An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.
Family in the order COLUMBIFORMES, comprised of pigeons or doves. They are BIRDS with short legs, stout bodies, small heads, and slender bills. Some sources call the smaller species doves and the larger pigeons, but the names are interchangeable.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.
Contractile tissue that produces movement in animals.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
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)
Organic chemistry methodology that mimics the modular nature of various biosynthetic processes. It uses highly reliable and selective reactions designed to "click" i.e., rapidly join small modular units together in high yield, without offensive byproducts. In combination with COMBINATORIAL CHEMISTRY TECHNIQUES, it is used for the synthesis of new compounds and combinatorial libraries.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A technique using antibodies for identifying or quantifying a substance. Usually the substance being studied serves as antigen both in antibody production and in measurement of antibody by the test substance.
Commercially prepared reagent sets, with accessory devices, containing all of the major components and literature necessary to perform one or more designated diagnostic tests or procedures. They may be for laboratory or personal use.
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Structures within the nucleus of fungal cells consisting of or containing DNA, which carry genetic information essential to the cell.
The functional hereditary units of FUNGI.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
Deoxyribonucleic acid that makes up the genetic material of fungi.
Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
A fatty acid with anticonvulsant properties used in the treatment of epilepsy. The mechanisms of its therapeutic actions are not well understood. It may act by increasing GAMMA-AMINOBUTYRIC ACID levels in the brain or by altering the properties of voltage dependent sodium channels.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.
Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
Disease of the RETINA as a complication of DIABETES MELLITUS. It is characterized by the progressive microvascular complications, such as ANEURYSM, interretinal EDEMA, and intraocular PATHOLOGIC NEOVASCULARIZATION.
A bilateral retinopathy occurring in premature infants treated with excessively high concentrations of oxygen, characterized by vascular dilatation, proliferation, and tortuosity, edema, and retinal detachment, with ultimate conversion of the retina into a fibrous mass that can be seen as a dense retrolental membrane. Usually growth of the eye is arrested and may result in microophthalmia, and blindness may occur. (Dorland, 27th ed)
The blood vessels which supply and drain the RETINA.
Formation of new blood vessels originating from the retinal veins and extending along the inner (vitreal) surface of the retina.
A subtype of DIABETES MELLITUS that is characterized by INSULIN deficiency. It is manifested by the sudden onset of severe HYPERGLYCEMIA, rapid progression to DIABETIC KETOACIDOSIS, and DEATH unless treated with insulin. The disease may occur at any age, but is most common in childhood or adolescence.

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)

A study was conducted of the effects of 10 hypolipidaemic agents on peroxisomal and microsomal enzyme activities in primary cultures of rat hepatocytes. Treatment with compounds such as Wy-14,643, tiadenol, nafenopin, BR-931, clofibrate and mono-(2-ethylhexyl)phthalate induced cyanide-insensitive palmitoyl-CoA oxidation (a specific peroxisomal marker enzyme), a polypeptide with a molecular weight of 80,000 associated with peroxisome proliferation, and carnitine acetyltransferase activity, after 70 h of culture. These compounds also maintained hepatocyte cytochrome P-450 levels and markedly induced lauric acid hydroxylation, whereas little effect was observed on 7-ethoxycoumarin O-deethylase. Studies with metyrapone, which also maintains cytochrome P-450, suggested that treatment with the hypolipidaemic agents resulted in the formation of different form(s) of cytochrome P-450 to those present in control cultures. Regression analysis demonstrated a high correlation between the induction of the peroxisomal
Objective Fatty acid oxidation in macrophages is thought to regulate inflammatory status and insulin-sensitivity. fatty acids and are required for fatty acid oxidation [13]. Carnitine O-octanoyltransferase (CrOT) and carnitine acetyltransferase (CrAT) conjugate medium-chain and short-chain acyl-CoA to carnitine, respectively [13]. CrAT is localized primarily within the mitochondrial matrix and catalyzes both the addition and the removal of carnitine from acetyl-CoA [14], facilitating the efflux of mitochondrial acetyl-CoA and buffering the intracellular pools of acetyl-CoA and carnitine. Consistent with an important role of fatty acid oxidation in macrophages, CPT1, CPT2, Crat and Crot are abundantly expressed in macrophages [15]. Interestingly, the CrAT activity is reduced during obesity and aging, leading to impaired glycemic control [16], [17]. Notably, muscle-specific deletion of CrAT was shown to reduce exercise performance [18] and exacerbated metabolic dysregulation in HFD mice [19]. ...
Objective Fatty acid oxidation in macrophages is thought to regulate inflammatory status and insulin-sensitivity. fatty acids and are required for fatty acid oxidation [13]. Carnitine O-octanoyltransferase (CrOT) and carnitine acetyltransferase (CrAT) conjugate medium-chain and short-chain acyl-CoA to carnitine, respectively [13]. CrAT is localized primarily within the mitochondrial matrix and catalyzes both the addition and the removal of carnitine from acetyl-CoA [14], facilitating the efflux of mitochondrial acetyl-CoA and buffering the intracellular pools of acetyl-CoA and carnitine. Consistent with an important role of fatty acid oxidation in macrophages, CPT1, CPT2, Crat and Crot are abundantly expressed in macrophages [15]. Interestingly, the CrAT activity is reduced during obesity and aging, leading to impaired glycemic control [16], [17]. Notably, muscle-specific deletion of CrAT was shown to reduce exercise performance [18] and exacerbated metabolic dysregulation in HFD mice [19]. ...
Complete information for CRAT gene (Protein Coding), Carnitine O-Acetyltransferase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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TY - JOUR. T1 - Altered carnitine homeostasis is associated with decreased mitochondrial function and altered nitric oxide signaling in lambs with pulmonary hypertension. AU - Sharma, Shruti. AU - Sud, Neetu. AU - Wiseman, Dean A.. AU - Carter, A. Lee. AU - Kumar, Sanjiv. AU - Hou, Yali. AU - Rau, Thomas. AU - Wilham, Jason. AU - Harmon, Cynthia. AU - Oishi, Peter. AU - Fineman, Jeffrey R.. AU - Black, Stephen M.. PY - 2008/1/1. Y1 - 2008/1/1. N2 - Utilizing aortopulmonary vascular graft placement in the fetal lamb, we have developed a model (shunt) of pulmonary hypertension that mimics congenital heart disease with increased pulmonary blood flow. Our previous studies have identified a progressive development of endothelial dysfunction in shunt lambs that is dependent, at least in part, on decreased nitric oxide (NO) signaling. The purpose of this study was to evaluate the possible role of a disruption in carnitine metabolism in shunt lambs and to determine the effect on NO signaling. Our data ...
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Cells, particularly in skeletal muscle and adipose tissue, primarily store energy as triacylglycerols and catabolize them as needed. Alterations in the expression of genes involved in fatty acid metabolism, such as carnitine O-acetyltransferase, are often associated with metabolic syndrome and insulin resistance. These 2 syndromes are risk factors for multiple diseases including diabetes and obesity, as well as other prevalent health problems such as cardiovascular disease. Triacylglycerols are metabolized into fatty acids, which are transported into the mitochondria. The process of -oxidation catabolizes these activated fatty acids yielding acetyl-CoA, the initial metabolite necessary for the TCA cycle and ketone body metabolism. In the reverse process, fatty acids and additional lipids can be synthesized, depending on energy needs. The majority of this process is performed in adipose tissue ...
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Alhamdulilah MGC Kluang telah berjaya mengadakan lawatan ke IAB pada 6 November 2009, Lawatan ini disertai oleh 30 orang ahli MGC Kluang. Kami telah di berikan taklimat mengenai peranan IAB dalam memperkasakan kepimpinan di sekolah. taklimat disampaikan oleh Dr Hamizer. kami juga berkesempatan berjumpa dan mendapat nasihat dari ketua pengarah Institut Aminuddin Baki dato Abd Ghaffar. Terima kasih Dr Hamizer atas layanan dan ilmu yang diberi. Selain itu kami berpeluang melawat Plaza Low Yat merupakan pusat ICT terbesar di Malaysia, disamping melawat Putra Jaya. Terima kasih kepada semua GC yang memberikan sokongan dan menjayakan program tersebut ...
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Enzyme-coupled method have also been applied to detect carnitine formation, by using the enzyme carnitine acetyltransferase and ... Parvin R, Pande SV (1976). "Microdetermination of (−)carnitine and carnitine acetyltransferase activity". Anal. Biochem. 79 (1- ... Carnitine Mildronate Carnitine biosynthesis Beta Oxidation Fatty acid metabolism Stevens rearrangement GRCh38: Ensembl release ... the last step in the L-carnitine biosynthesis pathway. Carnitine is essential for the transport of activated fatty acids across ...
... has also been shown by NMR to bind to carnitine acetyltransferase. Carnitine acetyltransferase belongs to a family of ... The co-A is then exchanged with carnitine (via the enzyme carnitine palmitoyltransferase I) to produce a fatty acid-carnitine ... Meldonium is a relatively weak inhibitor to carnitine acetyltransferase (when compared to γ-butyrobetaine hydroxylase), with an ... Once inside, carnitine is liberated (catalysed by the enzyme carnitine palmitoyltransferase II) and transported back outside so ...
3-Hydroxyisovaleryl CoA is likely detoxified by carnitine acetyltransferase producing 3HIA-carnitine, which is transported ... The transfer to carnitine by 4 carnitine acyl-CoA transferases distributed in subcellular compartments likely serves as an ... 3HIA-carnitine is thought to be either directly deacylated by a hydrolase to 3HIA or to undergo a second CoA exchange to again ... "Urinary excretion of 3-hydroxyisovaleric acid and 3-hydroxyisovaleryl carnitine increases in response to a leucine challenge in ...
Esfahan and Tabriz Confédération Syndicale du Congo Catapult C Synthesis Carnitine O-acetyltransferase, an enzyme CATC AB, A ...
... cleavage enzyme Protein tyrosine phosphatase Carnitine O-palmitoyltransferase Carnitine O-acetyltransferase Carnitine O- ...
... arylamine N-acetyltransferase EC 2.3.1.6: choline O-acetyltransferase EC 2.3.1.7: carnitine O-acetyltransferase EC 2.3.1.8: ... D-tryptophan N-acetyltransferase EC 2.3.1.35: glutamate N-acetyltransferase EC 2.3.1.36: D-amino-acid N-acetyltransferase EC ... amino-acid N-acetyltransferase EC 2.3.1.2: imidazole N-acetyltransferase EC 2.3.1.3: glucosamine N-acetyltransferase EC 2.3.1.4 ... glycine C-acetyltransferase EC 2.3.1.30: serine O-acetyltransferase EC 2.3.1.31: homoserine O-acetyltransferase EC 2.3.1.32: ...
... amino-acid n-acetyltransferase MeSH D08.811.913.050.134.150 - carnitine O-acetyltransferase MeSH D08.811.913.050.134.170 - ... carnitine O-acetyltransferase MeSH D08.811.913.050.350.200 - carnitine o-palmitoyltransferase MeSH D08.811.913.050.368 - ... arylamine N-acetyltransferase MeSH D08.811.913.050.331 - atp citrate (pro-s)-lyase MeSH D08.811.913.050.350 - carnitine ... phosphate acetyltransferase MeSH D08.811.913.050.134.850 - serine O-acetyltransferase MeSH D08.811.913.050.170 - acyl-carrier ...
... may refer to: Instrument landing system#ILS categories Chloramphenicol O-acetyltransferase I, an enzyme Carnitine O- ...
"Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport". Cell. ... Carnitine O-palmitoyltransferase (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3. ... A related transferase is carnitine acyltransferase. Palmitoylcarnitine Palmitoyl CoA There are four different forms of CPT in ... PDOC00402 - Acyltransferases ChoActase / COT / CPT family in PROSITE Choline/Carnitine o-acyltransferase family[permanent dead ...
One such mechanism based upon a carnitine acetyltransferase model is shown below in which the His 473 deprotonates carnitine ... Carnitine palmitoyltransferase I (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase ( ... such as carnitine acetyltransferase (CRAT). An important structural difference between CPT1 and CPT2, CRAT and carnitine ... "Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal". The Biochemical Journal ...
... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC 2.3.1.7) is an enzyme that encoded by ... carnitine O-acetyltransferase. Other names in common use include acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine ... "Entrez Gene: CRAT carnitine acetyltransferase". CS1 maint: discouraged parameter (link) McGarry JD, Brown NF (Feb 1997). "The ...
2003). "Structure of Human Carnitine Acetyltransferase: Molecular Basis For Fatty Acyl Transfer". J Biol Chem. 278 (15): 13159- ... Carnitine O-palmitoyltransferase Carnitine palmitoyltransferase I deficiency Fasciculation Myokymia Primary carnitine ... The "carnitine shuttle" is composed of three enzymes that utilize carnitine to facilitate the import of hydrophobic long-chain ... Longo N, Amat, San Filippo C, Pasquali M (2006). "Disorders of Carnitine Transport and the Carnitine Cycle". Am J Med Genet C ...
In pre-synaptic neurons the majority of choline will be acetylated by the enzyme choline acetyltransferase to form the ... and/or carnitine/organic cation transporters (OCTNs), and do not require ATP. Lastly, choline may enter the cell through ...
Carnitine palmitoyltransferase II deficiency (also known as CPT-II deficiency) leads to an excess long chain fatty acids, as ... Choline acetyltransferase (also known as ChAT or CAT) is an important enzyme which produces the neurotransmitter acetylcholine ... Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (Feb 1991). "Human choline acetyltransferase gene maps to ... "Choline O-Acetyltransferase". GeneCards: The Human Gene Compendium. Weizmann Institute of Science. Retrieved 5 December 2013. ...
ACAT1: acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase). *APOA4: apolipoprotein A-IV ... carnitine palmitoyltransferase I deficiency. *Charcot-Marie-Tooth disease. *Charcot-Marie-Tooth disease, type 4 ...
Acetyltransferase. References[edit]. *^ a b c d e f g h i Lee KK, Workman JL (April 2007). "Histone acetyltransferase complexes ... Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring ... Gcn5-related N-acetyltransferases (GNATs)[edit]. HATs can be grouped into several different families based on sequence homology ... The Gcn5-related N-acetyltransferase (GNAT) family includes Gcn5, PCAF, Hat1, Elp3, Hpa2, Hpa3, ATF-2, and Nut1. These HATs are ...
"Comparison of the effects of L-carnitine and acetyl-L-carnitine on carnitine levels, ambulatory activity, and oxidative stress ... For example, on the DNA level, histone acetylation by acetyltransferases (HATs) causes an expansion of chromatin architecture, ... There is some evidence that acetyl-L-carnitine may be more effective for some applications than L-carnitine. Acetylation of ...
ACAT1: acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase) ACRV1: encoding protein Acrosomal protein SP-10 ... carnitine palmitoyltransferase 1A (liver) CREBZF encoding protein CREB/ATF bZIP transcription factor DAK: Triokinase/FMN ... Beckwith-Wiedemann syndrome Best's disease beta-ketothiolase deficiency beta thalassemia bladder cancer breast cancer carnitine ...
It was also observed that the activity of peroxisomal enzyme carnitine acetyl transferase is increased in cultures of rat liver ...
Histone acetyltransferase *P300/CBP. *NAT2. *palmitoyltransferases: Carnitine O-palmitoyltransferase *CPT1. *CPT2. *Serine C- ...
acyl-carrier-protein S-acetyltransferase activity]. • hydrolase activity, acting on ester bonds. • [acyl-carrier-protein S- ... Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ... malonyl/acetyltransferase (MAT), and dehydrase (DH)), are separated by a core region of 600 residues from four C-terminal ...
... acetyltransferase inhibitors have also been developed. In 1849, Adolph Strecker was the first to isolate choline from ... Thus, excessive choline intake has been hypothetized to increase these risks in addition to carnitine, which also is formed ...
Carnitine-CoA ligase EC 6.2.1.49: Long-chain fatty acid adenylyltransferase FadD28 EC 6.2.1.50: 4-hydroxybenzoate ... EC 2.3.1 Aminolevulinic acid synthase EC 2.3.1.37 Choline acetyltransferase EC 2.3.1.6 Category:EC 2.3.2 Factor XIII EC 2.3. ...
It has been proposed that histidine residue His122 of serotonin N-acetyl transferase is the catalytic residue that deprotonates ... Acetyl-L-carnitine (ALCAR). *Alpha-lipoic acid (ALA). *Ascorbic acid (vitamin C) ... Hickman AB, Klein DC, Dyda F (1999). "Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A ... but is also converted into N-acetylserotonin by serotonin N-acetyltransferase with acetyl-CoA.[54] Hydroxyindole O- ...
Rytting E, Audus KL (January 2005). "Novel organic cation transporter 2-mediated carnitine uptake in placental choriocarcinoma ... the phosphorylation of which induces its association with the histone acetyltransferase, CREB binding protein (CBP) to ... and SLC22A5 is a high-affinity carnitine transporter. Amphetamine is known to strongly induce cocaine- and amphetamine- ...
Histone acetyltransferases (HATs) are enzymes responsible for the addition of acetyl groups, and histone deacetylases (HDACs) ... placebo-controlled trial of L-carnitine and valproic acid in spinal muscular atrophy". primary. PLOS ONE. 5 (8): e12140. ...
SLC22A3 is an extraneuronal monoamine transporter that is present in astrocytes, and SLC22A5 is a high-affinity carnitine ... the phosphorylation of which induces its association with the histone acetyltransferase, CREB binding protein (CBP) to ...
... formate-C-acetyltransferase)-activating enzyme EC 1.97.1.5: now *EC 1.20.4.1 EC 1.97.1.6: now *EC 1.20.99.1 EC 1.97.1.7: now * ... carnitine 3-dehydrogenase EC 1.1.1.109: now *EC 1.3.1.28 EC 1.1.1.110: indolelactate dehydrogenase EC 1.1.1.111: 3-(imidazol-5- ... carnitine 3-dehydrogenase EC 1.1.1.255: mannitol dehydrogenase EC 1.1.1.256: fluoren-9-ol dehydrogenase EC 1.1.1.257: 4-( ...
Dunn WA, Rettura G, Seifter E, Englard S. Carnitine biosynthesis from gamma-butyrobetaine and from exogenous protein-bound 6-N- ... Rebouche CJ: Ascorbic acid and carnitine biosynthesis. Am J Clin Nutr 54:1147S-1152S, 1991. ... AANAT(英语:Serotonin N-acetyltransferase)抑製劑. ASMT(英语:Acetylserotonin O-methyltransferase)抑製劑 ...
EC 6.2.1.48: Carnitine--CoA ligase. *EC 6.2.1.49: Long-chain fatty acid adenylyltransferase FadD28 ... Choline acetyltransferase EC 2.3.1.6. *Category:EC 2.3.2 *Factor XIII EC 2.3.2.13 ...
... the phosphorylation of which induces its association with the histone acetyltransferase, CREB binding protein (CBP) to ... and SLC22A5 is a high-affinity carnitine transporter.[97][108] ...
... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC 2.3.1.7) is an enzyme that encoded by ... carnitine O-acetyltransferase. Other names in common use include acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine ... "Entrez Gene: CRAT carnitine acetyltransferase". CS1 maint: discouraged parameter (link) McGarry JD, Brown NF (Feb 1997). "The ...
Compare carnitine acetyltransferase ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, ... carnitine acetyltransferase ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool ... Your search returned 59 carnitine acetyltransferase ELISA ELISA Kit across 8 suppliers. ...
... FASEB J. 2018 Jun ... Here we report that AgRP carnitine acetyltransferase (Crat) knockout (KO) mice exhibited increased fatty acid utilization and ... Carnitine acetyltransferase (Crat) in hunger-sensing AgRP neurons permits adaptation to calorie restriction. ...
... July 2013 , Volume ... A peroxisomal-specific pathway for acetyl-CoA transport requiring peroxisomal carnitine acetyl transferase (CAT) activity has ...
View and select products within our Carnitine Acetyltransferase Inhibitors category available for immediate purchase. ... R)-Amino Carnitine (R)-Amino Carnitine is an inhibitor of fatty acid oxidation 98063-21-9 sc-208234 5 mg. $220.00 0 ... S)-Amino Carnitine (S)-Amino Carnitine is a hypoglycemic and antiketogenic compound 125377-87-9 sc-391837 2.5 mg. $350.00 0 ... together with carnitine carrier. Biochemicals that inhibit Carnitine Acetyltransferase have many applications in biochemical ...
Crystal structure of the M564G mutant of murine carnitine acetyltransferase in complex with carnitine. *DOI: 10.2210/pdb1T7O/ ... Carnitine acetyltransferase. A. 618. Mus musculus. Mutation(s): 1 Gene Names: Crat. EC: 2.3.1.7 (PDB Primary Data), 2.3.1.137 ( ... Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase. Hsiao, Y.-S., Jogl, G., Tong, L ... Structural information on carnitine acetyltransferase suggests that residues Met-564 and Phe-565 may be important determinants ...
Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ...
This gene encodes carnitine O-acetyltransferase, a member of the carnitine acyltransferase family and a key metabolic pathway ... structure of a binary complex of human peroxisomal carnitine acetyltransferase and the substrate l-carnitine, refined to a ... Carnitine Acetyltransferase Mitigates Metabolic Inertia and Muscle Fatigue during Exercise.. 25944712. 2015. N-terminome ... Obesity and lipid stress inhibit carnitine acetyltransferase activity.. 24275569. 2014. An enzyme assisted RP-RPLC approach for ...
What is carnitine acetyltransferase? Meaning of carnitine acetyltransferase medical term. What does carnitine acetyltransferase ... Looking for online definition of carnitine acetyltransferase in the Medical Dictionary? carnitine acetyltransferase explanation ... carnitine acetyltransferase. Also found in: Dictionary, Acronyms, Encyclopedia.. Related to carnitine acetyltransferase: ... Carnitine acetyltransferase , definition of carnitine acetyltransferase by Medical dictionary https://medical-dictionary. ...
Mittal, Balraj and Kurup, CK Ramakrishna (1981) Induction of carnitine acetyltransferase by clofibrate in rat liver. In: ... acetyl-CoA-carnitine -acetyltransferase, EC 2.3.1.7) in liver and kidney. The drug-mediated increase in enzyme activity in ... of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase ( ...
This gene encodes carnitine O-acetyltransferase, a member of the carnitine acyltransferase family and a key metabolic pathway ... carnitine O-acetyltransferase. Enable Javascript to view the expand/collapse boxes.. Open All Close All ... Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also ... This enzyme catalyzes the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine and regulates the ratio of ...
... rabbit IgG against Pigeon breast muscle Carnitine acetyltransferase \ NE028/7S for more molecular products just contact us ... We have also other products like : rabbit IgG against Pigeon breast muscle Carnitine acetyltransferase. Related products : ... Index / Nordic Immunological Lab / rabbit IgG against Pigeon breast muscle Carnitine acetyltransferase / Product Detail : NE028 ... NE028/7S rabbit IgG against Pigeon breast muscle Carnitine acetyltransferase Ask technical file . ...
Enzyme-coupled method have also been applied to detect carnitine formation, by using the enzyme carnitine acetyltransferase and ... Parvin R, Pande SV (1976). "Microdetermination of (−)carnitine and carnitine acetyltransferase activity". Anal. Biochem. 79 (1- ... Carnitine Mildronate Carnitine biosynthesis Beta Oxidation Fatty acid metabolism Stevens rearrangement GRCh38: Ensembl release ... the last step in the L-carnitine biosynthesis pathway. Carnitine is essential for the transport of activated fatty acids across ...
... carnitine palmitoyltransferase I; CHOP: C/EBP-homologous protein; CREBH-N: cyclic AMP response element-binding protein H; ERK: ... histone acetyltransferase; Hdac: histone deacetylases; Hsp47: heat shock protein 47; ICAM-1: intercellular Adhesion Molecule 1 ...
Carnitine Acetyltransferase. 10810118001. CHAPS, 10g. 10810126001. CHAPS, 50g. 10378445001. Chromozym PK. 10378461001. ...
Carnitine Acetyltransferase 2.3.1.7. Casein Kinase II 2.7.1.37. Catalase 1.11.1.6. ...
Distribution of carnitine, acetylcarnitine and carnitine acetyltransferase in rat tissues.J. Biol. Chem. 240:2193-2196.PubMed ... Carnitine acetyltransferase the question of multiple forms. Eur. J. Biochem. 46:209-215.PubMedCrossRefGoogle Scholar ... Inhibition of ENZ carnitine acetyl transferase and mammalian ENZ fatty-acid synthetase by bromoacetyl coenzyme A. Abstracts of ... The substrate specificity of carnitine acetyltransferase in rat tissue. J. Biol. Chem. 240:2193-2196.Google Scholar ...
Putative mitochondrial carnitine O-acetyltransferase. Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Bakers yeast) ... Putative mitochondrial carnitine O-acetyltransferase UniProtKBInterProSTRINGInteractive Modelling. 687 aa; Sequence (Fasta) ...
Yar030p; Yar040p; acid phosphatase; carnitine N-acetyltransferase; homologue; membrane spanning; transfer RNA-Leu; transfer RNA ...
Crystal Structure of Carnitine Acetyltransferase and Implications for the Catalytic Mechanism and Fatty Acid Transport journal ... Substrate Binding and Catalytic Mechanism of Human Choline Acetyltransferase † , ‡ journal, December 2006 * Kim, Ae-Ri; Rylett ... Substrate Binding and Catalytic Mechanism of Human Choline Acetyltransferase † , ‡ journal, December 2006 * Kim, Ae-Ri; Rylett ... A Synthetic Receptor for Choline and Carnitine journal, November 2002 * Ballester, Pablo; Shivanyuk, Alexander; Far, Adel Rafai ...
... carnitine O-acetyltransferase, and coagulation factor III, were associated with decreased lung function (202). Zinc is a ... carnitine O-acetyltransferase; F3, coagulation factor III; CRP, C-reactive protein; EWAS, epigenome wide association studies; ... histone acetyltransferase monocytic leukemia zinc finger protein (189), and DNMT3a (190), are observed in resting and activated ... followed by the action of histone acetyltransferases recruited by Pax5, allowing gene expression (181). Pax5 can also interact ...
carnitine acetyltransferase 19 what regulates the b-oxidation of fat malonyl coa ...
2004) Redesign of carnitine acetyltransferase specificity by protein engineering. Modification of methionine564 broadens the ... 2003) Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA ...
The shortest acylcarnitine, acetylcarnitine, is synthesized from acetyl-CoA and carnitine by carnitine acetyltransferase (CrAT ... 2014) Obesity and lipid stress inhibit carnitine acetyltransferase activity. J Lipid Res 55(4):635-644. ... 2012) Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. Cell ... Acetyl-carnitine is of particular interest because it has been hypothesized to control the fate of acetyl-CoA during substrate ...
Rabbit polyclonal Choline Acetyltransferase antibody - C-terminal. Validated in WB and tested in Mouse, Rat. Cited in 1 ... Belongs to the carnitine/choline acetyltransferase family.. * Target information above from: UniProt accession P28329. The ... Anti-Choline Acetyltransferase antibody - C-terminal. See all Choline Acetyltransferase primary antibodies. ... Protein - Recombinant Rat Choline Acetyltransferase protein (ab119467) IHC-Fr, Blocking Secondary - Goat Anti-Rabbit IgG H&L ( ...
Buy our Choline Acetyltransferase peptide (736-748). Ab45678 is a blocking peptide for ab27484 and has been validated in BL. ... Belongs to the carnitine/choline acetyltransferase family.. * Target information above from: UniProt accession P28329. The ... Choline Acetyltransferase peptide (736-748). See all Choline Acetyltransferase proteins and peptides. ...
Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal Biochem J (May, 2004) ... carnitine and carnitine acetyltransferase for subsequent monitoring of the formation of propionylcarnitine and ... carnitine acetyltransferase; radio-HPLC, HPLC with radiochemical detection; ESI-MS/MS, electrospray ionization tandem MS. ...
Carnitine O-acetyltransferase. An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC ... Arginine and Carnitine Metabolites Are Altered in Diabetic Retinopathy.. 08:00 EDT 1st July 2019 , BioPortfolio ... Summary of "Arginine and Carnitine Metabolites Are Altered in Diabetic Retinopathy.". To determine plasma metabolite and ... Home » Topics » Diabetes » Research » Arginine and Carnitine Metabolites Are Altered in Diabetic Retinopathy. ...
... carnitine acetyltransferase; ECE, endothelin-converting enzyme-1; NOX, nicotinamide adenine dinucleotide phosphate oxidase; and ... Histone acetyltransferase is opposite the histone deacetylase action. In addition, lysine deacetylases (KDAC) enzymes are ...
IPR023213 Chloramphenicol acetyltransferase-like domain superfamily. IPR039551 Choline/carnitine acyltransferase domain. ... J:79496 Price N, et al., A novel brain-expressed protein related to carnitine palmitoyltransferase I. Genomics. 2002 Oct;80(4): ...
  • The role of carnitine acetyltransferase (CrAT) in regulating cardiac energy metabolism is poorly understood. (biochemj.org)
  • This gene encodes carnitine O-acetyltransferase, a member of the carnitine acyltransferase family and a key metabolic pathway enzyme which plays an important role in energy homeostasis and fat metabolism. (nih.gov)
  • Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism. (nih.gov)
  • Carnitine in intermediary metabolism. (springer.com)
  • The metabolism of fatty acid esters of carnitine by mitochondria. (springer.com)
  • Carnitine is an essential factor in fatty acid metabolism in mammals. (hmdb.ca)
  • Inborn errors of carnitine metabolism can lead to brain deterioration like that of Reye's syndrome, gradually worsening muscle weakness, Duchenne-like muscular dystrophy and extreme muscle weakness with fat accumulation in muscles. (hmdb.ca)
  • In all these conditions and the inborn errors of carnitine metabolism, carnitine is essential to life and carnitine supplements are valuable. (hmdb.ca)
  • Toxicity of cephaloridine to carnitine transport and fatty acid metabolism in rabbit renal cortical mitochondria: structure-activity relationships. (aspetjournals.org)
  • Role of carnitine acetyltransferases in acetyl coenzyme A metabolism in Aspergillus nidulans. (semanticscholar.org)
  • Alterations in the expression of genes involved in fatty acid metabolism, such as carnitine O-acetyltransferase, are often associated with metabolic syndrome and insulin resistance. (qiagen.com)
  • Muoio said these results strongly imply that carnitine and the CrAT enzyme work together to optimize muscle energy metabolism during exercise. (newswise.com)
  • Effects of acetyl-L-carnitine and myoinositol on high-energy phosphate and membrane phospholipid metabolism in zebra fish: a 31P-NMR-spectroscopy study // Neurochem Res. (medi.ru)
  • Although carnitine metabolism appears comparable in patients with type 1 diabetes and healthy control subjects ( 2 ), it is not known whether IMAC is related to variations in fuel metabolism observed during exercise under differing glycemic levels in type 1 diabetes ( 3 ). (diabetesjournals.org)
  • ENGLISH ABSTRACT: Carnitine plays an essential role in eukaryotic metabolism by mediating the shuttling of activated acyl residues between intracellular compartments. (sun.ac.za)
  • Reversible acetylation of carnitine by mitochondria. (springer.com)
  • The following was found: 1) both cephalosporins reduced carnitine-facilitated pyruvate oxidation (CFPO) and palmitoylcarnitine-mediated respiration (PCMR) by 40 to 50% in mitochondria exposed in vivo (300 mg/kg b.wt. (aspetjournals.org)
  • The protein encoded by this gene, a member of the carnitine/choline acetyltransferase family, is the rate-controlling enzyme of the long-chain fatty acid beta-oxidation pathway in muscle mitochondria. (genecards.org)
  • An acetyl group is transferred from acetyl co-enzyme A (CoA) to L-carnitine within cell mitochondria during strenuous exercise, primarily in the liver and kidneys. (xtend-life.com)
  • The acetyl L-carnitine is then transported outside the mitochondria, where it provides chemical energy when it breaks back down into L-carnitine and an acetyl group. (xtend-life.com)
  • The L-carnitine is then transported back to the mitochondria to repeat the cycle. (xtend-life.com)
  • Gerbling, H., Gerhardt, B. (1988) Carnitine acyltransferase activity of mitochondria from mung bean hypocotyls. (springer.com)
  • Ames has already carried out research on rats which showed that they responded to treatment with an antioxidant, alpha-lipoic acid, and another substance, acetyl-L-carnitine, that binds to an important enzyme in the energy-producing organs of each cell, the mitochondria. (newmediaexplorer.org)
  • Some readers may be familiar with the amino acid carnitine, which carries fatty acids into the mitochondria (the cellular furnaces), where they are oxidised for energy. (naturalsolutionsradio.com)
  • One of the main roles of acetyl L-carnitine (ALC) is to carry fatty acids from the cytosol (the main body of the cell) into the mitochondria (the energy-producing furnaces within cells) so that these fats can be oxidised for energy. (naturalsolutionsradio.com)
  • The addition of the acetyl group also endows acetyl L-carnitine (ALC) with a greater solubility in water, which enables it not only to diffuse easily across the inner wall of the mitochondria and into the cell cytosol, but also cross cell membranes in general more easily. (naturalsolutionsradio.com)
  • Muoio and colleagues focused on a metabolic enzyme called carnitine acetyltransferase, or CrAT, which uses the micronutrient carnitine to boost the energy economy within mitochondria, the tiny engines of cells. (newswise.com)
  • Moreover, a decreased activity of carnitine acetyltransferase, an enzyme present in peroxisome (but also detected in mitochondria, endoplasmic reticulum, and nucleus), was reported in AD patients. (j-alz.com)
  • Other names in common use include acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine transferase, carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, and CATC. (wikipedia.org)
  • Carnitine acetylase is specific for short chain fatty acids. (nih.gov)
  • Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. (nih.gov)
  • Carnitine acetylase. (expasy.org)
  • The enzyme carnitine O-acetyltransferase is also needed to catalyze this reaction. (xtend-life.com)
  • Because the supply of carnitine in the diet and from synthesis is limited, such patients readily develop carnitine deficiency as a result of the increased loss of acylcarnitine derivatives. (hmdb.ca)
  • carnitine deficiency is noted in abnormal liver function, renal dialysis patients, and severe to moderate muscular weakness with associated anorexia. (hmdb.ca)
  • CPT I is the key enzyme in the carnitine-dependent transport across the mitochondrial inner membrane and its deficiency results in a decreased rate of fatty acid beta-oxidation. (genecards.org)
  • Diseases associated with CPT1A include Carnitine Palmitoyltransferase I Deficiency and Carnitine Palmitoyltransferase Ii Deficiency, Infantile . (genecards.org)
  • A urine test can also indicate an acetyl-L-carnitine deficiency. (xtend-life.com)
  • Belongs to the carnitine/choline acetyltransferase family. (abcam.com)
  • This gene encodes a member of the carnitine/choline acetyltransferase family. (avivasysbio.com)
  • A peroxisomal-specific pathway for acetyl-CoA transport requiring peroxisomal carnitine acetyl transferase (CAT) activity has been identified in Magnaporthe grisea peroxisomes. (apsnet.org)
  • Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC 2.3.1.7) is an enzyme that encoded by the CRAT gene that catalyzes the chemical reaction acetyl-CoA + carnitine ⇌ {\displaystyle \rightleftharpoons } CoA + acetylcarnitine where the acetyl group displaces the hydrogen atom in the central hydroxyl group of carnitine. (wikipedia.org)
  • CPT1A (Carnitine Palmitoyltransferase 1A) is a Protein Coding gene. (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include identical protein binding and carnitine O-palmitoyltransferase activity . (genecards.org)
  • The facC gene of Aspergillus nidulans encodes an acetate-inducible carnitine acetyltransferase. (semanticscholar.org)
  • GO annotations related to this gene include transferase activity, transferring acyl groups and carnitine O-palmitoyltransferase activity . (genecards.org)
  • Modulation of myelin basic protein gene expression by acetyl-L-carnitine // Mol Neurobiol. (medi.ru)
  • Intestinal peroxisomes of goldfish (Carrassius auratus) - examination for hydrolase, dehydrogenase and carnitine acetyltransferase activities. (athabascau.ca)
  • We give an overview of the potential role of peroxisomes, especially in the part played by DHA, PLGN, carnitine, and carnitine-dependent peroxisomal enzymes, on the development of AD and DAT. (j-alz.com)
  • Carnitine acyltransferases catalyze the exchange of acyl groups between coenzyme A (CoA) and carnitine. (rcsb.org)
  • Human CPT1A, CPT1B, CPT2, CROT and CRAT are known to encode active carnitine acyltransferases. (nih.gov)
  • Endurance exercise training is known to increase fatty acid (FA) oxidation during exercise and to stimulate mRNA synthesis of mitochondrial carnitine acyltransferases in skeletal muscle. (springer.com)
  • Daily supplementation with acetyl L-carnitine may help support the central nervous system. (xtend-life.com)
  • There was already evidence that supplementation with acetyl L-carnitine (ALC) could reverse the age-related decline in mitochondrial activity in rats, increase fatty acid oxidation and boost general metabolic activity(2). (naturalsolutionsradio.com)
  • The mechanism of substrate inhibition of palmityl coenzyme A: Carnitine palmityltransferase by palmityl coenzyme A. (springer.com)
  • Although L-carnitine carries out this role too, acetyl L-carnitine (ALC) also provides acetyl groups, from which acetyl-coenzyme A (a key metabolic intermediate) can be regenerated, thereby facilitating the transport of metabolic energy and boosting mitochondrial activity. (naturalsolutionsradio.com)
  • However, vildagliptin also reduced levels of hepatic mRNA transcripts for farnesyl di-phosphate transferase (Fdft1), acetyl coenzyme A acyltransferase 1 (Acaa1), and carnitine palmitoyl transferase 1 (Cpt 1) in DIRKO mice. (diabetesjournals.org)
  • Thus, the two substrates of this enzyme are acetyl-CoA and carnitine, whereas its two products are CoA and O-acetylcarnitine. (wikipedia.org)
  • An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. (bioportfolio.com)
  • A marked increase of acylcarnitine excretion resulting in a reduction of the portion of short-chain acylcarnitines, other than acetylcarnitine, due to carnitine supplementation could be interpreted as a detoxifying function. (springer.com)
  • The mitochondrial β-oxidation of long-chain fatty acids is initiated by the sequential action of carnitine palmitoyltransferase (CPT) I (outer membrane and detergent labile) and II (inner membrane and detergent stable), together with carnitine carrier. (scbt.com)
  • Cephaloridine (Cld), the most widely studied nephrotoxic cephalosporin, has significant structural homology with carnitine, which facilitates the transport of long-chain fatty acids into the mitochondrial inner matrix. (aspetjournals.org)
  • Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (PubMed:9691089, PubMed:11350182, PubMed:14517221). (genecards.org)
  • L-carnitine has been reported to increase acetyl-CoA provision for fatty acid synthesis in the liver and for fatty acid and acetylcholine production in the brain (3,16), apparently through activation of the carnitine acetyltransferase pathway (3,16). (thefreedictionary.com)
  • Administration of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase (acetyl-CoA-carnitine -acetyltransferase, EC 2.3.1.7) in liver and kidney. (iisc.ac.in)
  • In humans, about 25% of carnitine is synthesized in the liver, kidney and brain from the amino acids lysine and methionine. (hmdb.ca)
  • carnitine supplements may be useful in many forms of toxic or metabolic liver disease and in cases of heart muscle disease. (hmdb.ca)
  • In WBC of middle aged untrained subjects, the mRNA content of the liver form of the carnitine palmitoyltransferase 1 (CPT1A) was stimulated 2-fold (placebo group) and 8-fold in the carnitine supplemented probands. (springer.com)
  • However, it is so important in providing energy to muscles including the heart-that some researchers are now recommending carnitine supplements in the diet, particularly for people who do not consume much red meat, the main food source for carnitine. (hmdb.ca)
  • Now, scientists from Monash University in Melbourne, Australia, have discovered yet another key player in the complex mechanism of weight maintenance: a protein called carnitine acetyltransferase (Crat). (thefreedictionary.com)
  • Thus, carnitine is an unusual amino acid and has different functions than most other amino acids, which are most usually employed by the body in the construction of protein. (hmdb.ca)
  • The encoded protein converts 4,8-dimethylnonanoyl-CoA to its corresponding carnitine ester. (avivasysbio.com)
  • Gamma-butyrobetaine dioxygenase catalyses the formation of L-carnitine from gamma-butyrobetaine, the last step in the L-carnitine biosynthesis pathway. (wikipedia.org)
  • In fungi, two systems for acetyl unit transport have been identified: a shuttle dependent on the carrier carnitine and a (peroxisomal) citrate synthase-dependent pathway. (asm.org)
  • In the carnitine-dependent pathway, carnitine acetyltransferases exchange the CoA group of acetyl-CoA for carnitine, thereby forming acetyl-carnitine, which can be transported between subcellular compartments. (asm.org)
  • Site-directed mutagenesis of the His residues of the rat mitochondrial carnitine/acylcarnitine carrier: implications for the role of His-29 in the transport pathway. (semanticscholar.org)
  • 12 Carnitine O-Acetyltransferase (CRAT) ELISA Kits from 6 manufacturers are available on www.antibodies-online.com. (antibodies-online.com)
  • Obesity and lipid stress inhibit carnitine acetyltransferase activity. (nih.gov)
  • Development changes in spermatogenesis, testicular carnitine acetyltransferase activity and serum testosterone in the ram. (thefreedictionary.com)
  • TMP treatment caused a 20 percent reduction in cauda epididymal spermatozoa carnitine- acetyltransferase activity. (cdc.gov)
  • In addition to its use in storing and transporting chemical energy, acetyl-L-carnitine has significant antioxidant activity. (xtend-life.com)
  • In addition to its role in mitochondrial activity, acetyl L-carnitine (ALC) is involved in the production of the key brain neurotransmitter acetylcholine and is also able to donate its acetyl group in a number of other biochemical reactions. (naturalsolutionsradio.com)
  • To date, the only reported metabolic and physiological roles for carnitine in Saccharomyces cerevisiae are related to the activity of the carnitine shuttle. (sun.ac.za)
  • Carnitine Acetyltransferase Mitigates Metabolic Inertia and Muscle Fatigue during Exercise. (nih.gov)
  • Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. (nih.gov)
  • Muoio said the short-term goal is to determine whether carnitine supplementation enhances the benefits of exercise training in older individuals at risk of metabolic disease. (newswise.com)
  • Neural dysfunction and metabolic imbalances in diabetic rats: prevention by acetyl-L-carnitine // Diabetes. (medi.ru)
  • Both residues are replaced by glycine in carnitine palmitoyltransferases. (rcsb.org)
  • Furthermore, host 2 is able to act as a fluorescence displacement sensor for discriminating choline, acetylcholine, l-carnitine, and glycine betaine effectively. (osti.gov)
  • Biochemicals that inhibit Carnitine Acetyltransferase have many applications in biochemical and physiological research. (scbt.com)
  • This enzyme catalyzes the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine and regulates the ratio of acyl-CoA/CoA. (nih.gov)
  • Because of this homology, and evidence of a role of lipids in cephaloglycin (Cgl) nephrotoxicity, protocols were designed to compare the effects of Cld and Cgl on renal cortical mitochondrial carnitine transport, on long-chain fatty acylcarnitine-mediated respiration and on the in situ mitochondrial pools and urinary excretion of carnitine and acylcarnitines. (aspetjournals.org)
  • Functional characterization of residues within the carnitine/acylcarnitine translocase RX2PANAAXF distinct motif. (semanticscholar.org)
  • Identification by site-directed mutagenesis of a hydrophobic binding site of the mitochondrial carnitine/acylcarnitine carrier involved in the interaction with acyl groups. (semanticscholar.org)
  • Site-directed mutagenesis of charged amino acids of the human mitochondrial carnitine/acylcarnitine carrier: insight into the molecular mechanism of transport. (semanticscholar.org)
  • Structural information on carnitine acetyltransferase suggests that residues Met-564 and Phe-565 may be important determinants of substrate selectivity with the side chain of Met-564 located in the putative binding pocket for acyl groups. (rcsb.org)
  • A 5-fold increase of the muscle form of carnitine palmitoyltransferase 1 (CPT1B), a 4-fold increase in carnitine acetyltransferase (CRAT), and a 6-fold increase in the mRNA content of the main carnitine carrier OCTN2 in the muscles of the athletes were determined by reverse transcription quantitative real time polymerase chain reaction (RTPCR). (springer.com)
  • Carnitine has been described as a vitamin, an amino acid, or a metabimin, i.e., an essential metabolite. (hmdb.ca)
  • Like the other amino acids used or manufactured by the body, carnitine is an amine. (hmdb.ca)
  • Acetyl L-carnitine is an amino acid that is an acetylated derivative of L-carnitine. (xtend-life.com)
  • Acetyl-L-Carnitine (ALC) is a naturally occurring form of L-Carnitine, a vitamin-like nutrient synthesized in the body from the amino acids lysine and methionine. (vitanetonline.com)
  • As its name suggests, acetyl L-carnitine (ALC) is very similar, consisting of the same basic amino acid structure, with an acetyl group attached. (naturalsolutionsradio.com)
  • These channels are utilized by the substrates of CRAT, one channel for carnitine, and one for CoA. (wikipedia.org)
  • We have determined the crystal structure of the F565A mutant in a ternary complex with both the carnitine and CoA substrates at a 1.8-A resolution. (rcsb.org)
  • It catalyses the following reaction: 4-trimethylammoniobutanoate (γ-butyrobetaine) + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } 3-hydroxy-4-trimethylammoniobutanoate (L-carnitine) + succinate + CO2 The three substrates of this enzyme are 4-trimethylammoniobutanoate (γ-butyrobetaine), 2-oxoglutarate, and O2, whereas its three products are 3-hydroxy-4-trimethylammoniobutanoate (L-carnitine), succinate, and carbon dioxide. (wikipedia.org)
  • Gamma-butyrobetaine dioxygenase is promiscuous in substrate selectivity and it processes a number of modified substrates, including the natural catalytic products L-carnitine and D-carnitine, forming 3-dehydrocarnitine and trimethylaminoacetone. (wikipedia.org)
  • Xenopus tropicalis carnitine O-acetyltransferase b (crat), mRNA. (genscript.com)
  • In the second trial of 24 middle aged untrained (12 placebo and 12 carnitine supplemented) probands the mRNA expression was determined at the beginning and after three months of a low intensity endurance training program. (springer.com)
  • The relative abundances of CPT1B mRNA were increased by a factor of 3 (placebo) and 5 (carnitine supplemented), respectively. (springer.com)
  • The mRNA abundances of OCTN2 increased 5-fold (placebo) and 7-fold (carnitine supplemented). (springer.com)
  • The biosynthesis of L-carnitine in eukaryotic organisms was first elucidated in the ascomycete Neurospora crassa. (sun.ac.za)
  • Athletes, particularly in Europe, have used carnitine supplements for improved endurance. (hmdb.ca)
  • Even the Physician's Desk Reference gives indication for carnitine supplements as "improving the tolerance of ischemic heart disease, myocardial insufficiencies, and type IV hyperlipoproteinemia. (hmdb.ca)
  • Athletes are one of the groups most likely to need acetyl-L-carnitine supplements, especially if they are distance runners or bodybuilders. (xtend-life.com)
  • Over the last 18 months, scientific interest in alpha lipoic acid (ALA) and acetyl L-carnitine (ALC), the two supplements used in the studies, has exploded and a large number of studies are now under way with humans. (naturalsolutionsradio.com)
  • This work is not meant to imply that everyone should be taking carnitine supplements," Muoio said. (newswise.com)
  • Known as a global leader in L-Carnitine research, Sigma Tau holds numerous patents for production of L-Carnitine, and its L-Carnitine derivatives, such as ALC, which are used in clinical trials. (vitanetonline.com)
  • Malaguarnera M. Carnitine derivatives: clinical usefulness // Curr Opin Gastroenterol. (medi.ru)
  • While the plasma carnitine levels also remained low during the study period in athletes, normal levels were determined in untrained subjects and significantly increased levels were found after carnitine supplementation. (springer.com)
  • Synthetic peptide corresponding to Rat Choline Acetyltransferase aa 600 to the C-terminus conjugated to keyhole limpet haemocyanin. (abcam.com)
  • l-Carnitine plays a well-documented role in eukaryotic energy homeostasis by acting as a shuttling molecule for activated acyl residues across intracellular membranes. (sun.ac.za)