. nidulans. (
  • Regarding the substrate specificity of \beta -oxidation pathway, mitochondrial and peroxisomal \beta -oxidation rate of \alpha -18:3-CoA, relative to 16:0- and 18:2-CoAs, was higher irrespective of the substrate/albumin ratios in the assay mixture or dietary fat sources. (
  • The substrate specificity of carnitine palmitoyltransferase I appeared to be responsible for the differential mitochondrial oxidation rates of these acyl-CoA substrates. (
  • 17. Presence of three acyl-CoA oxidases in rat liver peroxisomes. (
  • Mitochondrial and peroxisomal palmitoyl-CoA (16:0-CoA) oxidation rates in the liver homogenates were significantly higher in rats fed linseed and perilla oils than in those fed saturated fats and safflower oil. (
  • 4. Expression of an estrogen-regulated variant transcript of the peroxisomal branched chain fatty acid oxidase ACOX2 in breast carcinomas. (
  • 6. cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase. (
  • Acyl-CoA Oxidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (
  • 3alpha,7alpha-Dihydroxy-5beta-cholest-24-enoyl-CoA is an intermediate involved in bile acid synthesis, specifically in the synthesis of chenodeoxyglycocholate. (
  • This graph shows the total number of publications written about "Acyl-CoA Oxidase" by people in this website by year, and whether "Acyl-CoA Oxidase" was a major or minor topic of these publications. (