A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC
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.
Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.
An enzyme that catalyzes the formation of acetylcholine from acetyl-CoA and choline. EC
An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC
An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.
Formation of an acetyl derivative. (Stedman, 25th ed)
A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
An enzyme that catalyzes the HYDROXYLATION of gamma-butyrobetaine to L-CARNITINE. It is the last enzyme in the biosynthetic pathway of L-CARNITINE and is dependent on alpha-ketoglutarate; IRON; ASCORBIC ACID; and OXYGEN.
A family of proteins involved in the transport of organic cations. They play an important role in the elimination of a variety of endogenous substances, xenobiotics, and their metabolites from the body.
An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
An N-terminal acetyltransferase subtype that consists of the Naa10p catalytic subunit and the Naa15p auxiliary subunit. The structure of this enzyme is conserved between lower and higher eukaryotes. It has specificity for N-terminal SERINE; ALANINE; THREONINE; GLYCINE; VALINE; and CYSTINE residues and acts on nascent peptide chains after the removal of the initiator METHIONINE by METHIONYL AMINOPEPTIDASES.
An N-terminal acetyltransferase subtype that consists of the Naa50p catalytic subunit, and the Naa10p and Naa15p auxiliary subunits. It has specificity for the N-terminal METHIONINE of peptides where the next amino acid in the chain is hydrophobic.
Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.
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.
A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.
A long-chain fatty acid ester of carnitine which facilitates the transfer of long-chain fatty acids from cytoplasm into mitochondria during the oxidation of fatty acids.
An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A verocytotoxin-producing serogroup belonging to the O subfamily of Escherichia coli which has been shown to cause severe food-borne disease. A strain from this serogroup, serotype H7, which produces SHIGA TOXINS, has been linked to human disease outbreaks resulting from contamination of foods by E. coli O157 from bovine origin.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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.
A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.
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 large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
A member of the p300-CBP transcription factor family that was initially identified as a binding partner for CAMP RESPONSE ELEMENT-BINDING PROTEIN. Mutations in CREB-binding protein are associated with RUBINSTEIN-TAYBI SYNDROME.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
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.
An essential amino acid. It is often added to animal feed.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
The rate dynamics in chemical or physical systems.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
An enzyme that transfers methyl groups from O(6)-methylguanine, and other methylated moieties of DNA, to a cysteine residue in itself, thus repairing alkylated DNA in a single-step reaction. EC
A member of the p300-CBP transcription factors that was originally identified as a binding partner for ADENOVIRUS E1A PROTEINS.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A condition due to deficiency in any member of the VITAMIN B COMPLEX. These B vitamins are water-soluble and must be obtained from the diet because they are easily lost in the urine. Unlike the lipid-soluble vitamins, they cannot be stored in the body fat.
Enzymes that catalyze the transfer of an acetyl group, usually from ACETYL COENZYME A, to the N-terminus of a peptide chain.
An N-terminal acetyltransferase subtype that consists of the Naa20p catalytic subunit and the Naa25p auxiliary subunit. The structure of this enzyme is conserved between YEASTS and HUMAN. It has specificity for the N-terminal METHIONINE of peptides where the next amino acid in the chain is either ASPARTATE; GLUTAMATE; ASPARAGINE; OR GLUTAMINE.
Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.
Established cell cultures that have the potential to propagate indefinitely.
A biogenic polyamine formed from spermidine. It is found in a wide variety of organisms and tissues and is an essential growth factor in some bacteria. It is found as a polycation at all pH values. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The metabolic substances ACETONE; 3-HYDROXYBUTYRIC ACID; and acetoacetic acid (ACETOACETATES). They are produced in the liver and kidney during FATTY ACIDS oxidation and used as a source of energy by the heart, muscle and brain.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
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).
Vesicular amine transporter proteins that transport the neurotransmitter ACETYLCHOLINE into small SECRETORY VESICLES. Proteins of this family contain 12 transmembrane domains and exchange vesicular PROTONS for cytoplasmic acetylcholine.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
Nerve fibers liberating acetylcholine at the synapse after an impulse.
Nucleic acid sequences involved in regulating the expression of genes.
A polyamine formed from putrescine. It is found in almost all tissues in association with nucleic acids. It is found as a cation at all pH values, and is thought to help stabilize some membranes and nucleic acid structures. It is a precursor of spermine.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A basic constituent of lecithin that is found in many plants and animal organs. It is important as a precursor of acetylcholine, as a methyl donor in various metabolic processes, and in lipid metabolism.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
A naturally occurring metabolite of HISTIDINE that has antioxidant properties.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
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.
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.
Lengthy and continuous deprivation of food. (Stedman, 25th ed)
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
BUTYRIC ACID substituted in the beta or 3 position. It is one of the ketone bodies produced in the liver.
The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.
Proteins prepared by recombinant DNA technology.
Cis-acting DNA sequences which can increase transcription of genes. Enhancers can usually function in either orientation and at various distances from a promoter.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.
Contractile tissue that produces movement in animals.
A form of encephalopathy with fatty infiltration of the LIVER, characterized by brain EDEMA and VOMITING that may rapidly progress to SEIZURES; COMA; and DEATH. It is caused by a generalized loss of mitochondrial function leading to disturbances in fatty acid and CARNITINE metabolism.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC
Nonsusceptibility of bacteria to the action of CHLORAMPHENICOL, a potent inhibitor of protein synthesis in the 50S ribosomal subunit where amino acids are added to nascent bacterial polypeptides.
A group of 6-alkyl SALICYLIC ACIDS that are found in ANACARDIUM and known for causing CONTACT DERMATITIS.
A fibric acid derivative used in the treatment of HYPERLIPOPROTEINEMIA TYPE III and severe HYPERTRIGLYCERIDEMIA. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986)
Genes whose expression is easily detectable and therefore used to study promoter activity at many positions in a target genome. In recombinant DNA technology, these genes may be attached to a promoter region of interest.
An enzyme that catalyses the reaction of D-glucosamine 6-phosphate with ACETYL-COA to form N-acetylglucosamine 6-phosphate.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
A group of 16-carbon fatty acids that contain no double bonds.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Genes which regulate or circumscribe the activity of other genes; specifically, genes which code for PROTEINS or RNAs which have GENE EXPRESSION REGULATION functions.
Transport proteins that carry specific substances in the blood or across cell membranes.
Salts and esters of the 16-carbon saturated monocarboxylic acid--palmitic acid.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Elements of limited time intervals, contributing to particular results or situations.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106)
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.
A phospholipid derivative formed by PLATELETS; BASOPHILS; NEUTROPHILS; MONOCYTES; and MACROPHAGES. It is a potent platelet aggregating agent and inducer of systemic anaphylactic symptoms, including HYPOTENSION; THROMBOCYTOPENIA; NEUTROPENIA; and BRONCHOCONSTRICTION.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. The enzyme family can be divided into at least three structurally-defined subclasses. Class I and class II deacetylases utilize a zinc-dependent mechanism. The sirtuin histone deacetylases belong to class III and are NAD-dependent enzymes.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
A mitochondrial matrix enzyme that catalyzes the synthesis of L-GLUTAMATE to N-acetyl-L-glutamate in the presence of ACETYL-COA.
The functional hereditary units of BACTERIA.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
Hydrazines substituted by one or more methyl groups in any position.
A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
A toxic thiol mercury salt formerly used as a diuretic. It inhibits various biochemical functions, especially in mitochondria, and is used to study those functions.
Derivatives of caprylic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated eight carbon aliphatic structure.
Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
Biogenic amines having more than one amine group. These are long-chain aliphatic compounds that contain multiple amino and/or imino groups. Because of the linear arrangement of positive charge on these molecules, polyamines bind electrostatically to ribosomes, DNA, and RNA.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
Salts and esters of hydroxybutyric acid.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
The mitochondria of the myocardium.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.
The repeating structural units of chromatin, each consisting of approximately 200 base pairs of DNA wound around a protein core. This core is composed of the histones H2A, H2B, H3, and H4.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Neurons whose primary neurotransmitter is ACETYLCHOLINE.
Tissue in the BASAL FOREBRAIN inferior to the anterior perforated substance, and anterior to the GLOBUS PALLIDUS and ansa lenticularis. It contains the BASAL NUCLEUS OF MEYNERT.
A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Proteins found in any species of bacterium.
A neurotransmitter found at neuromuscular junctions, autonomic ganglia, parasympathetic effector junctions, a subset of sympathetic effector junctions, and at many sites in the central nervous system.

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 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 activity measured in the same assay system in response to added l-carnitine was very low in normal rat liver homogenates, owing to the apparent high acetyl-CoA hydrolase activity, but was increased markedly after Sephadex treatment. The V(max.) for this enzyme in rat liver homogenates was increased from 3.4 to 14.8nmol/min per mg of protein whereas the K(m) for l-carnitine was decreased from 936 to 32mum after Sephadex treatment. 7. Acetyl-CoA hydrolase activity could be demonstrated in disrupted rat liver mitochondria but not in separated outer or inner mitochondrial membrane fractions. Activity could be demonstrated after recombination of outer and inner mitochondrial membrane fractions. The outer mitochondrial membrane fraction showed acetylcarnitine hydrolase activity and the inner mitochondrial membrane fraction showed carnitine acetyltransferase activity. 8. The results presented here demonstrate that acetyl-CoA hydrolase activity in rat and sheep liver is an artifact and the activity is due to the combined activity of carnitine acetyltransferase and acetylcarnitine hydrolase.  (+info)

Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. (8/91)

Carnitine acyltransferases have crucial roles in the transport of fatty acids for beta-oxidation. Dysregulation of these enzymes can lead to serious diseases in humans, and they are targets for therapeutic development against diabetes. We report the crystal structures of murine carnitine acetyltransferase (CRAT), alone and in complex with its substrate carnitine or CoA. The structure contains two domains. Surprisingly, these two domains share the same backbone fold, which is also similar to that of chloramphenicol acetyltransferase and dihydrolipoyl transacetylase. The active site is located at the interface between the two domains. Carnitine and CoA are bound in deep channels in the enzyme, on opposite sides of the catalytic His343 residue. The structural information provides a molecular basis for understanding the catalysis by carnitine acyltransferases and for designing their inhibitors. Specifically, our structural information suggests that the substrate carnitine may assist the catalysis by stabilizing the oxyanion in the reaction intermediate.  (+info)

1. Vitamin B1 (Thiamine): necessary for converting carbohydrates into energy
2. Vitamin B2 (Riboflavin): important for vision health and immune system function
3. Vitamin B3 (Niacin): crucial for energy production and skin health
4. Vitamin B5 (Pantothenic acid): involved in energy production, hormone production, and blood cell formation
5. Vitamin B6: essential for brain function, immune system function, and the synthesis of neurotransmitters
6. Vitamin B7 (Biotin): important for hair, skin, and nail health, as well as energy production
7. Vitamin B9 (Folic acid): crucial for fetal development during pregnancy
8. Vitamin B12: necessary for the production of red blood cells, nerve function, and DNA synthesis.

Vitamin B deficiencies can occur due to several factors, including:

* Poor diet or malnutrition
* Gastrointestinal disorders that impair nutrient absorption (e.g., celiac disease, Crohn's disease)
* Increased demand for vitamins during pregnancy and lactation
* Certain medications (e.g., antacids, proton pump inhibitors) that interfere with nutrient absorption
* Malabsorption due to pancreas or small intestine disorders
* Inherited disorders (e.g., vitamin B12 deficiency due to pernicious anemia)

Symptoms of vitamin B deficiencies can vary depending on the specific vitamin and the severity of the deficiency. Some common symptoms include fatigue, weakness, irritability, depression, skin problems, and impaired cognitive function. Treatment typically involves dietary modifications and supplementation with the appropriate vitamin. In severe cases, hospitalization may be necessary to address any underlying conditions or complications.

The following are some of the most common vitamin B deficiencies:

1. Vitamin B12 deficiency: This is one of the most common vitamin B deficiencies and can cause fatigue, weakness, pale skin, and neurological problems such as numbness or tingling in the hands and feet.
2. Vitamin B6 deficiency: This can cause skin problems, such as acne-like rashes, and neurological symptoms like confusion, convulsions, and weakness in the arms and legs.
3. Folate deficiency: This can cause fatigue, weakness, pale skin, and neurological problems such as memory loss and confusion.
4. Vitamin B2 (riboflavin) deficiency: This can cause cracked lips, skin around the mouth, and tongue, and eyes.
5. Niacin (vitamin B3) deficiency: This can cause pellagra, a condition characterized by diarrhea, dermatitis, and dementia.
6. Vitamin B5 (pantothenic acid) deficiency: This can cause fatigue, weakness, and neurological symptoms like headaches and dizziness.
7. Vitamin B1 (thiamine) deficiency: This can cause beriberi, a condition characterized by weakness, fatigue, and neurological problems such as confusion and memory loss.
8. Biotin deficiency: This is rare but can cause skin problems, such as seborrhea, and neurological symptoms like numbness and tingling in the hands and feet.
9. Vitamin B12 (cobalamin) deficiency: This is common in vegetarians and vegans who do not consume enough animal products, and can cause fatigue, weakness, and neurological problems such as numbness and tingling in the hands and feet.

It's important to note that these deficiencies can have a significant impact on your overall health and well-being, so it's essential to be aware of the signs and symptoms and take steps to ensure you are getting enough of these vitamins in your diet.

Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.

Types of Starvation:

There are several types of starvation, each with different causes and effects. These include:

1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.

Effects of Starvation on the Body:

Starvation can have severe effects on the body, including:

1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.

It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.

There are several types of inborn errors of lipid metabolism, each with its own unique set of symptoms and characteristics. Some of the most common include:

* Familial hypercholesterolemia: A condition that causes high levels of low-density lipoprotein (LDL) cholesterol in the blood, which can lead to heart disease and other health problems.
* Fabry disease: A rare genetic disorder that affects the body's ability to break down certain fats, leading to a buildup of toxic substances in the body.
* Gaucher disease: Another rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.
* Lipoid cerebral degeneration: A condition that causes fatty deposits to accumulate in the brain, leading to cognitive decline and other neurological problems.
* Tangier disease: A rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.

Inborn errors of lipid metabolism can be diagnosed through a variety of tests, including blood tests and genetic analysis. Treatment options vary depending on the specific disorder and its severity, but may include dietary changes, medication, and other therapies. With proper treatment and management, many individuals with inborn errors of lipid metabolism can lead active and fulfilling lives.

Symptoms of Reye Syndrome can include:

* Headache
* Confusion
* Vomiting
* Seizures
* Loss of consciousness
* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Abdominal pain

If you suspect that your child may have Reye Syndrome, it is important to seek medical attention immediately. The condition can be difficult to diagnose, as it can resemble other conditions such as meningitis or encephalitis. A healthcare provider will typically perform a physical examination, take a medical history, and order laboratory tests to confirm the diagnosis.

There is no specific treatment for Reye Syndrome, but the condition is usually managed with supportive care in a hospital setting. Treatment may include:

* Medication to control seizures
* Intravenous fluids and nutrition
* Monitoring of vital signs and liver function
* Antiviral medication in some cases

Reye Syndrome can be fatal if left untreated, so early diagnosis and aggressive management are crucial. The condition is rare, but it is important for parents and healthcare providers to be aware of the signs and symptoms in order to provide prompt and appropriate care.

Causes of Hyperammonemia:

1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.

Symptoms of Hyperammonemia:

1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting

Diagnosis of Hyperammonemia:

1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.

Treatment of Hyperammonemia:

1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.

Complications of Hyperammonemia:

1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.

In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.

... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC 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". McGarry JD, Brown NF (Feb 1997). "The mitochondrial carnitine ...
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 ...
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 ...
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 ...
"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 ...
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- ...
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 ...
... arylamine N-acetyltransferase EC choline O-acetyltransferase EC carnitine O-acetyltransferase EC ... D-tryptophan N-acetyltransferase EC glutamate N-acetyltransferase EC D-amino-acid N-acetyltransferase EC ... amino-acid N-acetyltransferase EC imidazole N-acetyltransferase EC glucosamine N-acetyltransferase EC ... glycine C-acetyltransferase EC serine O-acetyltransferase EC homoserine O-acetyltransferase EC ...
... 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 ...
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 ...
... may refer to: Instrument landing system#ILS categories Chloramphenicol O-acetyltransferase I, an enzyme Carnitine O- ...
... may refer to: Instrument landing system#ILS categories Chloramphenicol O-acetyltransferase II, an enzyme Carnitine O- ...
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. ...
"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 ...
... 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 Long-chain fatty acid adenylyltransferase FadD28 EC 4-hydroxybenzoate ... EC 2.3.1 Aminolevulinic acid synthase EC Choline acetyltransferase EC Category:EC 2.3.2 Factor XIII EC 2.3. ...
L-carnitine CoA-transferase and EC, crotonobetainyl-CoA hydratase EC L-rhamnonate dehydratase EC ... sulfoacetaldehyde acetyltransferase EC cysteine-S-conjugate β-lyase EC 1-aminocyclopropane-1-carboxylate ... carnitine decarboxylase EC phenylpyruvate decarboxylase EC 4-carboxymuconolactone decarboxylase EC ...
... formate-C-acetyltransferase]-activating enzyme EC Now EC, arsenate reductase (glutaredoxin EC Now ... carnitine 3-dehydrogenase EC Now EC, 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase EC aromatic ... carnitine 3-dehydrogenase EC mannitol dehydrogenase EC fluoren-9-ol dehydrogenase EC 4-( ... carnitine monooxygenase EC 2-polyprenylphenol 6-hydroxylase EC 5-pyridoxate monooxygenase EC 1.14. ...
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- ...
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 ...
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. ...
The 2014 Ju-Jitsu World Championship were the 12th edition of the Ju-Jitsu World Championships, and were held in Paris, France from November 28 to November 30, 2014. 28.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Men's Duo System - Classic 29.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Women's Duo System - Classic 30.11.2014 - Men's Jiu-Jitsu (ne-waza), Mixed Duo System - Classic, Team event Vincent MATCZAK (2014-09-30). "4TH INVITAION TO WORLD CHAMPIONSHIP 2014" (PDF). Retrieved 2019-11-28.[dead link] Online results Official results (PDF) Mixed team event results (PDF) (All articles with dead external links, Articles with dead external links from April 2022, Ju-Jitsu World Championships, 2014 in French sport ...
Bolley L. "Bo" Johnson (born November 15, 1951) is an American politician from the state of Florida. A member of the Democratic Party, Johnson was a member of the Florida House of Representatives, and served as the Speaker of the Florida House of Representatives. Johnson is from Milton, Florida. His father and grandfather served as county commissioners for Santa Rosa County, Florida. Johnson graduated from Milton High School, and became the first member of his family to attend college. He received his bachelor's degree from Florida State University. Johnson volunteered for Mallory Horne when Horne served as the president of the Florida Senate. At the age of 22, Johnson met Lawton Chiles, then a member of the United States Senate, who hired him as a legislative aide in 1973. Johnson was elected to the Florida House of Representatives, representing the 4th district from November 7, 1978 to November 3, 1992. He also served the 1st district from November 3, 1992 to November 8, 1994. He became the ...
... may refer to: Don't Say No (Billy Squier album), a 1981 album by American rock singer Billy Squier, and its title track Don't Say No (Seohyun EP), a 2016 extended play by South Korean pop singer Seohyun, and its title track "Don't Say No" (Tom Tom Club song), from the 1988 album Boom Boom Chi Boom Boom "Don't Say No", by Robbie Williams from the 2005 album Intensive Care "Don't Say No Tonight", a 1985 single by Eugene Wilde This disambiguation page lists articles associated with the title Don't Say No. If an internal link led you here, you may wish to change the link to point directly to the intended article. (Disambiguation pages with short descriptions, Short description is different from Wikidata, All article disambiguation pages, All disambiguation pages, Disambiguation pages ...
The Dewoitine 37 was the first of a family of 1930s French-built monoplane fighter aircraft. The D.37 was a single-seat aircraft of conventional configuration. Its fixed landing gear used a tailskid. The open cockpit was located slightly aft of the parasol wing. The radial engine allowed for a comparatively wide fuselage and cockpit. Design of this machine was by SAF-Avions Dewoitine but owing to over work at that companies plant at the time, manufacture of the D.37/01 was transferred to Lioré et Olivier. They were high-wing monoplanes of all-metal construction with valve head blisters on their engine cowlings. The first prototype flew in October 1931. Flight testing resulted in the need for multiple revisions in both engine and airframe, so it was February 1934 before the second prototype flew. Its performance prompted the French government to order for 28 for the Armée de l'Air and Aéronavale. The Lithuanian government ordered 14 that remained in service with their Air Force until 1936, ...
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Carnitine Acetyltransferase Carnitine O Acetyltransferase Carnitine-Acetyl-CoA-Transferase O-Acetyltransferase, Carnitine ... Carnitine Acetyltransferase. Carnitine O Acetyltransferase. Carnitine-Acetyl-CoA-Transferase. O-Acetyltransferase, Carnitine. ... Carnitine O-Acetyltransferase Entry term(s). Acetyltransferase, Carnitine Carnitine Acetyl CoA Transferase ... Carnitine O-acetyltransferase Entry term(s):. Acetyltransferase, Carnitine. Carnitine Acetyl CoA Transferase. ...
... chloramphenicol acetyltransferase; CM: complete medium; CPT1A: carnitine palmitoyltransferase 1a, liver; CQ: chloroquine; CTRL ...
Carnitine O-Acetyltransferase. Carnitine O-Palmitoyltransferase. Carnitine Palmitoyltransferase use Carnitine O- ...
Carnitine Acetyltransferase (CTA) is a cellular organelle in your body that needs carnitine. The machine moves free fatty acids ... L-Carnitine Fumarate. L-carnitine fumarate is a naturally occurring amino acid that you discover in green vegetables, nuts and ... PhenQ is a supplement to 150 mg L-carnitine fumarate.. Magnesium Stearate. Magnesium stearate can be a component you can find ... to the cells so that your body can burn them for energy production. Without carnitine, this device cannot carry the fat to ...
Carnitine Orotate Complex Ameliorates Insulin Resistance and Hepatic Steatosis Through Carnitine Acetyltransferase Pathway Jung ...
The urothelium of various species has been shown to express choline acetyltransferase (ChAT) and/or carnitine acetyltransferase ... MR1 and MR2), carnitine acetyltransferase (CarAT), immunoregulatory cytokines IL7, IL15, and IL23, along with the chemokine ...
... free carnitine ratio as compared with vehicle-treated shunt lambs. These changes correlated with increased carnitine acetyl ... free carnitine ratio as compared with vehicle-treated shunt lambs. These changes correlated with increased carnitine acetyl ... free carnitine ratio as compared with vehicle-treated shunt lambs. These changes correlated with increased carnitine acetyl ... free carnitine ratio as compared with vehicle-treated shunt lambs. These changes correlated with increased carnitine acetyl ...
Acetyl-l-carnitine treatment increases choline acetyltransferase activity and NGF levels in the CNS of adult rats following ... Acetyl-l-carnitine treatment increases nerve growth factor levels and choline acetyltransferase activity in the central nervous ... Acetyl-l-carnitine restores choline acetyltransferase activity in the hippocampus of rats with partial unilateral fimbria- ... Acetyl-l-carnitine enhances the response of PC12 cells to nerve growth factor. Taglialatela, G., Angelucci, L., Ramacci, M. T. ...
... carnitine O-acetyltransferase (EC; phosphate acetyltransferase (EC Carnitine O-acetyltransferase, ... mitochondrial; Carnitine acetylase; EC *Comment: BRENDA misannotates yeasts carnitine acetyltransferase with EC 2.3. ... phosphate acetyltransferase (EC (characterized). 67%. 100%. 958. hi. Shewana3_1551. phosphate acetyltransferase ( ... 1 candidates for pta: phosphate acetyltransferase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other id. ...
ACAT1: acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase). *ACRV1: encoding protein Acrosomal protein SP- ... CPT1A: carnitine palmitoyltransferase 1A (liver). *CREBZF encoding protein CREB/ATF bZIP transcription factor ...
Carnitine O-acetyltransferase. hsa04146. 1NM8; 1S5O. 10. SLC22A5. O76082. Solute carrier family 22 member 5. hsa05231. NA. ... Mitochondrial carnitine/acylcarnitine carrier protein. hsa04714. NA. 2. CROT. Q9UKG9. Peroxisomal carnitine O- ... Carnitine O-palmitoyltransferase 2, mitochondrial. hsa00071; hsa01212; hsa03320; hsa04714. NA. 20 predicted interactions ( ... Carnitine O-palmitoyltransferase 1, liver isoform. hsa00071; hsa01212; hsa03320; hsa04152; hsa04714; hsa04920; hsa04922; ...
Mouse CRAT(Carnitine Acetyltransferase) ELISA Kit. *Mouse CAST(Calpastatin) ELISA Kit. *Mouse CA9(Carbonic Anhydrase IX) ELISA ...
Mouse CRAT(Carnitine Acetyltransferase) ELISA Kit. *Mouse CRN(Corin) ELISA Kit. *Mouse CRYaB(Crystallin Alpha B) ELISA Kit ... Rat CPT2(Carnitine Palmitoyltransferase 2, Mitochondrial) ELISA Kit. *Rat CRHBP(Corticotropin Releasing Hormone Binding Protein ... histone acetyltransferase (4) histone antibody (4) histone code (4) histone deacetylase (4) histone deacetylase inhibitors (4) ... histone acetyltransferase, histone antibody, histone code, histone deacetylase, histone deacetylase inhibitors, histone ...
Rat CPT1A(Carnitine Palmitoyltransferase 1A, Liver) ELISA Kit. *Rat CRAT(Carnitine Acetyltransferase) ELISA Kit ...
Human CRAT(Carnitine Acetyltransferase) ELISA Kit. *Human CRBN(Cereblon) ELISA Kit. *Human CRHR1(Corticotropin Releasing ... Human CACT(Carnitine Acylcarnitine Translocase) ELISA Kit. *Human CAMK2b(Calcium/Calmodulin Dependent Protein Kinase II Beta) ...
Human CRAT(Carnitine Acetyltransferase) ELISA Kit. *Human CRBN(Cereblon) ELISA Kit. *Human CRHR1(Corticotropin Releasing ... Human CACT(Carnitine Acylcarnitine Translocase) ELISA Kit. *Human CAMK2b(Calcium/Calmodulin Dependent Protein Kinase II Beta) ...
Rat CRAT(Carnitine Acetyltransferase) ELISA Kit. *Mouse SSB(Sjogren Syndrome Antigen B) ELISA Kit ... Mouse SAT1(Spermidine/Spermine N1-Acetyltransferase 1) ELISA Kit. *Rat DSTYK(Dual Serine/Threonine And Tyrosine Protein Kinase ... Mouse ACAT2(Acetyl Coenzyme A Acetyltransferase 2) ELISA Kit. *Rat PNPLA3(Patatin Like Phospholipase Domain Containing Protein ...
","N-acetyltransferase-like protein [Ensembl]. Acetyltransferase (GNAT) domain [InterProScan].","protein_coding" "AGT26858"," ... ","secondary glycine betaine transporter BetU [Ensembl]. betaine/carnitine/choline family transporter, BCCT transporter family ... ","putative acetyltransferase [Ensembl]. Acetyltransferase (GNAT) domain [InterProScan].","protein_coding" "AGT26853","N559_ ... ","putative N-acetyltransferase [Ensembl]. GNAT domain [InterProScan].","protein_coding" "AGT26100","N559_4495","Klebsiella ...
CPT1A: carnitine palmitoyltransferase 1A. *CPT2: carnitine palmitoyltransferase 2. *CRB1: crumbs cell polarity complex ... CHAT: choline O-acetyltransferase. *CHD2: chromodomain helicase DNA binding protein 2. *CHD3: chromodomain helicase DNA binding ...
carnitine O-acetyltransferase activity. transferase activity, transferring acyl groups. No GO terms in record ... histone acetyltransferase activity. peptide alpha-N-acetyltransferase activity. N-acetyltransferase activity. transferase ...
Carnitine acetyltransferase (CRAT) expression in macrophages is dispensable for nutrient stress sensing and inflammation ...
Acetyl CoA acetyltransferase 2 deficiency. *Acetyl-carnitine deficiency. *Achalasia microcephaly syndrome. *Achard syndrome ...
Complex:galactoside O-acetyltransferase. *Complex:GALACTURIDYLYLTRANS-CPLX. *Complex:gamma-butyrobetainyl-CoA:carnitine CoA ...
Shaker, M.E.; Houssen, M.E.; Abo-Hashem, E.M. Comparison of vitamin E, L-carnitine and melatonin in ameliorating carbon ... In the subsequent step, serotonin is converted into melatonin through the influence of arylalkylamine N-acetyltransferase ( ... AADC, aromatic-l-amino-acid decarboxylase; AANAT, arylalkylamine N-acetyltransferase; ASMT, N-acetylserotonin methyltransferase ... AADC, aromatic-l-amino-acid decarboxylase; AANAT, arylalkylamine N-acetyltransferase; ASMT, N-acetylserotonin methyltransferase ...
Rat CACT(Carnitine Acylcarnitine Translocase) ELISA Kit. *Rat CAMP(Cathelicidin Antimicrobial Peptide) ELISA Kit ... Rat HAT1(Histone Acetyltransferase 1) ELISA Kit. *Rat HbA1c(Glycated Hemoglobin A1c) ELISA Kit ...
Rat CACT(Carnitine Acylcarnitine Translocase) ELISA Kit. *Rat CAMP(Cathelicidin Antimicrobial Peptide) ELISA Kit ... Rat HAT1(Histone Acetyltransferase 1) ELISA Kit. *Rat HbA1c(Glycated Hemoglobin A1c) ELISA Kit ...
Rhamanosyl-N-acetylglucosamyl-undecaprenyl diphosphate O-acetyltransferase (LPS O16 antigen biosynthesis). OBTFL ...
2000): Carnitine supplementation and ketogenesis by small-for-date neonates on. medium -and long- chain fatty acid formulae. ... coenzyme A: α-glucosaminie N-acetyltransferase deficiency in MPS III C (Sanfilippo. C) patients: an update. 16 th ESGLD ... and L-carnitine as precursors of trimethylamine. Biochemical Society Meeting No.. 659, London, September 1996. ... Thalassinos A., Costalos Ch.: Carnitine and MCT supplementation in small for. dates premature neonates. XIIIth European ...
  • The urothelium of various species has been shown to express choline acetyltransferase (ChAT) and/or carnitine acetyltransferase (CarAT), enzymes that synthesize the neurotransmitter acetylcholine (Ach) [5], [6]. (bioerc-iend.org)
  • gene provides instructions for making a protein called choline acetyltransferase. (nih.gov)
  • Acetyl-L-carnitine is a mitochondrial metabolite that facilitates the movement of fatty acids into the mitochondria for energy and is also used to generate acetyl coenzyme A. '-Lipoic acid is a coenzyme involved in mitochondrial ATP production and its reduced form can recycle other antioxidants. (nih.gov)
  • This decay, a major contributor to aging, can be ameliorated by feeding old rats the normal mitochondrial metabolites acetyl carnitine (ALCAR) and lipoic acid (LA) at high levels. (nih.gov)
  • TGF-β1 attenuates mitochondrial bioenergetics in pulmonary arterial endothelial cells via the disruption of carnitine homeostasis. (nih.gov)
  • TGF-β1 induced mitochondrial dysfunction was linked to a nitration-mediated activation of Akt1 and the subsequent mitochondrial translocation of endothelial NO synthase (eNOS) resulting in the nitration of carnitine acetyl transferase (CrAT) and the disruption of carnitine homeostasis. (nih.gov)
  • shunt), we have recently shown a disruption in carnitine homeostasis, associated with mitochondrial dysfunction and decreased endothelial nitric oxide synthase (eNOS)/heat shock protein (Hsp)90 interactions that contribute to eNOS uncoupling, increased superoxide levels, and decreased bioavailable nitric oxide (NO). Therefore, we undertook this study to test the hypothesis that L-carnitine therapy would maintain mitochondrial function and NO signaling. (arizona.edu)
  • These changes correlated with increased carnitine acetyl transferase (CrAT) protein and enzyme activity and decreased levels of nitrated CrAT. (arizona.edu)
  • Thus, acetyl carnitine/'-lipoic acid dietary supplements have a potential market of tens of millions of middle-aged and elderly Americans who desire to improve their general health. (nih.gov)
  • Virtually no information on the potential toxicity of acetyl-L-carnitine/'-lipoic acid combinations was found in the available literature. (nih.gov)
  • Approximately one year following the presentation of acetyl-L-carnitine/'-lipoic acid at the CSWG meeting on July 1, 2003, a search of PubMed was conducted to identify new published information. (nih.gov)
  • Although no new studies of acetyl-L-carnitine/'-lipoic acid combinations were identified in the literature search, several studies describing protective effects for lipoic acid were published in the last year. (nih.gov)
  • Oxidation: Partial Reversal by Feeding Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
  • Improvement of Carnitine Acetyltransferase Substrate Binding Affinity and Activity in Brain by Feeding Old Rats Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
  • Together with carnitine palmitoyltransferase I, the encoded protein oxidizes long-chain fatty acids in the mitochondria. (nih.gov)
  • An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. (nih.gov)
  • 7. The leucine twenty homeobox (LEUTX) gene, which lacks a histone acetyltransferase domain, is fused to KAT6A in therapy-related acute myeloid leukemia with t(8;19)(p11;q13). (nih.gov)
  • Conclusion: L-Carnitine therapy may improve the endothelial dysfunction noted in children with CHDs and has important clinical implications that warrant further investigation. (arizona.edu)
  • Furthermore, acetylcholine significantly decreased left pulmonary vascular resistance only in L-carnitine-treated lambs. (arizona.edu)
  • In this formulation, acetyl-L-carnitine hydrochloride is thought to increase general metabolic activity and to improve cognitive function. (nih.gov)
  • Immediately after delivery, lambs received daily treatment with oral L-carnitine or its vehicle. (arizona.edu)
  • Results: L-Carnitine-treated lambs had decreased levels of acylcarnitine and a reduced acylcarnitine:free carnitine ratio as compared with vehicle-treated shunt lambs. (arizona.edu)
  • In this formulation, acetyl-L-carnitine hydrochloride is thought to increase general metabolic activity and to improve cognitive function. (nih.gov)
  • Acetyl-L-carnitine is a mitochondrial metabolite that facilitates the movement of fatty acids into the mitochondria for energy and is also used to generate acetyl coenzyme A. '-Lipoic acid is a coenzyme involved in mitochondrial ATP production and its reduced form can recycle other antioxidants. (nih.gov)
  • Virtually no information on the potential toxicity of acetyl-L-carnitine/'-lipoic acid combinations was found in the available literature. (nih.gov)
  • Approximately one year following the presentation of acetyl-L-carnitine/'-lipoic acid at the CSWG meeting on July 1, 2003, a search of PubMed was conducted to identify new published information. (nih.gov)
  • Although no new studies of acetyl-L-carnitine/'-lipoic acid combinations were identified in the literature search, several studies describing protective effects for lipoic acid were published in the last year. (nih.gov)
  • A report indicating that acetyl-L-carnitine had beneficial effects in animal models of Parkinson's disease (Beal, 2004). (nih.gov)
  • Oxidation: Partial Reversal by Feeding Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
  • Improvement of Carnitine Acetyltransferase Substrate Binding Affinity and Activity in Brain by Feeding Old Rats Acetyl-L-Carnitine and/or R--Lipoic Acid. (nih.gov)
  • 10. Oxaliplatin transport mediated by organic cation/carnitine transporters OCTN1 and OCTN2 in overexpressing human embryonic kidney 293 cells and rat dorsal root ganglion neurons. (nih.gov)
  • L-Carnitine Improves Skeletal Muscle Fat Oxidation in Primary Carnitine Deficiency. (nih.gov)
  • An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. (nih.gov)
  • 12. Combination effects of platinum drugs and N1, N11 diethylnorspermine on spermidine/spermine N1-acetyltransferase, polyamines and growth inhibition in A2780 human ovarian carcinoma cells and their oxaliplatin and cisplatin-resistant variants. (nih.gov)
  • The effects of adjunctive treatment with L-carnitine on monitoring laboratory variables in ICU patients: a double-blinded randomized controlled clinical trial. (nih.gov)