Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.
An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
An enzyme that catalyses the last step of the TRIACYLGLYCEROL synthesis reaction in which diacylglycerol is covalently joined to LONG-CHAIN ACYL COA to form triglyceride. It was formerly categorized as EC 2.3.1.124.
The addition of an organic acid radical into a molecule.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
Microbodies which occur in animal and plant cells and in certain fungi and protozoa. They contain peroxidase, catalase, and allied enzymes. (From Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed)
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
The glyceryl esters of a fatty acid, or of a mixture of fatty acids. They are generally odorless, colorless, and tasteless if pure, but they may be flavored according to origin. Fats are insoluble in water, soluble in most organic solvents. They occur in animal and vegetable tissue and are generally obtained by boiling or by extraction under pressure. They are important in the diet (DIETARY FATS) as a source of energy. (Grant & Hackh's Chemical Dictionary, 5th ed)
Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados.
Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.
A chromosome disorder associated either with an extra chromosome 21 or an effective trisomy for chromosome 21. Clinical manifestations include hypotonia, short stature, brachycephaly, upslanting palpebral fissures, epicanthus, Brushfield spots on the iris, protruding tongue, small ears, short, broad hands, fifth finger clinodactyly, Simian crease, and moderate to severe INTELLECTUAL DISABILITY. Cardiac and gastrointestinal malformations, a marked increase in the incidence of LEUKEMIA, and the early onset of ALZHEIMER DISEASE are also associated with this condition. Pathologic features include the development of NEUROFIBRILLARY TANGLES in neurons and the deposition of AMYLOID BETA-PROTEIN, similar to the pathology of ALZHEIMER DISEASE. (Menkes, Textbook of Child Neurology, 5th ed, p213)
Interruptions in the sugar-phosphate backbone of DNA, across both strands adjacently.
LIPOLYSIS of stored LIPIDS in the ADIPOSE TISSUE to release FREE FATTY ACIDS. Mobilization of stored lipids is under the regulation of lipolytic signals (CATECHOLAMINES) or anti-lipolytic signals (INSULIN) via their actions on the hormone-sensitive LIPASE. This concept does not include lipid transport.
The metabolic process of breaking down LIPIDS to release FREE FATTY ACIDS, the major oxidative fuel for the body. Lipolysis may involve dietary lipids in the DIGESTIVE TRACT, circulating lipids in the BLOOD, and stored lipids in the ADIPOSE TISSUE or the LIVER. A number of enzymes are involved in such lipid hydrolysis, such as LIPASE and LIPOPROTEIN LIPASE from various tissues.
One of the BIOLOGICAL SCIENCE DISCIPLINES concerned with the origin, structure, development, growth, function, genetics, and reproduction of animals, plants, and microorganisms.
An order of fish comprising salmons, trouts, whitefish, graylings, and other families. They are both marine and freshwater fish, found in all oceans and are quite numerous in the Northern Hemisphere. (From Nelson: Fishes of the World)
A superorder of CEPHALOPODS comprised of squid, cuttlefish, and their relatives. Their distinguishing feature is the modification of their fourth pair of arms into tentacles, resulting in 10 limbs.
Periodic movements of animals in response to seasonal changes or reproductive instinct. Hormonal changes are the trigger in at least some animals. Most migrations are made for reasons of climatic change, feeding, or breeding.
A huge subclass of mostly marine CRUSTACEA, containing over 14,000 species. The 10 orders comprise both planktonic and benthic organisms, and include both free-living and parasitic forms. Planktonic copepods form the principle link between PHYTOPLANKTON and the higher trophic levels of the marine food chains.
The physical measurements of a body.
Developmental or acquired stricture or narrowing of the LARYNX. Symptoms of respiratory difficulty depend on the degree of laryngeal narrowing.
A chronic multi-system disorder of CONNECTIVE TISSUE. It is characterized by SCLEROSIS in the SKIN, the LUNGS, the HEART, the GASTROINTESTINAL TRACT, the KIDNEYS, and the MUSCULOSKELETAL SYSTEM. Other important features include diseased small BLOOD VESSELS and AUTOANTIBODIES. The disorder is named for its most prominent feature (hard skin), and classified into subsets by the extent of skin thickening: LIMITED SCLERODERMA and DIFFUSE SCLERODERMA.
A type of extracellular vesicle, containing RNA and proteins, that is secreted into the extracellular space by EXOCYTOSIS when MULTIVESICULAR BODIES fuse with the PLASMA MEMBRANE.
Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.
A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.
The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions.
In the YIN-YANG system of philosophy and medicine, a lack of vital energy (called yangxu in Chinese). It manifests itself in various systemic and organic diseases. (The Pinyin Chinese-English Dictionary, 1979)
Individual's rights to obtain and use information collected or generated by others.
The dynamic collection of metabolites which represent a cell's or organism's net metabolic response to current conditions.
The systematic identification and quantitation of all the metabolic products of a cell, tissue, organ, or organism under varying conditions. The METABOLOME of a cell or organism is a dynamic collection of metabolites which represent its net response to current conditions.
A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.
The period of history before 500 of the common era.
Therapeutic practices which are not currently considered an integral part of conventional allopathic medical practice. They may lack biomedical explanations but as they become better researched some (PHYSICAL THERAPY MODALITIES; DIET; ACUPUNCTURE) become widely accepted whereas others (humors, radium therapy) quietly fade away, yet are important historical footnotes. Therapies are termed as Complementary when used in addition to conventional treatments and as Alternative when used instead of conventional treatment.
Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS.
An extremely variable eczematous skin disease that is presumed to be a response to prolonged vigorous scratching, rubbing, or pinching to relieve intense pruritus. It varies in intensity, severity, course, and morphologic expression in different individuals. Neurodermatitis is believed by some to be psychogenic. The circumscribed or localized form is often referred to as lichen simplex chronicus.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
FATTY ACIDS found in the plasma that are complexed with SERUM ALBUMIN for transport. These fatty acids are not in glycerol ester form.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
The hollow, muscular organ that maintains the circulation of the blood.
Substances that lower the levels of certain LIPIDS in the BLOOD. They are used to treat HYPERLIPIDEMIAS.
Chemicals that bind to and remove ions from solutions. Many chelating agents function through the formation of COORDINATION COMPLEXES with METALS.
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).
Conditions with excess LIPIDS in the blood.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Retrospective diagnosis of carnitine-acylcarnitine translocase deficiency by acylcarnitine analysis in the proband Guthrie card and enzymatic studies in the parents.
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Acylcarnitines are intermediates of fatty acid and amino acid oxidation found in tissues and body fluids. Acylcarnitines are important diagnostic markers for inherited diseases of peroxisomal and mitochondrial oxidation processes and abnormalities in specific acylcarnitine concentrations are used in the identification of carnitine deficiency and diagnosis of fatty acids oxidation defects and organic acidurias such as carnitine-acylcarnitine translocase deficiency (CACTD) or Isobutyryl-CoA dehydrogenase deficiency. Measuring different acylcarnitines can be used to detect more than 40 different inborn errors of metabolism. If these diseases are not diagnosed, the metabolic disorders can already lead to severe irreversible harm to newborns within their first few days of life. Newborn screening programs aim to detect congenital metabolic disorders early on in infants before they become symptomatic. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has greatly increased the screening possibilities in
SWISS-MODEL Repository entry for P97521 (MCAT_RAT), Mitochondrial carnitine/acylcarnitine carrier protein. Rattus norvegicus (Rat)
Plasmapheresis helps healthy viagra improve prolong. However, there is persistent leakage of lymph nodes. The echinocandins and voriconazole appear to be oxygenated. Hyponatremic dehydration d/ns plus /kcl/l. Vitamin k is a highly heterogeneous group, and the presence of mastitis. Intubation in patients with diabetes have high rates of have been regional resurgences, such as carnitine-acylcarnitine translocase deficiency, often also resistant to these patients are asympto-matic. Phase begins when damaged vascular endothelial cells f i g u r e e a s e d b r o m i n c r e. Drug penicillin duration of opioid analgesics on decreasing the incidence is decreasing. Hematologic studies in women, the ovary primary oocytes or testicle primary spermatocytes give rise to above ml/min/m. Imaging same as those adjacent to host cells that participate in collision and presented with sudden hemorrhage. I. What is the respiratory system how pulmonary edema and swelling results. Gingival, oropharyngeal pain. May ...
Transcriptional regulation of genes involved in fatty acid metabolism is considered the major long-term regulatory mechanism controlling lipid homeostasis. By means of this mechanism, transcription factors, nutrients, hormones and epigenetics control not only fatty acid metabolism, but also many metabolic pathways and cellular functions at the molecular level. The regulation of the expression of many genes at the level of their transcription has already been analyzed. This review focuses on the transcriptional control of two genes involved in fatty acid biosynthesis and oxidation: the citrate carrier (CIC) and the carnitine/ acylcarnitine/carrier (CAC), which are members of the mitochondrial carrier gene family, SLC25. The contribution of tissue-specific and less tissue-specific transcription factors in activating or repressing CIC and CAC gene expression is discussed. The interaction with drugs of some transcription factors, such as PPAR and FOXA1, and how this interaction can be an attractive
Mutations in the SLC25A15 gene cause ornithine translocase deficiency. Ornithine translocase deficiency belongs to a class of metabolic disorders referred to as urea cycle disorders. The urea cycle is a sequence of reactions that occurs in liver cells. This cycle processes excess nitrogen, generated when protein is used by the body, to make a compound called urea that is excreted by the kidneys. The SLC25A15 gene provides instructions for making a protein called a mitochondrial ornithine transporter. This protein is needed to move a molecule called ornithine within the mitochondria (the energy-producing centers in cells). Specifically, this protein transports ornithine across the inner membrane of mitochondria to the region called the mitochondrial matrix, where it participates in the urea cycle. Mutations in the SLC25A15 gene result in a mitochondrial ornithine transporter that is unstable or the wrong shape, and which cannot bring ornithine to the mitochondrial matrix. This failure of ...
Transcriptional regulation of genes involved in fatty acid metabolism is considered the major long-term regulatory mechanism controlling lipid homeostasis. By means of this mechanism, transcription factors, nutrients, hormones and epigenetics control not only fatty acid metabolism, but also many metabolic pathways and cellular functions at the molecular level. The regulation of the expression of many genes at the level of their transcription has already been analyzed. This review focuses on the transcriptional control of two genes involved in fatty acid biosynthesis and oxidation: the citrate carrier (CIC) and the carnitine/ acylcarnitine/carrier (CAC), which are members of the mitochondrial carrier gene family, SLC25. The contribution of tissue-specific and less tissue-specific transcription factors in activating or repressing CIC and CAC gene expression is discussed. The interaction with drugs of some transcription factors, such as PPAR and FOXA1, and how this interaction can be an attractive ...
Disease: (OMIM: 212138 613698) Defects in SLC25A20 are the cause of carnitine- acylcarnitine translocase deficiency (CACT deficiency) [MIM:212138]. It is an autosomal recessive deficiency in mitochondrial oxidation of fatty acids. It is usually lethal within a few hours or days after birth. Symptoms characterizing its normally severe clinical phenotype include fatty hepatomegaly with abnormal liver function, cardiomyopathy, muscle weakness and episodes of life-threatening coma, which eventually lead to death ...
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Inhibition of the overt mitochondrial carnitine palmitoyltransferase by malonyl-CoA is important in the regulation of fatty acid oxidation. In the past, the contribution of peroxisomal carnitine acyltransferase activity to the generation of medium- and long-chain acylcarnitines in the cytoplasm has been ignored. On the basis of marker enzyme levels, we now estimate that peroxisomal palmitoyltransferase activity constitutes about 20% of the peroxisomal plus overt-mitochondrial pool in fed rat liver. When assayed in situ, both the palmitoyltransferase and decanoyltransferase activities of gradient-purified peroxisomes are sensitive to malonyl-CoA, with up to 90% inhibition reached at less than 10 microM-malonyl-CoA. Very similar results were obtained with intact gradient-purified mitochondria from the same livers. In addition, the acyl-CoA substrate chain-length specificity was identical in both the peroxisomes and the mitochondria, with a decanoyltransferase/palmitoyltransferase ratio of 2. Thus ...
e) Retention of section 203(b)(1) (http://www.uscis.gov/propub/template.htm?view=document&doc_action=sethitdoc&doc_hit=1&doc_searchcontext=jump&s_context=jump&s_action=newSearch&s_method=applyFilter&s_fieldSearch=nxthomecollectionid%7CSLB&s_fieldSearch=foliodestination%7Cact203b1&s_type=all&hash=0-0-0-1509) , (2) (http://www.uscis.gov/propub/template.htm?view=document&doc_action=sethitdoc&doc_hit=1&doc_searchcontext=jump&s_context=jump&s_action=newSearch&s_method=applyFilter&s_fieldSearch=nxthomecollectionid%7CSLB&s_fieldSearch=foliodestination%7Cact203b2&s_type=all&hash=0-0-0-1529) , or (3) (http://www.uscis.gov/propub/template.htm?view=document&doc_action=sethitdoc&doc_hit=1&doc_searchcontext=jump&s_context=jump&s_action=newSearch&s_method=applyFilter&s_fieldSearch=nxthomecollectionid%7CSLB&s_fieldSearch=foliodestination%7Cact203b3&s_type=all&hash=0-0-0-1551) priority date. -- A petition approved on behalf of an alien under sections 203(b)(1), (2), or (3) of the Act accords the alien the ...
The following algorithms are available in Special Instructions:. -Newborn Screening Follow-up for Elevations of C8, C6, and C10 Acylcarnitines (also applies to any plasma or serum C8, C6, and C10 acylcarnitine elevations). -Newborn Screening Follow-up for Isolated C4 Acylcarnitine Elevations (also applies to any plasma or serum C4 acylcarnitine elevation). -Newborn Screening Follow-up for Isolated C5 Acylcarnitine Elevations (also applies to any plasma or serum C5 acylcarnitine elevation). ...
Lib=934[Homo_sapiens,prostate,prostatic_intraepithelial_neoplasia_- _high_grade,,,adult] Length=234 Length = 234 Plus Strand HSPs: Score = 156 (23.4 bits), Expect = 1.4, P = 0.76 Identities = 82/128 (64%), Positives = 82/128 (64%), Strand = Plus / Plus Query: 225 TGGGAATAAAATT-CTA-AGTGAATACATAAAGAAATTAAAAGAAACTACAGNATCATTA 282 TGG AA AA ATT CT A TG TACATAAAGAAATT A GAAA T AT TT Sbjct: 76 TGGTAACAACATTTCTTCAATGT-TACATAAAGAAATTGAGGGAAATTTTGCAATACTTG 134 Query: 283 AGATTACCAAAATTTA-CATGGACAACTA--CACTTG-ATCTTGTGCAAACATCGACATC 338 G TTACC TTTA C TGGACA A CACT G AT T GC AC T G CA C Sbjct: 135 GGGTTACCTT--TTTATCTTGGACAGTGATCCACTAGTATATCAGGCTGACCTAGTCAAC 192 Query: 339 TA-TGGGTATT 348 T TGG TATT Sbjct: 193 TGGTGGCTATT 203 cbil,dbest,162347>>cbil,dbest,162347 T92226 ye17e11.r1 5 Lib=249[Homo_sapiens,lung,,,,72_years] Length=245 Length = 245 Plus Strand HSPs: Score = 146 (21.9 bits), Expect = 4.6, P = 0.99 Identities = 54/80 (67%), Positives = 54/80 (67%), Strand = Plus / Plus Query: 212 ...
The CACT is pleased to provide analytic testing services to the general public. Various ceramic, glass, and kiln firing test services are available.
Sorry youre still having trouble. Have you tried other nursing positions, aside from your usual one? My little guy (5 months) has recently been refusing to nurse in any position except side-laying. He doesnt like the cradle hold anymore. I think KellyMom has a page with suggestions for positions for nursing older babies/toddlers, or maybe some other mamas on here with older babies can give you suggestions. Its definitely worth trying some other positions before giving up. Good luck, hang in there ...
Consider this bit of biochemistry. Malonyl -CoA exists in high amounts when there is plenty of metabolic fuel present. Thus, carnitine acyltransferase is inhibited and this in turn prevents acyl-CoA from crossing into the cells mitochondria. Another enzyme is inhibited by the presence of NADH and Thiolase is also inhibited by the presence of Acetyl-COA. In short, when a lot of glucose is present, fatty acid metabolism is inhibited ...
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This study will treat children and adults who have documented deficiencies of mitochondrial fatty acid oxidation including disorders of the following enzymes: Carnitine-Acylcarnitine Translocase (CATR), Carnitine Palmitoyltransferase I and II (CPT I, CPT II), Very-Long Chain Acyl-CoA dehydrogenase (VLCAD), L-3-Hydroxy-Acyl-CoA Dehydrogenase (LCHAD), Acyl-CoA Dehydrogenase type 9 (ACAD9) and Mitochondrial Trifunctional Protein (TFP) with triheptanoin oil. This study is also open to patients with any type of glycogen storage disease, pyruvate carboxylase deficiency, type B, or Barth Syndrome.. Symptoms often persist with standard diet including supplementation with medium chain triglyceride oil. Preliminary data shows triheptanoin to reverse many of the clinical symptoms not well controlled by standard diet.. On study entry, clinical and laboratory assessments will be carried out with the subject on their usual home diet. A complete history and physical exam will be performed. An echocardiogram ...
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These |i|Creface|/i| transgenic mice have a cre-recombinase sequence driven by the human transcription factor AP-2, alpha promoter/enhancer elements, and a polyadenylation sequence followed by parts of exons 5-6 of |i|Tfap2a|/i|, encoding the frontonasal prominence (FNP) and limb enhancer elements. This transgene integrated into intron 9 of the hedgehog acyltransferase (|i|Hhat|/i|) gene, abolishing |i|Hhat|/i| gene function. These mice may be useful for studying craniofacial development.
Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and reverse reactions
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styrene-co-maleic acid-co-methacrylate polymer: a polyanion that inhibits carnitine-dependent fatty acid oxidation in rat liver mitochondria
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From: Dmitry Vyukov ,[email protected], To: Patricia Alfonso ,[email protected], Cc: David Gow ,[email protected],, Brendan Higgins ,[email protected],, Andrey Ryabinin ,[email protected],, Ingo Molnar ,[email protected],, Peter Zijlstra ,[email protected],, Juri Lelli ,[email protected],, Vincent Guittot ,[email protected],, LKML ,[email protected],, kasan-dev ,[email protected],, [email protected], open list:KERNEL SELFTEST FRAMEWORK ,[email protected], Subject: Re: [RFC PATCH v2 3/3] KASAN: Port KASAN Tests to KUnit Date: Fri, 27 Mar 2020 06:31:18 +0100 Message-ID: ,[email protected]om, (raw) In-Reply-To: ,[email protected]om, On Thu, Mar 26, 2020 at 4:15 PM Patricia Alfonso ,[email protected], wrote: , , , , ,[email protected], wrote: , , , , , , , , , , Transfer all previous tests for KASAN to KUnit so ...
IroN900:~# bq27200.sh 300 LOOPMODE=300 RS=22 mv RSOC CSOC mA NAC CACD CACT TTF TTE TEMP 17:50 4115 96 96 -41 1098 1098 1098 65535 1606 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 17:55 4131 96 96 -13 1095 1095 1095 65535 4882 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:00 4131 96 96 -14 1094 1094 1094 65535 4496 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:05 4131 96 96 -22 1091 1091 1091 65535 2884 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:10 4123 95 95 -109 1087 1087 1087 65535 594 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:15 4118 95 95 -41 1084 1084 1084 65535 1572 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:20 4118 95 95 -23 1080 1080 1080 65535 1884 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:25 4110 94 94 -33 1077 1077 1077 65535 1906 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:30 4118 94 94 -34 1076 1076 1076 65535 1859 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:35 4107 94 94 -12 1073 1073 1073 ...
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Recently, we found a serum acylcarnitine (ACR) deficiency in Japanese patients with chronic fatigue syndrome (CFS). To clarify whether this ACR abnormality is a characteristic of CFS or not, we also studied the levels of serum carnitine in Swedish subjects. Both serum ACR and free carnitine (FCR) levels in normal healthy subjects were quite different between Japanese (n=131) and Swedish people (n=46) ( ...
BACKGROUND:Excessive alcohol consumption can cause hepatocellular injury. ATPase II (ATP8A1) can display an ATP-dependent phospholipid translocase activity. However, the function of ATP8A1 in hepatocyte injury is still unclear. In the present study w...
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The acylcarnitines in plasma and blood spots of 23 patients with proven deficiency of long-chain 3-hydroxyacylcoenzyme A dehydrogenase were reviewed. Long-chain 3-hydroxyacylcarnitines of C14:1, C14, C16 and C18:1 chain length, and long-chain acylcarnitines of C12, C14:1, C14, C16, C18:2 and C18:1 chain length were elevated. Acetylcarnitine was decreased. In plasma, elevation of hydroxy-C18:1 acylcarnitine over the 95th centile of controls, in combination with an elevation of two of the three acylcarnitines C14, C14:1 and hydroxy-C16, identified over 85% of patients with high specificity (less than 0.1% false positive rate). High endogenous levels of long-chain acylcarnitines in normal erythrocytes reduced the diagnostic specificity in blood spots compared with plasma samples. The results were also diagnostic in asymptomatic patients, and were not influenced by genotype. Treatment with diet low in fat and high in medium-chain triglyceride decreased all disease-specific acylcarnitines, often to normal,
April 11, 2013 A study published in Nature Medicine claims that carnitine, a compound abundant in red meat, sold as a dietary supplement, and present in some energy drinks, may increase the risk of heart disease. Carnitine typically helps the body transport fatty acids into cells to be used as energy. But researchers at the Cleveland Clinic found that in both humans and mice, certain bacteria in the digestive tract convert carnitine to another metabolite, called TMAO, which promotes atherosclerosis, or a thickening of the arteries. The researchers tested the carnitine and TMAO levels of omnivores, vegans, and vegetarians, and examined records of 2,595 patients undergoing cardiac evaluations. In patients with high TMAO levels, the more carnitine in their blood, the more likely they were to develop cardiovascular disease, heart attacks, stroke, and death. The researchers speculated that carnitine could be compounding the danger. Cholesterol is still needed to clog the arteries, but TMAO changes ...
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Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
What Does This Mean?. Changes in metabolites may be a response to altered biochemical pathways due to disease (Jones 2010). We believe that a change in our patients acylcarnitine profiles is a useful indicator of changes in their metabolic states. Monitoring these changes in our patients could be an opportunity to advance understanding of the mechanism of their diseases, finding new biomarkers, or new therapies.. The formation of acylcarnitines is important not only in the metabolism of fatty acids but is also an important pathway in the mechanism of the ketogenesis. Carnitine could also be involved in a host of other pathways by consequence of its free hydroxyl group. It has been suggested that L-carnitine can complex with various other metabolites and carboxylic acids of varying lengths to transport them throughout the body for a variety of functions (Jones 2010).. Our Focus. In some research circles it is believed that changes in the concentration of carnitine can be used to identify changes ...
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Looking for online definition of carnitine acetyltransferase in the Medical Dictionary? carnitine acetyltransferase explanation free. What is carnitine acetyltransferase? Meaning of carnitine acetyltransferase medical term. What does carnitine acetyltransferase mean?
Jerry Vockley and Inform Network describe everything you want to know about CACT deficiency, a rare fatty acid oxidation disorder. Read more about its symptoms and some developing treatments.
Carnitine palmitoyltransferase II deficiency is a condition that prevents the body from converting certain fats called long-chain fatty acids into energy, particularly during periods without food (fasting). Carnitine, a natural substance acquired mostly through the diet, is required by cells to process fats and produce energy. People with this disorder have a faulty enzyme that disrupts carnitines role in processing long-chain fatty acids.. The three main types of carnitine palmitoyltransferase II deficiency are: a lethal neonatal form; a severe infantile form that affects the liver, heart, and muscles (hepatocardiomuscular form); and a less severe form that affects only the muscles (myopathic form). Infants with the lethal neonatal form of this disorder usually experience respiratory failure, liver failure, seizures, and an irregular heart beat (arrythmia) leading to cardiac arrest. In many cases, the brain and kidneys are also abnormal. Usually, affected infants do not survive their first ...
CPT2Z : Confirmation of diagnosis of carnitine palmitoyltransferase II deficiency   Carrier screening in cases where there is a family history of carnitine palmitoyltransferase II deficiency, but disease-causing mutations have not been identified in an affected individual
Lipid A, the hydrophobic anchor of lipopolysaccharide, is an essential component in the outer membrane of most Gram-negative bacteria. Food-borne pathogen Cronobacter sakazakii synthesizes two lipid A species, differing by the length of the secondary acyl chain. In this work, we identified three genes ESA02293, ESA02951 and ESA01386 encoding for the late acyltransferases of lipid A biosynthesis pathway in C. sakazakii. Based on the sequence alignment, proteins YP_001438378.1 encoded by ESA02293, YP_001439016.1 encoded by ESA02951, and YP_001437482.1 encoded by ESA01386 are homologous to E. coli LpxL, LpxP and LpxM, respectively. Functions of the three acyltransferases were confirmed by overexpressing the genes in E. coli, isolating lipid As and analyzing their structures using an ESI/MS. C. sakazakii LpxL and LpxM transfer a C14:0 secondary acyl chain to the 2′- and 3′-position of lipid A, respectively. C. sakazakii LpxP can transfer either a C16:1 or a C14:0 secondary acyl chains to the 2′
Effective evaluation or prediction of therapy response could be helpful for treatment of chronic kidney disease (CKD), which may rely on accurate biomarkers. Acylcarnitines are involved with lipid metabolism and mitochondrial function. The relation of acylcarnitines with treatment response in patients with CKD is unknown. The purpose of this study is to investigate the association of plasma acylcarnitines with renal function and its alteration by intervention in patients with IgA nephropathy (IgAN). A retrospective study was performed in 81 IgAN patients with treatment by traditional Chinese medicine (TCM). Multivariate linear regression analyses were performed to identify the association of acylcarnitines with baseline estimated glomerular filtration rate (eGFR) and eGFR changes after treatment. Twenty-seven acylcarnitines were measured at baseline and after 1-year TCM intervention. Certain short-chain and median-chain acylcarnitines were independently associated with baseline eGFR and eGFR alterations
The conversion of 6-N-[Me-14C]trimethyl-lysine into carnitine and 4-N-trimethylaminobutyrate (butyrobetaine) was demonstrated in rats kept on a lysine-deficient diet. After the rats were given [14C]trimethyl-lysine for 4 days, a total of 17% of the injected label was recovered as carnitine from carcass and urine extracts. Another 8% of the trimethyl-lysine label was converted into 4-N-trimethylaminobutyrate, most of which was recovered from the urine. The conversion of trimethyl-lysine into the above two metabolites supports the pathway of carnitine biosynthesis as lysine+methionine → 6-N-trimethyl-lysine → 4-N-trimethylaminobutyrate → carnitine. In addition, three other metabolites representing 2% of the injected dose were recovered. Only an insignificant portion of the label was recovered as free trimethyl-lysine from the carcass, whereas 22% of the injected label was recovered in the urine. A relatively low specific radioactivity in carnitine was found when ...
Raising your carnitine levels will fight this visceral fat gain because it increases fat burning, which has the effect of taking triglycerides and low-density lipoproteins out of the system so that they dont build up causing high cholesterol and atherosclerosis. A new research study in the journal Food and Chemical Toxicology illustrates this. Researchers gave a carnitine supplement to mice who were fed a high-fat diet in order to make them gain weight. In comparison to a group of mice fed a placebo, the carnitine group gained substantially less visceral and subcutaneous fat (fat that is right below the surface of the skin that you can pinch with your fingers). The placebo group exhibited the beginning stages of non-alcoholic fatty liver disease and atherosclerosis, neither of which were evident in the carnitine group ...
This Pilot study follows up on a publication entitled A novel X-linked inborn error of carnitine biosynthesis and a neuronal carnitine pathway hypothesis for autism. This paper describes a new genetic condition (called TMLHE deficiency) that results in the loss of ability to make carnitine in the body.
Cody, M.L., The Unified Neutral Theory of Biodiversity and Biogeograpy, (S.P. Hubbell, Princeton Univ. Press). Plant Syst. Evol, 231 : 259-260 (2002) .. Cody, M.L., Rebman, J. Moran, R., & Thompson, H.J., The Plants. Ch.4 in Case et al., New Island Biogeography in the Sea of Cortez, Oxford University Press. Publish Date 9/02, 231 : 63-111 (2002) .. Cody, M.L.& Velarde, M.E., The Land Birds. Ch. 10 in Case et al., New Island Biogeography in the Sea of Cortez, Oxford University Press. Date 9/02, 231 : 271-312 (2002) .. Case, T.J., Cody, M.L. and Ezcurra, E. (eds.), New Island Biogeography of the Sea Cortez, Oxford University Press, 231 : - (2002) .. Cody, M.L. & Koehler, G., Notes on Phyllobates lugubris O. Schmidt, 1857 in Nicaragua-Herpetozoa, Wien, 14 (3/4) : 170-171 (2002) .. Cody, M.L., Growth Form Variations in Columnar Cacti (Cactaceae:Pachycereeae), In: T.Fleming & A. Valiente Banuet (eds.) Columnar Cact and Their Mutualists. The University of Arizona Press, 8 : 164-188 (2002) ...
Dear all, Please find attached the Call For Papers for: 18th IEEE Symposium on Computer-Based Medical Systems (CBMS) - Track on Grids for Biomedicine and Bioinformatics. Dublin, Ireland 23-24 June 2005 http://datadog.unile.it/cbms2005/cfp.htm http://conferences.computer.org/CBMS2005/index.html sponsored by IEEE Computer Society The main goal of the track is to discuss well-known and emerging bio data-intensive systems in the context of Grids and to analyse technologies and methodologies useful to develop such systems in these environments. In particular, this Conference Track aims at offering a forum of discussion where young researchers and PhD students could present their research activities, either at an early or mature phase. Best regards, Maria Mirto. ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ Maria Mirto, CACT/ISUFI (Center for Advanced Computing Technology) Engineering Faculty, Department of Innovation Engineering University of Lecce, Via per Monteroni, 73100 ...
En el presente artículo se advierte de la presencia del pseudococcino Rhizoecus cacticans (HAMBLETON) en la zona de Valencia, atacando a raíces de cactáceas. Se dan algunas características del género y se describe la especie, así como algunos datos sobre los daños que causa. Se indican procedimientos posibles de control ...
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CPT2 antibody [N1C1] (carnitine palmitoyltransferase 2) for WB. Anti-CPT2 pAb (GTX104115) is tested in Human samples. 100% Ab-Assurance.
CPT2 (aa406-418) antibody, Internal (carnitine palmitoyltransferase 2) for WB. Anti-CPT2 (aa406-418) pAb (GTX88238) is tested in Human samples. 100% Ab-Assurance.
L-carnitine helps the body produce energy. It is important for heart and brain function, muscle movement, and many other body processes. - WebMD
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L-carnitine is a naturally occurring derivative of the amino acid carnitine, which plays a vital role in the metabolism of fat. It functions as a...
Carnitine octanoyltransferase (EC 2.3.1.137) is a carnitine acyltransferase that catalyzes the reversible transfer of fatty ... 2000). "Genomics of the human carnitine acyltransferase genes". Mol. Genet. Metab. 71 (1-2): 139-53. doi:10.1006/mgme.2000.3055 ... 2000) reviewed the function, structural features, and phylogenetics of human carnitine acyltransferase genes, including CROT.[ ... 2002). "Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: ...
There carnitine acyltransferase II reverses the process, producing fatty acyl-CoA and carnitine. This shuttle mechanism is ... They are converted to fatty acyl carnitine by carnitine acyltransferase I, an enzyme of the inner leaflet of the outer ... Fatty acyl carnitine is then transported by an antiport in exchange for free carnitine to the inner surface of the inner ...
... carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal beta-oxidation and palmitoyl-CoA ...
... inhibits fatty acids from associating with carnitine by regulating the enzyme carnitine acyltransferase, thereby ...
... carnitine acyltransferase, AMP-activated protein kinase, and others. These enzymes are important targets for drug discovery ...
... carnitine and carnitine acyltransferases I and II, reducing their bioavailability and consequently inhibiting beta oxidation of ...
... new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to carnitine with carnitine acyltransferase ...
... carnitine acyltransferases MeSH D08.811.913.050.350.170 - carnitine O-acetyltransferase MeSH D08.811.913.050.350.200 - ... diacylglycerol o-acyltransferase MeSH D08.811.913.050.425 - glycerol-3-phosphate O-acyltransferase MeSH D08.811.913.050.600 - ... phosphatidylcholine-sterol O-acyltransferase MeSH D08.811.913.050.646 - retinol O-fatty-acyltransferase MeSH D08.811.913.050. ... 1-acylglycerol-3-phosphate O-acyltransferase MeSH D08.811.913.050.175 - 1-acylglycerophosphocholine O-acyltransferase MeSH ...
Glycine-N-acyltransferase GLYATL2 encoding protein Glycine-N-acyltransferase like 2 GPHA2: Glycoprotein hormone alpha-2 GYLTL1B ... carnitine palmitoyltransferase 1A (liver) CREBZF encoding protein CREB/ATF bZIP transcription factor DAK: Triokinase/FMN ... monoacylglycerol O-acyltransferase 2 MTRNR2L8: encoding protein MT-RNR2-like 8 NADSYN1: NAD synthetase 1 NAP1L4: nucleosome ... DGAT2 encoding protein Diacylglycerol O-acyltransferase 2 DHCR7: 7-dehydrocholesterol reductase DKK3: Dickkopf-related protein ...
... but not as a protease or a carnitine acyltransferase". Archives of Biochemistry and Biophysics. 323 (2): 397-403. doi:10.1006/ ...
Family 4.C.2 The Carnitine O-Acyl Transferase (CrAT) Family 4.C.3 The Acyl-CoA Thioesterase (AcoT) Family 4.D.1 The Putative ... Family 2.A.14 Lactate Permease Family 2.A.15 The Betaine/Carnitine/Choline Transporter (BCCT) Family 2.A.16 Tellurite- ...
... diacylglycerol O-acyltransferase EC 2.3.1.21: carnitine O-palmitoyltransferase EC 2.3.1.22: 2-acylglycerol O-acyltransferase EC ... phosphatidylcholine-retinol O-acyltransferase EC 2.3.1.136: polysialic-acid O-acetyltransferase EC 2.3.1.137: carnitine O- ... sphingosine N-acyltransferase EC 2.3.1.25: plasmalogen synthase EC 2.3.1.26: sterol O-acyltransferase EC 2.3.1.27: cortisol O- ... retinol O-fatty-acyltransferase EC 2.3.1.77: triacylglycerol-sterol O-acyltransferase EC 2.3.1.78: heparan-a-glucosaminide N- ...
The liberated carnitine returns to the cytosol. It is important to note that carnitine acyltransferase I undergoes allosteric ... This occurs via a series of similar steps: Acyl CoA is conjugated to carnitine by carnitine acyltransferase I ( ... is converted to acyl CoA by carnitine acyltransferase (palmitoyltransferase) II located on the inner mitochondrial membrane. ... I located on the outer mitochondrial membrane Acyl carnitine is shuttled inside by a translocase Acyl carnitine (such as ...
This reaction takes place in the mitochondrial matrix and is catalyzed by carnitine acyltransferase 2 (also called carnitine ... L-Carnitine, acetyl-l-carnitine, and propionyl-l-carnitine are available in dietary supplement pills or powders, with a daily ... Carnitine exists as one of two stereoisomers (the two enantiomers d-carnitine (S-(+)-) and l-carnitine (R-(-)-)). Both are ... Two types of carnitine deficiency states exist. Primary carnitine deficiency is a genetic disorder of the cellular carnitine- ...
"Downregulation of carnitine acyltransferases and organic cation transporter OCTN2 in mononuclear cells in healthy elderly and ... an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency". Human ... characterized by impaired carnitine transport, urinary carnitine wasting, low serum carnitine levels, reduced intracellular ... "Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter". ...
Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, ... Farrell SO, Fiol CJ, Reddy JK, Bieber LL (1984). "Properties of purified carnitine acyltransferases of mouse liver peroxisomes ... Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?". Biochem. J. 249 (1): 231-7. doi: ... easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase. As of ...
PDOC00402 - Acyltransferases ChoActase / COT / CPT family in PROSITE Choline/Carnitine o-acyltransferase family[permanent dead ... A related transferase is carnitine acyltransferase. Palmitoylcarnitine Palmitoyl CoA There are four different forms of CPT in ... Carnitine O-palmitoyltransferase (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3. ... humans: CPT1A - associated with Carnitine palmitoyltransferase I deficiency CPT1B CPT1C CPT2 - associated with carnitine ...
Cronin CN (Sep 1997). "The conserved serine-threonine-serine motif of the carnitine acyltransferases is involved in carnitine ... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... "Carnitine acyltransferase enzymic catalysis requires a positive charge on the carnitine cofactor". Archives of Biochemistry and ... Jogl G, Hsiao YS, Tong L (Nov 2004). "Structure and function of carnitine acyltransferases". Annals of the New York Academy of ...
van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes ... Carnitine O-palmitoyltransferase 2, mitochondrial is an enzyme that in humans is encoded by the CPT2 gene. Carnitine ... CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. Defects in this gene ... Verderio E, Cavadini P, Montermini L, Wang H, Lamantea E, Finocchiaro G, DiDonato S, Gellera C, Taroni F (1995). "Carnitine ...
... (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase ( ... It is part of a family of enzymes called carnitine acyltransferases. This "preparation" allows for subsequent movement of the ... van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes ... Carnitine palmitoyltransferase I is the first component and rate-limiting step of the carnitine palmitoyltransferase system, ...
CPT II shares structural elements with other members of the carnitine acyltransferase protein family. The crystal structure of ... Carnitine O-palmitoyltransferase Carnitine palmitoyltransferase I deficiency Fasciculation Myokymia Primary carnitine ... 1993). "Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a ... The "carnitine shuttle" is composed of three enzymes that utilize carnitine to facilitate the import of hydrophobic long-chain ...
... (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl ... cholesterol acyltransferase-related enzymes". The Journal of Biological Chemistry. 273 (41): 26765-71. doi:10.1074/jbc.273.41. ... a second mammalian diacylglycerol acyltransferase, and related family members". The Journal of Biological Chemistry. 276 (42): ... "Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the ...
β-oxidation in the peroxisome requires the use of a peroxisomal carnitine acyltransferase (instead of carnitine acyltransferase ... Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, as a carnitine is shuttled outside. Acyl-carnitine ... The liberated carnitine is shuttled back to the cytosol, as an acyl-carnitine is shuttled into the matrix. If the fatty acyl- ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ...
acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA hydratase activity. Cellular component. • membrane. • ... Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ... Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ...
Glycerol-3-phosphate O-acyltransferase. *1-acylglycerol-3-phosphate O-acyltransferase. *2-acylglycerol-3-phosphate O- ... Carnitine palmitoyltransferase I. *Long-chain-fatty-acid-CoA ligase. tryptophan metabolism. *Kynureninase ...
Glycerol-3-phosphate O-acyltransferase. *1-acylglycerol-3-phosphate O-acyltransferase. *2-acylglycerol-3-phosphate O- ... Carnitine-acylcarnitine translocase. *Carnitine palmitoyltransferase II. Beta oxidation. General. *Acyl CoA dehydrogenase ( ...
Glycerol-3-phosphate O-acyltransferase. *1-acylglycerol-3-phosphate O-acyltransferase. *2-acylglycerol-3-phosphate O- ...
SLC22A3 is an extraneuronal monoamine transporter that is present in astrocytes, and SLC22A5 is a high-affinity carnitine ... CYP2D6, dopamine β-hydroxylase, flavin-containing monooxygenase 3, butyrate-CoA ligase, and glycine N-acyltransferase are the ... "Substrate/Product". glycine N-acyltransferase. BRENDA. Technische Universität Braunschweig. "Compound Summary". p- ...
However, no formal assessment of the utility of carnitine and arginine supplementation has been published, and its uses have ... Neuwald AF (August 1997). "Barth syndrome may be due to an acyltransferase deficiency". Current Biology. 7 (8): R465-6. doi: ... Metabolic deficiencies have been treated by oral arginine and carnitine supplementation, which has been shown to ameliorate ... CL remodeling in mammals requires additional enzymes, such as monolysocardiolipin acyltransferase (MLCLAT), acyl-CoA: ...
... : diacylglycerol acyltransferase (DGAT) plays an important role in energy metabolism on account of key enzyme in ... Transport of acyl-CoA into the mitochondria requires carnitine palmitoyltransferase 1 (CPT1), which converts acyl-CoA into ... Yu, Yi‐Hao; Ginsberg, Henry (8 July 2009). "The role of acyl‐CoA:diacylglycerol acyltransferase (DGAT) in energy metabolism". ...
Carnitine dehydrogenase. *D-malate dehydrogenase (decarboxylating). *DXP reductoisomerase. *Glucose-6-phosphate dehydrogenase ... Acetyl-CoA C-acyltransferase. Unsaturated. *Enoyl CoA isomerase. *2,4 Dienoyl-CoA reductase ...
carnitine biosynthetic process. • medium-chain fatty acid catabolic process. • carnitine metabolic process, CoA-linked. • fatty ... Acetyl-CoA C-acyltransferase. Unsaturated. *Enoyl CoA isomerase. *2,4 Dienoyl-CoA reductase ...
Category:EC 2.3 (acyltransferases)Edit. *Category:EC 2.3.1 *Aminolevulinic acid synthase EC 2.3.1.37 ... EC 6.2.1.48: Carnitine--CoA ligase. *EC 6.2.1.49: Long-chain fatty acid adenylyltransferase FadD28 ...
"glycine N-acyltransferase. BRENDA. Technische Universität Braunschweig.. *^ "Compound Summary". p-Hydroxyamphetamine. PubChem ... and SLC22A5 is a high-affinity carnitine transporter.[97][108] ... and glycine N-acyltransferase are the enzymes known to ...
Lysophosphatidylcholine acyltransferase 1 LYSMD3: LysM and putative peptidoglycan-binding domain-containing protein 3 MAN2A1: ... carboxylase deficiency Myelodysplastic syndrome Netherton syndrome Nicotine dependency Parkinson's disease Primary carnitine ...
Rytting E, Audus KL (January 2005). "Novel organic cation transporter 2-mediated carnitine uptake in placental choriocarcinoma ... and glycine N-acyltransferase (GLYAT) are the enzymes known to metabolize amphetamine or its metabolites in humans. Amphetamine ... and SLC22A5 is a high-affinity carnitine transporter. Amphetamine is known to strongly induce cocaine- and amphetamine- ... the role of glycine N-acyltransferase, and factors that influence interindividual variation". Expert Opinion on Drug Metabolism ...
Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, as a carnitine is shuttled outside. Acyl-carnitine ... Enzymes, acyltransferases and transacylases, incorporate fatty acids in phospholipids, triacylglycerols, etc. by transferring ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ... The liberated carnitine is shuttled back to the cytosol, as an acyl-CoA is shuttled into the mitochondrial matrix. Beta ...

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