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Acetyl Coenzyme AAcetyltransferasesAcetyl-CoA CarboxylaseCoenzyme AHistone AcetyltransferasesCholine O-AcetyltransferasePyruvate CarboxylaseAcetylationChloramphenicol O-AcetyltransferaseAcetate-CoA LigaseAcetatesATP Citrate (pro-S)-LyaseCarnitine O-AcetyltransferaseLigasesBiotinp300-CBP Transcription FactorsAcetylcarnitineAcetyl-CoA C-AcetyltransferaseMolecular Sequence DataSerine O-AcetyltransferaseN-Terminal Acetyltransferase AMagnesium CompoundsN-Terminal Acetyltransferase EMalonyl Coenzyme ADihydrolipoyllysine-Residue AcetyltransferaseLiverPromoter Regions, GeneticFatty Acid SynthasesBase SequenceRhizobium etliTranscription, GeneticFatty AcidsKineticsCarbon IsotopesCitratesAmino Acid SequenceMevalonic AcidHistonesCaprylatesAcetylesteraseEscherichia coliRNA, MessengerAMP-Activated Protein KinasesPhosphate AcetyltransferasePyruvate Dehydrogenase ComplexMultienzyme ComplexesLipid MetabolismAcyl Coenzyme APlasmidsSaccharomyces cerevisiae ProteinsCREB-Binding ProteinCitric Acid CycleTransfectionCloning, MolecularN-Terminal AcetyltransferasesTranscription FactorsE1A-Associated p300 ProteinGlucoseAcyltransferasesOrganophosphatesGene Expression RegulationCytosolMitochondria, LiverSpermineCatalysisCell LineN-Terminal Acetyltransferase BSubstrate SpecificityBinding SitesNuclear ProteinsLysineCarbon RadioisotopesAdenosine TriphosphateCarnitineRats, Inbred StrainsVesicular Acetylcholine Transport ProteinsSpermidineRegulatory Sequences, Nucleic AcidMutationAdipose TissuePolyaminesTranscriptional ActivationDNA-Binding ProteinsGene Expression Regulation, EnzymologicCholinergic FibersCoenzyme A-TransferasesProtein BindingDietary CarbohydratesCoenzyme A LigasesEnzyme ActivationRestriction MappingRecombinant Fusion ProteinsTrans-ActivatorsCysteine SynthaseLipidsOxidation-ReductionChromatinSaccharomyces cerevisiaeAcetylcholinesteraseEnhancer Elements, GeneticPhosphorylationInsulinRecombinant ProteinsGlucosamine 6-Phosphate N-AcetyltransferasePlatelet Activating FactorSequence Homology, Amino AcidHydroxymethylglutaryl CoA ReductasesAmino-Acid N-AcetyltransferaseHeLa CellsDNAAcetate KinaseGenes, ReporterCells, CulturedHistone DeacetylasesEnergy MetabolismAnacardic AcidsChloramphenicol ResistanceProtein Structure, TertiaryChloramphenicolDietary FatsArylamine N-AcetyltransferaseGenes, RegulatorGenesPhenylacetatesGenes, BacterialGene ExpressionTumor Cells, CulturedMuscle, SkeletalEnzyme InductionCholineCell NucleusBacterial ProteinsMutagenesis, Site-DirectedBiogenic PolyaminesNucleosomesAcetylcholineCell Cycle ProteinsSequence AlignmentDNA PrimersPantothenic AcidCholinergic NeuronsRepressor ProteinsSubstantia InnominataPutrescineGeobacillus stearothermophilusEuonymusSequence Homology, Nucleic AcidBlotting, NorthernElectrophoresis, Polyacrylamide GelMolecular WeightSequence DeletionFungal ProteinsGene Expression Regulation, FungalModels, MolecularPalmitoyl Coenzyme AStructure-Activity RelationshipProtein BiosynthesisDNA, ComplementaryAcetyl-CoA C-AcyltransferaseEstersOrnithine DecarboxylaseOligodeoxyribonucleotidesHydroxamic AcidsGene Expression Regulation, ViralGenetic Complementation TestThioctic AcidTime FactorsChromatin Assembly and DisassemblyProtein Processing, Post-TranslationalParasympathetic Nervous SystemGenetic VectorsCrystallography, X-RayGenes, ViralNitrophenolsPyruvatesThiolester HydrolasesChromatography, High Pressure LiquidHydrogen-Ion ConcentrationGene DeletionN-Terminal Acetyltransferase FPolymerase Chain ReactionDrug Resistance, MicrobialPantetheineProtein KinasesGene Expression Regulation, BacterialSirtuinsCarnitine AcyltransferasesMethylationRepetitive Sequences, Nucleic AcidPhenotypeCatalytic DomainHemicholinium 3IsoenzymesChromosome DeletionPropionatesChemistryPlumbaginaceaeMice, TransgenicUridine Diphosphate N-AcetylglucosamineNeuronsCarrier Proteins
Acetyl Coenzyme A: 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.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Acetyl-CoA Carboxylase: A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.Coenzyme AHistone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.Choline O-Acetyltransferase: An enzyme that catalyzes the formation of acetylcholine from acetyl-CoA and choline. EC 2.3.1.6.Pyruvate Carboxylase: A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)Chloramphenicol O-Acetyltransferase: 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 2.3.1.28.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.ATP Citrate (pro-S)-Lyase: An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATE. This reaction represents an important step in fatty acid biosynthesis. This enzyme was formerly listed as EC 4.1.3.8.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.Biotin: A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.p300-CBP Transcription Factors: 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.Acetylcarnitine: An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.Acetyl-CoA C-Acetyltransferase: 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.Molecular Sequence Data: 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.Serine O-Acetyltransferase: An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.N-Terminal Acetyltransferase A: 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.Magnesium Compounds: Inorganic compounds that contain magnesium as an integral part of the molecule.N-Terminal Acetyltransferase E: 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.Malonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.Dihydrolipoyllysine-Residue Acetyltransferase: 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.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Promoter Regions, Genetic: 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.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Rhizobium etli: A species of gram-negative bacteria and nitrogen innoculant of PHASEOLUS VULGARIS.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Fatty Acids: 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)Kinetics: The rate dynamics in chemical or physical systems.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.CitratesAmino Acid Sequence: 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.Mevalonic AcidHistones: 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.Caprylates: 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.Acetylesterase: An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.Escherichia coli: 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.RNA, Messenger: 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.AMP-Activated Protein Kinases: Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. Their activity largely depends upon the concentration of cellular AMP which is increased under conditions of low energy or metabolic stress. AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP.Phosphate Acetyltransferase: An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.Pyruvate Dehydrogenase Complex: 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)Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.Acyl Coenzyme A: 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.Plasmids: 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.Saccharomyces cerevisiae Proteins: 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.CREB-Binding Protein: 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.Citric Acid Cycle: A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.Transfection: 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.Cloning, Molecular: 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.N-Terminal Acetyltransferases: Enzymes that catalyze the transfer of an acetyl group, usually from ACETYL COENZYME A, to the N-terminus of a peptide chain.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.E1A-Associated p300 Protein: A member of the p300-CBP transcription factors that was originally identified as a binding partner for ADENOVIRUS E1A PROTEINS.Glucose: 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.Acyltransferases: 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.Organophosphates: Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.Gene Expression Regulation: 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.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Mitochondria, Liver: 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)Spermine: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Cell Line: Established cell cultures that have the potential to propagate indefinitely.N-Terminal Acetyltransferase B: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Nuclear Proteins: 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.Lysine: An essential amino acid. It is often added to animal feed.Carbon Radioisotopes: Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Rats, Inbred Strains: 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.Vesicular Acetylcholine Transport Proteins: 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.Spermidine: 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.Regulatory Sequences, Nucleic Acid: Nucleic acid sequences involved in regulating the expression of genes.Mutation: 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.Adipose Tissue: 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.PolyaminesTranscriptional Activation: Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.DNA-Binding Proteins: 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.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Cholinergic Fibers: Nerve fibers liberating acetylcholine at the synapse after an impulse.Coenzyme A-Transferases: Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. Enzymes in this group are instrumental in ketone body metabolism and utilization of acetoacetate in mitochondria. EC 2.8.3.Protein Binding: 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.Dietary Carbohydrates: Carbohydrates present in food comprising digestible sugars and starches and indigestible cellulose and other dietary fibers. The former are the major source of energy. The sugars are in beet and cane sugar, fruits, honey, sweet corn, corn syrup, milk and milk products, etc.; the starches are in cereal grains, legumes (FABACEAE), tubers, etc. (From Claudio & Lagua, Nutrition and Diet Therapy Dictionary, 3d ed, p32, p277)Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Recombinant Fusion Proteins: 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.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Cysteine Synthase: 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 4.2.99.8.Lipids: A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)Oxidation-Reduction: 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).Chromatin: 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.Saccharomyces cerevisiae: 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.Acetylcholinesterase: 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 3.1.1.7.Enhancer Elements, Genetic: Cis-acting DNA sequences which can increase transcription of genes. Enhancers can usually function in either orientation and at various distances from a promoter.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Insulin: 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).Recombinant Proteins: Proteins prepared by recombinant DNA technology.Glucosamine 6-Phosphate N-Acetyltransferase: An enzyme that catalyses the reaction of D-glucosamine 6-phosphate with ACETYL-COA to form N-acetylglucosamine 6-phosphate.Platelet Activating Factor: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Hydroxymethylglutaryl CoA Reductases: Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.Amino-Acid N-Acetyltransferase: A mitochondrial matrix enzyme that catalyzes the synthesis of L-GLUTAMATE to N-acetyl-L-glutamate in the presence of ACETYL-COA.HeLa Cells: 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.DNA: 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).Acetate Kinase: An enzyme that catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP. It is important in the glycolysis process. EC 2.7.2.1.Genes, Reporter: 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.Cells, Cultured: 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.Histone Deacetylases: 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.Energy Metabolism: The chemical reactions involved in the production and utilization of various forms of energy in cells.Anacardic Acids: A group of 6-alkyl SALICYLIC ACIDS that are found in ANACARDIUM and known for causing CONTACT DERMATITIS.Chloramphenicol Resistance: 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.Protein Structure, Tertiary: 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.Chloramphenicol: 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)Dietary Fats: 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.Arylamine N-Acetyltransferase: An enzyme that catalyzes the transfer of acetyl groups from ACETYL-COA to arylamines. It can also catalyze acetyl transfer between arylamines without COENZYME A and has a wide specificity for aromatic amines, including SEROTONIN. However, arylamine N-acetyltransferase should not be confused with the enzyme ARYLALKYLAMINE N-ACETYLTRANSFERASE which is also referred to as SEROTONIN ACETYLTRANSFERASE.Genes, Regulator: Genes which regulate or circumscribe the activity of other genes; specifically, genes which code for PROTEINS or RNAs which have GENE EXPRESSION REGULATION functions.Genes: 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.Phenylacetates: Derivatives of phenylacetic acid. Included under this heading are a variety of acid forms, salts, esters, and amides that contain the benzeneacetic acid structure. Note that this class of compounds should not be confused with derivatives of phenyl acetate, which contain the PHENOL ester of ACETIC ACID.Genes, Bacterial: The functional hereditary units of BACTERIA.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Tumor Cells, Cultured: 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.Muscle, Skeletal: A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.Enzyme Induction: 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.Choline: 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.Cell Nucleus: 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)Bacterial Proteins: Proteins found in any species of bacterium.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Biogenic Polyamines: 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.Nucleosomes: 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.Acetylcholine: 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.Cell Cycle Proteins: 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.Sequence Alignment: 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.DNA Primers: 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.Pantothenic Acid: A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE.Cholinergic Neurons: Neurons whose primary neurotransmitter is ACETYLCHOLINE.Repressor Proteins: Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.Substantia Innominata: 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.Putrescine: A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.Geobacillus stearothermophilus: A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.Euonymus: A plant genus of the family CELASTRACEAE.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Blotting, Northern: 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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Molecular Weight: The sum of the weight of all the atoms in a molecule.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Fungal Proteins: Proteins found in any species of fungus.Gene Expression Regulation, Fungal: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.DNA, Complementary: 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.Acetyl-CoA C-Acyltransferase: Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.EstersOrnithine Decarboxylase: A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine.Oligodeoxyribonucleotides: A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.Hydroxamic Acids: A class of weak acids with the general formula R-CONHOH.Gene Expression Regulation, Viral: Any of the processes by which cytoplasmic factors influence the differential control of gene action in viruses.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Thioctic Acid: An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Chromatin Assembly and Disassembly: The mechanisms effecting establishment, maintenance, and modification of that specific physical conformation of CHROMATIN determining the transcriptional accessibility or inaccessibility of the DNA.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Parasympathetic Nervous System: The craniosacral division of the autonomic nervous system. The cell bodies of the parasympathetic preganglionic fibers are in brain stem nuclei and in the sacral spinal cord. They synapse in cranial autonomic ganglia or in terminal ganglia near target organs. The parasympathetic nervous system generally acts to conserve resources and restore homeostasis, often with effects reciprocal to the sympathetic nervous system.Genetic Vectors: DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Genes, Viral: The functional hereditary units of VIRUSES.NitrophenolsPyruvatesThiolester HydrolasesChromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Gene Deletion: A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.N-Terminal Acetyltransferase F: An N-terminal acetyltransferase subtype that consists of the Naa60p catalytic subunit. It is found in higher eukayotes and displays a substrate specificity for the N-terminal METHIONINE of peptides where the next amino acid in the chain is either LEUCINE; LYSINE; PHENYALANINE; ISOLEUCINE; or TRYPTOPHANE.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Drug Resistance, Microbial: The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS).Pantetheine: An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Sirtuins: A homologous family of regulatory enzymes that are structurally related to the protein silent mating type information regulator 2 (Sir2) found in Saccharomyces cerevisiae. Sirtuins contain a central catalytic core region which binds NAD. Several of the sirtuins utilize NAD to deacetylate proteins such as HISTONES and are categorized as GROUP III HISTONE DEACETYLASES. Several other sirtuin members utilize NAD to transfer ADP-RIBOSE to proteins and are categorized as MONO ADP-RIBOSE TRANSFERASES, while a third group of sirtuins appears to have both deacetylase and ADP ribose transferase activities.Carnitine Acyltransferases: 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.Methylation: Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)Repetitive Sequences, Nucleic Acid: Sequences of DNA or RNA that occur in multiple copies. There are several types: INTERSPERSED REPETITIVE SEQUENCES are copies of transposable elements (DNA TRANSPOSABLE ELEMENTS or RETROELEMENTS) dispersed throughout the genome. TERMINAL REPEAT SEQUENCES flank both ends of another sequence, for example, the long terminal repeats (LTRs) on RETROVIRUSES. Variations may be direct repeats, those occurring in the same direction, or inverted repeats, those opposite to each other in direction. TANDEM REPEAT SEQUENCES are copies which lie adjacent to each other, direct or inverted (INVERTED REPEAT SEQUENCES).Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Hemicholinium 3: A potent inhibitor of the high affinity uptake system for CHOLINE. It has less effect on the low affinity uptake system. Since choline is one of the components of ACETYLCHOLINE, treatment with hemicholinium can deplete acetylcholine from cholinergic terminals. Hemicholinium 3 is commonly used as a research tool in animal and in vitro experiments.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Chromosome Deletion: Actual loss of portion of a chromosome.Propionates: Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Plumbaginaceae: A plant family of the order Plumbaginales, subclass Caryophyllidae, class Magnoliopsida of shrubs and herbs. Some members contain ANTHOCYANINS and naphthaquinones.Mice, Transgenic: Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.Uridine Diphosphate N-Acetylglucosamine: Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.Neurons: The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.

Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. (1/222)

Poly(3-hydroxyalkanoates) (PHAs) are a class of microbially produced polyesters that have potential applications as conventional plastics, specifically thermoplastic elastomers. A wealth of biological diversity in PHA formation exists, with at least 100 different PHA constituents and at least five different dedicated PHA biosynthetic pathways. This diversity, in combination with classical microbial physiology and modern molecular biology, has now opened up this area for genetic and metabolic engineering to develop optimal PHA-producing organisms. Commercial processes for PHA production were initially developed by W. R. Grace in the 1960s and later developed by Imperial Chemical Industries, Ltd., in the United Kingdom in the 1970s and 1980s. Since the early 1990s, Metabolix Inc. and Monsanto have been the driving forces behind the commercial exploitation of PHA polymers in the United States. The gram-negative bacterium Ralstonia eutropha, formerly known as Alcaligenes eutrophus, has generally been used as the production organism of choice, and intracellular accumulation of PHA of over 90% of the cell dry weight have been reported. The advent of molecular biological techniques and a developing environmental awareness initiated a renewed scientific interest in PHAs, and the biosynthetic machinery for PHA metabolism has been studied in great detail over the last two decades. Because the structure and monomeric composition of PHAs determine the applications for each type of polymer, a variety of polymers have been synthesized by cofeeding of various substrates or by metabolic engineering of the production organism. Classical microbiology and modern molecular bacterial physiology have been brought together to decipher the intricacies of PHA metabolism both for production purposes and for the unraveling of the natural role of PHAs. This review provides an overview of the different PHA biosynthetic systems and their genetic background, followed by a detailed summation of how this natural diversity is being used to develop commercially attractive, recombinant processes for the large-scale production of PHAs.  (+info)

Pregnenolone esterification in Saccharomyces cerevisiae. A potential detoxification mechanism. (2/222)

While studying the effect of steroids on the growth of the yeast Saccharomyces cerevisiae, we found that pregnenolone was converted into the acetate ester. This reaction was identified as a transfer of the acetyl group from acetyl-CoA to the 3beta-hydroxyl group of pregnenolone. The corresponding enzyme, acetyl-CoA:pregnenolone acetyltransferase (APAT) is specific for Delta5- or Delta4-3beta-hydroxysteroids and short-chain acyl-CoAs. The apparent Km for pregnenolone is approximately 0.5 microm. The protein associated with APAT activity was partially purified and finally isolated from an SDS/polyacrylamide gel. Tryptic peptides were generated and N-terminally sequenced. Two peptide sequences allowed the identification of an open reading frame (YGR177c, in the S. cerevisiae genome database) translating into a 62-kDa protein of hitherto unknown function. This protein encoded by a gene known as ATF2 displays 37% identity with an alcohol acetyltransferase encoded by the yeast gene ATF1. Disruption of ATF2 led to the complete elimination of APAT activity and consequently abolished the esterification of pregnenolone. In addition, a toxic effect of pregnenolone linked to the disruption of ATF2 was observed. Pregnenolone toxicity is more pronounced when the atf2-Delta mutation is introduced in a yeast strain devoid of the ATP-binding cassette transporters, PDR5 and SNQ2. Our results suggest that Atf2p (APAT) plays an active role in the detoxification of 3beta-hydroxysteroids in association with the efflux pumps Pdr5p and Snq2p.  (+info)

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (3/222)

The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself.  (+info)

Origin of gene overlap: the case of TCP1 and ACAT2. (4/222)

The human acetyl-CoA acetyltransferase 2 gene, ACAT2, codes for a thiolase, an enzyme involved in lipid metabolism. The human T-complex protein 1 gene, TCP1, encodes a molecular chaperone of the chaperonin family. The two genes overlap by their 3'-untranslated regions, their coding sequences being located on opposite DNA strands in a tail-to-tail orientation. To find out how the overlap might have arisen in evolution, the homologous genes of the zebrafish, the African toad, caiman, platypus, opossum, and wallaby were identified. In each species, standard or long polymerase chain reactions were used to determine whether the ACAT2 and TCP1 homologs are closely linked and, if so, whether they overlap. The results reveal that the overlap apparently arose during the transition from therapsid reptiles to mammals and has been retained for >200 million years. Part of the overlapping untranslated region shows remarkable sequence conservation. The overlap presumably arose during the chromosomal rearrangement that brought the two unrelated and previously separated genes together. One or both of the transposed genes found by chance signals that are necessary for the processing of their transcripts to be present on the noncoding strand of the partner gene.  (+info)

Development and characterization of a gene expression reporter system for Clostridium acetobutylicum ATCC 824. (5/222)

A gene expression reporter system (pHT3) for Clostridium acetobutylicum ATCC 824 was developed by using the lacZ gene from Thermoanaerobacterium thermosulfurogenes EM1 as the reporter gene. In order to test the reporter system, promoters of three key metabolic pathway genes, ptb (coding for phosphotransbutyrylase), thl (coding for thiolase), and adc (coding for acetoacetate decarboxylase), were cloned upstream of the reporter gene in pHT3 in order to construct vectors pHT4, pHT5, and pHTA, respectively. Detection of beta-galactosidase activity in time course studies performed with strains ATCC 824(pHT4), ATCC 824(pHT5), and ATCC 824(pHTA) demonstrated that the reporter gene produced a functional beta-galactosidase in C. acetobutylicum. In addition, time course studies revealed differences in the beta-galactosidase specific activity profiles of strains ATCC 824(pHT4), ATCC 824(pHT5), and ATCC 824(pHTA), suggesting that the reporter system developed in this study is able to effectively distinguish between different promoters. The stability of the beta-galactosidase produced by the reporter gene was also examined with strains ATCC 824(pHT4) and ATCC 824(pHT5) by using chloramphenicol treatment to inhibit protein synthesis. The data indicated that the beta-galactosidase produced by the lacZ gene from T. thermosulfurogenes EM1 was stable in the exponential phase of growth. In pH-controlled fermentations of ATCC 824(pHT4), the kinetics of beta-galactosidase formation from the ptb promoter and phosphotransbutyrylase formation from its own autologous promoter were found to be similar.  (+info)

A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism. (6/222)

BACKGROUND: Thiolases are ubiquitous and form a large family of dimeric or tetrameric enzymes with a conserved, five-layered alphabetaalphabetaalpha catalytic domain. Thiolases can function either degradatively, in the beta-oxidation pathway of fatty acids, or biosynthetically. Biosynthetic thiolases catalyze the biological Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA. This is one of the fundamental categories of carbon skeletal assembly patterns in biological systems and is the first step in a wide range of biosynthetic pathways, including those that generate cholesterol, steroid hormones, and various energy-storage molecules. RESULTS: The crystal structure of the tetrameric biosynthetic thiolase from Zoogloea ramigera has been determined at 2.0 A resolution. The structure contains a striking and novel 'cage-like' tetramerization motif, which allows for some hinge motion of the two tight dimers with respect to each other. The protein crystals were flash-frozen after a short soak with the enzyme's substrate, acetoacetyl-CoA. A reaction intermediate was thus trapped: the enzyme tetramer is acetylated at Cys89 and has a CoA molecule bound in each of its active-site pockets. CONCLUSIONS: The shape of the substrate-binding pocket reveals the basis for the short-chain substrate specificity of the enzyme. The active-site architecture, and in particular the position of the covalently attached acetyl group, allow a more detailed reaction mechanism to be proposed in which Cys378 is involved in both steps of the reaction. The structure also suggests an important role for the thioester oxygen atom of the acetylated enzyme in catalysis.  (+info)

Aberrant oxidation of the cholesterol side chain in bile acid synthesis of sterol carrier protein-2/sterol carrier protein-x knockout mice. (7/222)

Peroxisomal beta-oxidation plays an important role in the metabolism of a wide range of substrates, including various fatty acids and the steroid side chain in bile acid synthesis. Two distinct thiolases have been implicated to function in peroxisomal beta-oxidation: the long known 41-kDa beta-ketothiolase identified by Hashimoto and co-workers (Hijikata, M., Ishii, N., Kagamiyama, H., Osumi, T., and Hashimoto, T. (1987) J. Biol. Chem. 262, 8151-8158) and the recently discovered 60-kDa SCPx thiolase, that consists of an N-terminal domain with beta-ketothiolase activity and a C-terminal moiety of sterol carrier protein-2 (SCP2, a lipid carrier or transfer protein). Recently, gene targeting of the SCP2/SCPx gene has shown in mice that the SCPx beta-ketothiolase is involved in peroxisomal beta-oxidation of 2-methyl-branched chain fatty acids like pristanic acid. In our present work we have investigated bile acid synthesis in the SCP2/SCPx knockout mice. Specific inhibition of beta-oxidation at the thiolytic cleavage step in bile acid synthesis is supported by our finding of pronounced accumulation in bile and serum from the knockout mice of 3alpha,7alpha, 12alpha-trihydroxy-27-nor-5beta-cholestane-24-one (which is a known bile alcohol derivative of the cholic acid synthetic intermediate 3alpha,7alpha,12alpha-trihydroxy-24-keto-cholestano yl-coenzyme A). Moreover, these mice have elevated concentrations of bile acids with shortened side chains (i.e. 23-norcholic acid and 23-norchenodeoxycholic acid), which may be produced via alpha- rather than beta-oxidation. Our results demonstrate that the SCPx thiolase is critical for beta-oxidation of the steroid side chain in conversion of cholesterol into bile acids.  (+info)

Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method. (8/222)

Sterol carrier protein X (SCPx) plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. To investigate whether patients with an unresolved defect in peroxisomal beta-oxidation are deficient for SCPx, we developed a novel and specific assay to measure the activity of SCPx in both liver and fibroblast homogenates. The substrate used in the assay, 3alpha, 7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoy l-CoA (24-keto-THC-CoA), is produced by preincubating the enoyl-CoA of the bile acid intermediate THCA with a lysate from the yeast Saccharomyces cerevisiae expressing human D-bifunctional protein. After the preincubation period, liver or fibroblast homogenate is added plus CoASH, and the production of choloyl-CoA is determined by HPLC. The specificity of the assay was demonstrated by the finding of a full deficiency in fibroblasts from an SCPx knock-out mouse. In addition to SCPx activity measurements in fibroblasts from patients with a defect in peroxisomal beta-oxidation of unresolved etiology, we studied the stability and activity of SCPx in fibroblasts from patients with Zellweger syndrome, which lack functional peroxisomes. We found that SCPx is not only stable in the cytosol, but displays a higher activity in fibroblasts from patients with Zellweger syndrome than in control fibroblasts. Furthermore, in all patients studied with a defect in peroxisomal beta-oxidation of unknown origin, SCPx was found to be normally active, indicating that human SCPx deficiency remains to be identified.  (+info)

Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast,...Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast,...
TY - JOUR. T1 - Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast, Candida tropicalis. AU - Ueda, Mitsuyoshi. AU - Kanayama, Naoki. AU - Tanaka, Atsuo. PY - 2000. Y1 - 2000. N2 - The n-alkane-assimilating diploid yeast, Candida tropicalis, possesses two acetoacetyl-CoA thiolase (Thiolase I) isozymes encoded by one allele: peroxisomal and cytosolic Thiolase Is encoded by both CT-T1A and CT-T1B. To clarify the function of peroxisomal and cytosolic Thiolase Is, the site-directed mutation leading Thiolase I ΔC6 without a putative C-terminal peroxisomal targeting signal was introduced on CT-T1A locus in the ct-t1bΔ-null mutant. The C-terminus-truncated Thiolase I was active and solely present in the cytosol. Although the ct-t1aΔ/t1bΔ-null mutants showed mevalonate auxotrophy, the mutants having the C-terminus-truncated Thiolase I did not require mevalonate for growth, as did the strains having cytosolic Thiolase I. These ...
EMBL: CR382138.PE377EMBL: CR382138.PE377
CR382138.PE377 Location/Qualifiers FT CDS complement(751782..752987) FT /transl_table=12 FT /locus_tag="DEHA2F08712g" FT /old_locus_tag="DEHA0F09603g" FT /old_locus_tag="DEHA-IPF8377" FT /old_locus_tag="DEHA-CDS3172.1" FT /product="DEHA2F08712p" FT /note="similar to uniprot,P41338 Saccharomyces cerevisiae FT YPL028W ERG10 Acetyl-CoA C-acetyltransferase (acetoacetyl- FT CoA thiolase) cytosolic enzyme that transfers an acetyl FT group from one acetyl-CoA molecule to another forming FT acetoacetyl-CoA" FT /db_xref="EnsemblGenomes-Gn:DEHA2F08712g" FT /db_xref="EnsemblGenomes-Tr:CAG89081" FT /db_xref="GOA:Q6BM30" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020610" FT /db_xref="InterPro:IPR020613" FT /db_xref="InterPro:IPR020615" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:Q6BM30" FT /protein_id="CAG89081.1" FT /translation="MSSVYIVSTARTPIGAFQGGLSSLTYSDLGSHAVHAALKKVPQIK FT ...
SAUSA300 0221 - AureoWikiSAUSA300 0221 - AureoWiki
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_0221 (SAUSA300_RS01160); symbol: pflA; product: pyruvate formate-lyase activating enzyme
anti-ACAT1 antibody | GeneTexanti-ACAT1 antibody | GeneTex
ACAT1 antibody (acetyl-CoA acetyltransferase 1) for IP, WB. Anti-ACAT1 pAb (GTX30683) is tested in Human, Mouse, Hamster samples. 100% Ab-Assurance.
Acetoacetyl-CoA thiolase | definition of acetoacetyl-CoA thiolase by Medical dictionaryAcetoacetyl-CoA thiolase | definition of acetoacetyl-CoA thiolase by Medical dictionary
Looking for online definition of acetoacetyl-CoA thiolase in the Medical Dictionary? acetoacetyl-CoA thiolase explanation free. What is acetoacetyl-CoA thiolase? Meaning of acetoacetyl-CoA thiolase medical term. What does acetoacetyl-CoA thiolase mean?
Beta ketothiolase deficiencyBeta ketothiolase deficiency
... or 2M3HBA is a rare genetic condition. 2M3HBA results from a mutation (error) in a persons DNA. 2M3HBA is considered an organic acid condition because it leads to a buildup of harmful amounts of organic acids in the body. Protein in the food we eat is broken down into amino acids, or "building blocks". We typically eat more protein than needed; therefore we often have more amino acids than we need. Enzymes (special proteins) breakdown the extra amino acids into organic acids and ammonia, and then harmless products our body can get rid of. If one of the enzymes needed is missing or not working correctly, the amino acid is not broken all the way down and builds up in our system as organic acids. Although organic acids are only mild acids, both organic acids and ammonia can damage our bodies if too much builds up. In this case the enzyme, 2-methyl-3-hydroxybutyryl, is unable to break down the amino acid, isoleucine.. Signs of 2M3HBA typically begin to show during ...
Beta ketothiolase deficiency | Genetic and Rare Diseases Information Center (GARD) - an NCATS ProgramBeta ketothiolase deficiency | Genetic and Rare Diseases Information Center (GARD) - an NCATS Program
A collection of disease information resources and questions answered by our Genetic and Rare Diseases Information Specialists for Beta ketothiolase deficiency
Gene | ACAT1Gene | ACAT1
The ACAT1 gene is associated with autosomal recessive beta-ketothiolase deficiency (aka mitochondrial acetoacetyl-CoA thiolase deficiency) (MedGen UID: 280689).
phaA - Acetyl-CoA acetyltransferase - Zoogloea ramigera - phaA gene & proteinphaA - Acetyl-CoA acetyltransferase - Zoogloea ramigera - phaA gene & protein
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Lirias: Isolation and subunit composition of native sterol carrier protein 2/3-oxoacyl-coenzyme a thiolase from normal rat...Lirias: Isolation and subunit composition of native sterol carrier protein 2/3-oxoacyl-coenzyme a thiolase from normal rat...
In the present report we describe a method for the complete purification of native sterol carrier protein 2/3-oxoacyl-CoA thiolase (SCP-2/thiolase) from normal rat liver peroxisomes. The isolation procedure is based on the alteration in chromatographic properties of the enzyme in the presence of low concentrations of CoA. The purified preparation of SCP-2/thiolase consisted of 58- and 46-kDa polypeptides. Peroxisomes prepared freshly from normal rat liver contained three SCP-2/thiolase isoforms, separable by conventional chromatography. Immunochemical, molecular sieving, and chemical cross-linking experiments indicated that these isoforms represent thiolytically active homo- and heterodimeric combinations of the 46- and 58-kDa subunits (2 x 58, 58-46, and 2 x 46-kDa proteins). (C) 2000 Academic Press ...
Formate C-acetyltransferase - WikipediaFormate C-acetyltransferase - Wikipedia
In enzymology, formate C-acetyltransferase (pyruvate formate lyase, PFL) (EC 2.3.1.54) is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA. The reaction occurs as follows: This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:formate C-acetyltransferase. Other names in common use include pyruvate formate-lyase, pyruvic formate-lyase, and formate acetyltransferase. This enzyme participates in 3 metabolic pathways: pyruvate metabolism, propanoate metabolism, and butanoate metabolism. As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1CM5, 1H16, 1H17, 1H18, 1MZO, 1QHM, 2PFL, and 3PFL. Pyruvate formate lyase ...
UniProtKB/SwissProt variant VAR 007499UniProtKB/SwissProt variant VAR 007499
3-ketothiolase deficiency (3KTD) [MIM:203750]: An inborn error of isoleucine catabolism characterized by intermittent ketoacidotic attacks associated with unconsciousness. Some patients die during an attack or are mentally retarded. Urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine, butanone is increased. It seems likely that the severity of this disease correlates better with the environmental or acquired factors than with the ACAT1 genotype. {ECO:0000269,PubMed:1346617, ECO:0000269,PubMed:1715688, ECO:0000269,PubMed:7728148, ECO:0000269,PubMed:9744475}. Note=The disease is caused by mutations affecting the gene represented in this entry ...
3-ketoacyl-CoA thiolase | definition of 3-ketoacyl-CoA thiolase by Medical dictionary3-ketoacyl-CoA thiolase | definition of 3-ketoacyl-CoA thiolase by Medical dictionary
Looking for online definition of 3-ketoacyl-CoA thiolase in the Medical Dictionary? 3-ketoacyl-CoA thiolase explanation free. What is 3-ketoacyl-CoA thiolase? Meaning of 3-ketoacyl-CoA thiolase medical term. What does 3-ketoacyl-CoA thiolase mean?
Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat...Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat...
The enzyme 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine: acetyl-CoA acetyltransferase (EC 2.3.1.67) was purified from rat spleen approx. 1500-fold in 1.6% yield. The specific activity of the purified enzyme was 0.317 +/- 0.089 mumol/min per mg of protein (mean +/- S.D., n = 6). The Km for the substrate acetyl-CoA was 137 +/- 13 microM and the pH optimum was about 8. Incubation of the purified enzyme was 1-O-[3H]octadecyl-2-lyso-sn-glycero-3-phosphocholine followed by electrophoresis resulted in the incorporation of radioactivity into a protein of Mr 29,000. The enzyme was most active towards 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine as substrate, 1-palmitoyl-2-lyso-glycero-3-phosphocholine being a poor substrate. In addition, the enzyme preferred acetyl-CoA to palmitoyl-CoA or oleoyl-CoA as substrate.. ...
PRIME PubMed | Identification of three novel frameshift mutations (83delAT, 754insCT, and 435 + 1G to A) of mitochondrial...PRIME PubMed | Identification of three novel frameshift mutations (83delAT, 754insCT, and 435 + 1G to A) of mitochondrial...
PubMed journal article Identification of three novel frameshift mutations (83delAT, 754insCT, and 435 + 1G to A) of mitochondrial acetoacetyl-coenzyme A thiolase gene in two Swiss patients with CRM-negative beta-ketothiolase deficienc were found in PRIME PubMed. Download Prime PubMed App to iPhone or iPad.
Increased expression of acyl-coenzyme A: cholesterol acyltransferase-1 by J.-H Kim, S.-M Ee et al."Increased expression of acyl-coenzyme A: cholesterol acyltransferase-1" by J.-H Kim, S.-M Ee et al.
Significant increases in levels of cholesterol and cholesterol oxidation products are detected in the hippocampus undergoing degeneration after excitotoxicity induced by the potent glutamate analog, kainate (KA), but until now, it is unclear whether the cholesterol is in the free or esterified form. The present study was carried out to examine the expression of the enzyme involved in cholesteryl ester biosynthesis, acyl-coenzyme A: cholesterol acyltransferase (ACAT) and cholesteryl esters after KA excitotoxicity. A 1000-fold greater basal mRNA level of ACAT1 than ACAT2 was detected in the normal brain. ACAT1 mRNA and protein were upregulated in the hippocampus at 1 and 2 weeks after KA injections, at a time of glial reaction. Immunohistochemistry showed ACAT1 labeling of oligodendrocytes in the white matter and axon terminals in hippocampal CA fields of normal rats, and loss of staining in neurons but increased immunoreactivity of oligodendrocytes, in areas affected by KA. Gas chromatography-mass
fadA - 3-ketoacyl-CoA thiolase - Escherichia coli O9:H4 (strain HS) - fadA gene & proteinfadA - 3-ketoacyl-CoA thiolase - Escherichia coli O9:H4 (strain HS) - fadA gene & protein
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
The promiscuous enzyme medium-chain 3-keto-acyl-CoA thiolase triggers a vicious cycle in fatty-acid beta-oxidation - Research...The promiscuous enzyme medium-chain 3-keto-acyl-CoA thiolase triggers a vicious cycle in fatty-acid beta-oxidation - Research...
Mitochondrial fatty-acid beta-oxidation (mFAO) plays a central role in mammalian energy metabolism. Multiple severe diseases are associated with defects in this pathway. Its kinetic structure is characterized by a complex wiring of which the functional implications have hardly been explored. Repetitive cycles of reversible reactions, each cycle shortening the fatty acid by two carbon atoms, evoke competition between intermediates of different chain lengths for a common set of promiscuous enzymes (enzymes with activity towards multiple substrates). In our validated kinetic model of the pathway, substrate overload causes a steep and detrimental flux decline. Here, we unravel the underlying mechanism and the role of enzyme promiscuity in it. Comparison of alternative model versions elucidated the role of promiscuity of individual enzymes. Promiscuity of the last enzyme of the pathway, medium-chain ketoacyl-CoA thiolase (MCKAT), was both necessary and sufficient to elicit the flux decline. ...
Das aktive Zentrum der Thiolase blockieren | EurekAlert! Science NewsDas aktive Zentrum der Thiolase blockieren | EurekAlert! Science News
Wissenschaftler der finnischen Universität Oulu und des Helmholtz-Zentrum Berlin haben neue Wege zur Medikamentenentwicklung gegen die afrikanische Schlafkrankheit und andere von Parasiten übertragene, tropische Erkrankungen aufgezeigt. Grundlage dafür sind Strukturuntersuchungen an einem als Thiolase bezeichneten Enzym. Thiolase spielt eine wichtige Rolle im Lipid-Stoffwechsel krankheitsübertragender Parasiten. Die Struktur des Biomoleküls haben die Forscher an der MX-Beamline des Elektronenspeicherrings BESSY II des HZB untersucht.
WikiGenes - SCP2 - sterol carrier protein 2WikiGenes - SCP2 - sterol carrier protein 2
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
Human Metabolome Database: Showing metabocard for Acetoacetyl-CoA (HMDB0001484)Human Metabolome Database: Showing metabocard for Acetoacetyl-CoA (HMDB0001484)
InChI=1S/C25H40N7O18P3S/c1-13(33)8-16(35)54-7-6-27-15(34)4-5-28-23(38)20(37)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-19(49-51(39,40)41)18(36)24(48-14)32-12-31-17-21(26)29-11-30-22(17)32/h11-12,14,18-20,24,36-37H,4-10H2,1-3H3,(H,27,34)(H,28,38)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41)/t14-,18-,19-,20?,24-/m1/ ...
EMBL: CP000859.PE558EMBL: CP000859.PE558
CP000859.PE558 Location/Qualifiers FT CDS_pept 625652..626875 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Dole_0558" FT /product="Thiolase" FT /note="PFAM: Thiolase; KEGG: bbr:BB1086 putative thiolase" FT /db_xref="EnsemblGenomes-Gn:Dole_0558" FT /db_xref="EnsemblGenomes-Tr:ABW66368" FT /db_xref="GOA:A8ZU56" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:A8ZU56" FT /protein_id="ABW66368.1" FT /translation="MRDVAIIGAGMTRFGKFPEKSIKDLVKESSQAAIKDAGIQPSDIQ FT AAYVGSAVAGLMTGQEMIKAQVTLSAMGIEAIPMYNVENACASSSSALNLAWTAVGAGI FT FDCVLVTGFEKLYDEDKKKSFAALGTAVDIELFKLFLAEFQKNQGKGESIIKEGSGQKR FT SVFMDMYAHYTKIYMDRYGLTQEHFARIAVKSHKNGALNPHSQYQEEVTLEQVLNSGDV FT SWPLTRMMCSPIGDGAAAVIVCSKEAAARFGARPVWIASSVVGSGKLSGDLEDTLTKRL FT APKAFEAAGIGPDDIDVIEVHDATSPSEIITLIELGLCPGADAPKWIDEGYMEIDGSRP FT SNTSGGLAAKGHPIGATGLGQVYEIVNQLRGTAGKRQVKNPKVGMTHNGGGILGVDAAA FT MALHVFKN" atgcgtgatg tggcaattat cggagcgggc ...
Yagyu Hiroaki | TRIOSYagyu Hiroaki | TRIOS
マクロファージのアシルC0A:コレステロールアシルトランスフェラーゼ1 (ACAT1)欠損マウスの皮膚黄色腫、動脈硬化病変形成におけるインフラマソームの役割についての検討 ...
Expression and Automated Purification of Acetoacetyl CoA Thiolase from Sunflower Cotyledon<...Expression and Automated Purification of Acetoacetyl CoA Thiolase from Sunflower Cotyledon<...
TY - JOUR. T1 - Expression and Automated Purification of Acetoacetyl CoA Thiolase from Sunflower Cotyledon. AU - Dyer, James H.. AU - Becker, James. AU - Geraldo, Victor. AU - Giron, Mario. PY - 2006/4. Y1 - 2006/4. N2 - In the sunflower (Helianthus annuus L.) cotyledons, two distinguishable thiolase activities have been identified: acetoacetyl CoA thiolase (AACT), specifically active during oxidation of short chain acetoacetyl CoA, and 3-oxoacyl CoA thiolase (OACT), active towards short, medium, and long-chain acyl CoAs. The purpose of this research was to optimize the purification of the AACT expressed in bacteria. Escherischia coli (E. coli) with the full-length sunflower AACT cDNA cloned into the expression vector pBAD-His B was induced for production of the AACT using 0.2% arabinose. Optimizing the conditions for protein purification is often an extremely empirical process requiring several iterations of a basic protocol each with specific changes. This iterative process was simplified ...
3-ketoacyl-CoA thiolase, peroxisomal (P27796) - Yeast Metabolome Database3-ketoacyl-CoA thiolase, peroxisomal (P27796) - Yeast Metabolome Database
Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287 ...
Fatty acid recycling and degradation | LAMPFatty acid recycling and degradation | LAMP
This pathway mainly shows the oxidation of fatty acids. The fatty acid oxidation takes place in mitochondria in animals. This is the reverse of fatty acid biosynthesis and utilises CoA as acyl carrier. The four main enzymes involved in the degradation of fatty acids are acyl-CoA oxidase (acyl-CoA dehydrogenase), Enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase. Each cycle of activities of these enzymes removes 2-carbon units in the form of acetyl-CoA. This cycle of activities can continue until the fatty acid chain is degraded to 4-carbon acetoacetyl-CoA. Acetoacetyl-CoA can then be cleaved to 2 acetyl-CoAs by the reverse action of the enzyme acetyl-CoA C-acetyltransferase.. This pathway may provide a carbon source in the form of acetyl-CoA for mitochondrial TCA cycle and other biosynthesis pathways. The enzymes acyl-CoA oxidase and 3-hydroxyacyl-CoA dehydrogenase are absent in Plasmodium falciparum. There is no biochemical evidence of this pathway taking place in ...
Complete β-oxidation of valproate: cleavage of 3-oxovalproyl-CoA by a mitochondrial 3-oxoacyl-CoA thiolase | Biochemical...Complete β-oxidation of valproate: cleavage of 3-oxovalproyl-CoA by a mitochondrial 3-oxoacyl-CoA thiolase | Biochemical...
The β-oxidation of valproic acid (VPA; 2-n-propylpentanoic acid) was investigated in vitro in intact rat liver mitochondria incubated with 3H-labelled VPA. The metabolism of [4,5-3H2]VPA and [2-3H]VPA was studied by analysing the different acyl-CoA intermediates formed by reverse-phase HPLC with radiochemical detection. Valproyl-CoA, Δ2(E)-valproyl-CoA,3-hydroxyvalproyl-CoA and 3-oxovalproyl-CoA (labelled and non-labelled) were determined using continuous on-line radiochemical and UV detection. The formation of these intermediates was investigated using the two tritiated precursors in respiratory states 3 and 4. Valproyl-CoA was present at highest concentrations under both conditions. Two distinct labelled peaks were found, which were identified as 3H2O and [4,5-3H2]3-oxo-VPA. The formation of 3H2O strongly suggested that VPA underwent complete β-oxidation and that [4,5-3H2]3-oxo-VPA was formed by hydrolysis of the corresponding thioester. The hypothesis that 3-oxovalproyl-CoA undergoes ...
Role of the Sterol Carrier Protein-2 N-Terminal Membrane Binding Domain in Sterol Transfer †Role of the Sterol Carrier Protein-2 N-Terminal Membrane Binding Domain in Sterol Transfer †
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acetoacetyl-CoA (CHEBI:15345)acetoacetyl-CoA (CHEBI:15345)
Chemical Entities of Biological Interest (ChEBI) is a freely available dictionary of molecular entities focused on small chemical compounds.
Differential regulation of two thiolase genes from Clostridium acetobutylicum DSM 792. - Lancaster EPrintsDifferential regulation of two thiolase genes from Clostridium acetobutylicum DSM 792. - Lancaster EPrints
Thiolase of Clostridium acetobutylicum is an important enzyme involved in both, acid and solvent fermentation. Two thiolase genes (thlA and thlB) have been cloned and sequenced from Clostridium acetobutylicum DSM 792, showing high homology to each other and to thiolases of PHA-synthesizing bacteria. The thlA gene is identical to the gene already cloned and sequenced from strain ATCC 824 (Stim- Herndon et al., 1995, Gene 154: 81-85). Using primer extension and S1 nuclease analysis a transcriptional start site was identified 102 bp upstream of the thlA start codon. This site was preceded by a region that exhibits high similarity to the s70 consensus promoter sequences of Gram-positive and -negative bacteria. Regulation of thlA and thlB was studied at the transcriptional level to elucidate the specific function of each gene. Non-radioactive primer extension analysis using fluorescein-labelled oligonucleotides and Northern blot analysis revealed high levels of thlA transcripts in acid- and ...
SCP-1884 - SCP FoundationSCP-1884 - SCP Foundation
Begin Log,. Dr. Hayfield: How long have you been connected to SCP-1884-B?. SCP-1884-A: As long as I can remember. Wherever I have been, Luana has been there with me, even if only in my mind.. Dr. Hayfield: Where did SCP-1884-B come from?. SCP-1884-A: When I was still very young, I asked my mother the same question. She would not tell me. She said she did not want to frighten me.. Dr. Hayfield: Have your blindness and physical abnormalities been present since birth?. SCP-1884-A: Yes. Luana has always been my eyes. She feels the ground so I can walk. She helps me hold things. In my old age, there have been times she has carried me. I am very grateful to her.. Dr. Hayfield: What were the events that led to the incident at the hotel?. SCP-1884-A: That may take some time to explain.. Dr. Hayfield: Thats perfectly fine. Please proceed.. SCP-1884-A: When I was eight years old, men came to our house asking to buy me and Luana. My parents were upset. They always tried to hide us and keep us a secret, ...
What is Acetyl-CoA? (with picture)What is Acetyl-CoA? (with picture)
Acetyl-CoA is a molecule that is broken down and used by the body for energy production. If the body has too much acetyl-CoA, it...
Association of Train Operating Companies (ATOC) - Fujitsu NetherlandsAssociation of Train Operating Companies (ATOC) - Fujitsu Netherlands
ATOC agreed a five year, £13 million deal with Fujitsu to refresh, enhance and streamline the hardware and applications technology used by RJIS, so that it could be supported until at least 2014. It also had to have the capacity to handle an increase in workload, largely driven by a massive growth in online sales (25% year-on-year) and greater use of Ticket-on-Departure vending-style machines used to collect ticket.
Addgene: pEB2-DsRed-ExpressAddgene: pEB2-DsRed-Express
Plasmid pEB2-DsRed-Express from Dr. Philippe Cluzels lab contains the insert DsRed-Express and is published in Nat Methods. 2018 Jan;15(1):47-51. doi: 10.1038/nmeth.4509. Epub 2017 Nov 20. This plasmid is available through Addgene.
Mutation analysis of a family with 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency]. - Semantic ScholarMutation analysis of a family with 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency]. - Semantic Scholar
OBJECTIVE The aim of this study was to explore the genetic features of a family with 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBDD) which may provide the basis for the diagnosis and genetic counseling. METHOD Clinical data of the proband was collected, total RNA and genomic DNA were extracted from the peripheral blood. The whole coding region of the ACAT1 gene was amplified by RT-PCR. 5 noncoding region of the ACAT1 gene and all 6 exons and flanking intron regions of the HADH2 gene were amplified by PCR. All amplification products were directly sequenced and compared with the reference sequence. RESULT (1) The patient was a one-year-old boy who presented with psychomotor retardation and astasia when he was admitted to the hospital. Biochemical test revealed slight hyperlactatemia (3.19 mmol/L) and magnetic resonance imaging showed delayed myelination. 2-Methylacetoacetyl-CoA thiolase deficiency was suggested by gas chromatography-mass spectrometry. (2) There was no mutation in the
Trimetazidine - A Drug A DayTrimetazidine - A Drug A Day
Trimetazidine is used for the treatment of angina pectoris, and works as an anti-ischemic metabolic agent. The utilization of myocardial glucose improves through the inhibition of long-chain-3-ketacyl CoA thiolase activity, reducing fatty acid oxidation and stimulating the oxidation of glucose. High rates of fatty acid oxidation can be detrimental during spells of angina due to…
BMRB Entry 25984BMRB Entry 25984
Deposition date: 2016-03-07 Original release date: 2017-03-02. Authors: Singarapu, Kiran; Ummanni, Ramesh. Citation: Singarapu, Kiran; Ahuja, Ashish; Potula, Purushotam; Ummanni, Ramesh. "Solution Nuclear Magnetic Resonance Studies of Sterol Carrier Protein 2 Like 2 (SCP2L2) Reveal the Insecticide Specific Structural Characteristics of SCP2 Proteins in Aedes aegypti Mosquitoes" Biochemistry 55, 4919-4927 (2016).. Assembly members: ...
Rhizomelic chondrodysplasia punctata type 1: Report of mutations in 3 children from India<...Rhizomelic chondrodysplasia punctata type 1: Report of mutations in 3 children from India<...
TY - JOUR. T1 - Rhizomelic chondrodysplasia punctata type 1. T2 - Report of mutations in 3 children from India. AU - Phadke, S. R.. AU - Gupta, N.. AU - Girisha, K. M.. AU - Kabra, M.. AU - Maeda, M.. AU - Vidal, E.. AU - Moser, A.. AU - Steinberg, S.. AU - Puri, R. D.. AU - Verma, I. C.. AU - Braverman, N.. PY - 2010/1/1. Y1 - 2010/1/1. N2 - Rhizomelic chondrodysplasia punctata is a rare autosomal recessive disorder characterized by stippled epiphyses and rhizomelic shortening of the long bones. We report 3 subjects of rhizomelic chondrodysplasia punctata from India and the PEX7 mutations identified in them. The common PEX7-L292X allele, whose high frequency is due to a founder effect in the northern European Caucasian population, was not identified in these patients. Instead, 2 novel alleles are described, including 64_65delGC, which was present on a single PEX7 haplotype and could represent a common allele in the Indian population.. AB - Rhizomelic chondrodysplasia punctata is a rare ...
OriGene - HADHA (NM 000182) cDNA CloneOriGene - HADHA (NM 000182) cDNA Clone
HADHA - HADHA (untagged)-Human hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit (HADHA), nuclear gene encoding mitochondrial protein available for purchase from OriGene - Your Gene Company.
Rhizomelic chondrodysplasia punctata - Genetics Home ReferenceRhizomelic chondrodysplasia punctata - Genetics Home Reference
Rhizomelic chondrodysplasia punctata is a condition that impairs the normal development of many parts of the body. The major features of this disorder include skeletal abnormalities, distinctive facial features, intellectual disability, and respiratory problems.. Rhizomelic chondrodysplasia punctata is characterized by shortening of the bones in the upper arms and thighs (rhizomelia). Affected individuals also have a specific bone abnormality called chondrodysplasia punctata, which affects the growth of the long bones and can be seen on x-rays. People with rhizomelic chondrodysplasia punctata often develop joint deformities (contractures) that make the joints stiff and painful.. Distinctive facial features are also seen with rhizomelic chondrodysplasia punctata. These include a prominent forehead, widely set eyes (hypertelorism), a sunken appearance of the middle of the face (midface hypoplasia), a small nose with upturned nostrils, and full cheeks. Additionally, almost all affected individuals ...
Patent US5534432 - Polyhydroxybutyrate polymerase - Google PatentsPatent US5534432 - Polyhydroxybutyrate polymerase - Google Patents
A method for controlling and modifying biopolymer synthesis by manipulation of the genetics and enzymology of synthesis of polyhydroxybutyrate (PHB) and polyhydroxyalkanoate (PHA) polyesters at the molecular level in procaryotic and eukaryotic cells, especially plants. Examples demonstrate the isolation, characterization, and expression of the genes involved in the production of PHB and PHA polymers. Genes encoding the enzymes in the PHB and PHA synthetic pathway (beta-ketothiolase, acetoacetyl-CoA reductase and PHB polymerass or PHA polymerase) from Zoogloea ramigera strain I-16-M, Alcaligenes eutrophus, Nocardia salmonicolur, and P. olevorans were identified or isolated and expressed in a non-PHB producing organism, E. coli. Specific modifications to the polymers include variation in the chain length of the polymers and incorporation of different monomers into the polymers to produce co-polymers with different physical properties.
Peroxisomal targeting signal - WikipediaPeroxisomal targeting signal - Wikipedia
In biochemical protein targeting, a peroxisomal targeting signal (PTS) is a region of the peroxisomal protein that receptors recognize and bind to. It is responsible for specifying that proteins containing this motif are localised to the peroxisome. All peroxisomal proteins are synthesized in the cytoplasm and must be directed to the peroxisome. The first step in this process is the binding of the protein to a receptor. The receptor then directs the complex to the peroxisome. Receptors recognize and bind to a region of the peroxisomal protein called a peroxisomal targeting signal, or PTS. Peroxisomes consist of a matrix surrounded by a specific membrane. Most peroxisomal matrix proteins contain a short sequence, usually three amino acids at the extreme carboxy tail of the protein, that serves as the PTS. The prototypic sequence (many variations exist) is serine-lysine-leucine (-SKL in the one letter amino acid code). This motif, and its variations, is known as the PTS1, and the receptor is ...
Glenmax PEB DM: Indications, Side Effects, Warnings - Drugs.comGlenmax PEB DM: Indications, Side Effects, Warnings - Drugs.com
Easy to read patient leaflet for Glenmax PEB DM. Includes indications, proper use, special instructions, precautions, and possible side effects.
Severe rhizomelic chondrodysplasia punctata in a fetus due to maternal mixed connective tissue disorder<...Severe rhizomelic chondrodysplasia punctata in a fetus due to maternal mixed connective tissue disorder<...
TY - JOUR. T1 - Severe rhizomelic chondrodysplasia punctata in a fetus due to maternal mixed connective tissue disorder. AU - Nayak, S. S.. AU - Adiga, P. K.. AU - Rai, L.. AU - Girisha, K. M.. PY - 2012. Y1 - 2012. N2 - Maternal systemic lupus erythematosus and autoimmune diseases have been extremely rarely reported to cause rhizomelic chondrodysplasia punctata. We report on a fetus aborted spontaneously at 21 weeks of gestation due to complications of maternal mixed connective tissue disorder. The fetus had micrognathia, a depressed nasal bridge, flat nose, long philtrum, short columella and rhizomelia. Radiographic study showed stippling of carpal and tarsal bones, short humeri and coronal clefts in the vertebrae. Ossification centers were present at the lower end of the femora and upper end of the tibiae.. AB - Maternal systemic lupus erythematosus and autoimmune diseases have been extremely rarely reported to cause rhizomelic chondrodysplasia punctata. We report on a fetus aborted ...
Chondrodysplasia Punctata, Tibia-Metacarpal Type disease: Malacards - Research Articles, Drugs, Genes, Clinical TrialsChondrodysplasia Punctata, Tibia-Metacarpal Type disease: Malacards - Research Articles, Drugs, Genes, Clinical Trials
MalaCards based summary : Chondrodysplasia Punctata, Tibia-Metacarpal Type, also known as chondrodysplasia punctata, tibial-metacarpal type, is related to chondrodysplasia punctata syndrome and otitis media. An important gene associated with Chondrodysplasia Punctata, Tibia-Metacarpal Type is ARSD (Arylsulfatase D). Affiliated tissues include bone, and related phenotypes are short 4th metacarpal and malar flattening ...
Crystal structure of β‐ketoacyl‐acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing...Crystal structure of β‐ketoacyl‐acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing...
The assignment of Cys163 as the active site cysteine is based on several lines of evidence. In a sequence comparison of 42 condensing enzymes of fatty acid and polyketide synthesis, Siggaard‐Andersen (1993) identified one conserved cysteine residue, which in KAS II corresponds to Cys163. In addition, this cysteine residue superimposes with the active site cysteine in thiolase I, Cys125. Covalent modification studies of β‐ketoacyl synthases (Kauppinen et al., 1988; Funabashi et al., 1989) and thiolases (Izbicka‐Dimitrijevio et al., 1982) as well as mutagenesis of this residue in the β‐ketoacyl synthase domain of rat fatty acid synthase (Joshi et al., 1997) and thiolase from Zooglea ramigera (Thompson et al., 1989) support the proposed role of this cysteine as the nucleophile in the catalytic reaction.. At the entrance of the active site pocket, a bulky conserved residue, Phe400, is located. This residue points into the active site pocket and in part blocks access to the nucleophilic ...
Euclid) SCP-3083 - Echoes of a MistakeEuclid) SCP-3083 - Echoes of a Mistake
Item #: SCP-3083. Object Class: Euclid. Special Containment Procedures: The orbit of the SCPS Kama has been altered to allow for easier monitoring of SCP-3083. The status of SCP-3083 is to be checked once daily, and its orientation noted if an activation event has occurred. SCP-3083-1 should always be retrieved if present, however samples of SCP-3083 need only be taken if its form is visibly altered. SCP-3083-1 instances are to be transferred to Site-22 during routine cargo exchanges with the Kama and stored in a secure locker.. As SCP-3083 is too small to be observed by amateur telescopes, disinformation campaigns need only be directed at major observatories. As the number of independent sightings since containment has been miniscule, disinformation is considered a Foxtrot-Omega Priority containment task.. Investigation into possible anomalous activity regarding Researcher Benich has concluded as of 14/05/2017, with negative results. Doctor Benich is not to be informed of the existence of ...
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsTechnology, Industry, AgricultureInformation Science
Acetyl Coenzyme AAcetyltransferasesAcetyl-CoA CarboxylaseCoenzyme AHistone AcetyltransferasesCholine O-AcetyltransferasePyruvate CarboxylaseAcetylationChloramphenicol O-AcetyltransferaseAcetate-CoA LigaseAcetatesATP Citrate (pro-S)-LyaseCarnitine O-AcetyltransferaseLigasesBiotinp300-CBP Transcription FactorsAcetylcarnitineAcetyl-CoA C-AcetyltransferaseMolecular Sequence DataSerine O-AcetyltransferaseN-Terminal Acetyltransferase AMagnesium CompoundsN-Terminal Acetyltransferase EMalonyl Coenzyme ADihydrolipoyllysine-Residue AcetyltransferaseLiverPromoter Regions, GeneticFatty Acid SynthasesBase SequenceRhizobium etliTranscription, GeneticFatty AcidsKineticsCarbon IsotopesCitratesAmino Acid SequenceMevalonic AcidHistonesCaprylatesAcetylesteraseEscherichia coliRNA, MessengerAMP-Activated Protein KinasesPhosphate AcetyltransferasePyruvate Dehydrogenase ComplexMultienzyme ComplexesLipid MetabolismAcyl Coenzyme APlasmidsSaccharomyces cerevisiae ProteinsCREB-Binding ProteinCitric Acid CycleTransfectionCloning, MolecularN-Terminal AcetyltransferasesTranscription FactorsE1A-Associated p300 ProteinGlucoseAcyltransferasesOrganophosphatesGene Expression RegulationCytosolMitochondria, LiverSpermineCatalysisCell LineN-Terminal Acetyltransferase BSubstrate SpecificityBinding SitesNuclear ProteinsLysineCarbon RadioisotopesAdenosine TriphosphateCarnitineRats, Inbred StrainsVesicular Acetylcholine Transport ProteinsSpermidineRegulatory Sequences, Nucleic AcidMutationAdipose TissuePolyaminesTranscriptional ActivationDNA-Binding ProteinsGene Expression Regulation, EnzymologicCholinergic FibersCoenzyme A-TransferasesProtein BindingDietary CarbohydratesCoenzyme A LigasesEnzyme ActivationRestriction MappingRecombinant Fusion ProteinsTrans-ActivatorsCysteine SynthaseLipidsOxidation-ReductionChromatinSaccharomyces cerevisiaeAcetylcholinesteraseEnhancer Elements, GeneticPhosphorylationInsulinRecombinant ProteinsGlucosamine 6-Phosphate N-AcetyltransferasePlatelet Activating FactorSequence Homology, Amino AcidHydroxymethylglutaryl CoA ReductasesAmino-Acid N-AcetyltransferaseHeLa CellsDNAAcetate KinaseGenes, ReporterCells, CulturedHistone DeacetylasesEnergy MetabolismAnacardic AcidsChloramphenicol ResistanceProtein Structure, TertiaryChloramphenicolDietary FatsArylamine N-AcetyltransferaseGenes, RegulatorGenesPhenylacetatesGenes, BacterialGene ExpressionTumor Cells, CulturedMuscle, SkeletalEnzyme InductionCholineCell NucleusBacterial ProteinsMutagenesis, Site-DirectedBiogenic PolyaminesNucleosomesAcetylcholineCell Cycle ProteinsSequence AlignmentDNA PrimersPantothenic AcidCholinergic NeuronsRepressor ProteinsSubstantia InnominataPutrescineGeobacillus stearothermophilusEuonymusSequence Homology, Nucleic AcidBlotting, NorthernElectrophoresis, Polyacrylamide GelMolecular WeightSequence DeletionFungal ProteinsGene Expression Regulation, FungalModels, MolecularPalmitoyl Coenzyme AStructure-Activity RelationshipProtein BiosynthesisDNA, ComplementaryAcetyl-CoA C-AcyltransferaseEstersOrnithine DecarboxylaseOligodeoxyribonucleotidesHydroxamic AcidsGene Expression Regulation, ViralGenetic Complementation TestThioctic AcidTime FactorsChromatin Assembly and DisassemblyProtein Processing, Post-TranslationalParasympathetic Nervous SystemGenetic VectorsCrystallography, X-RayGenes, ViralNitrophenolsPyruvatesThiolester HydrolasesChromatography, High Pressure LiquidHydrogen-Ion ConcentrationGene DeletionN-Terminal Acetyltransferase FPolymerase Chain ReactionDrug Resistance, MicrobialPantetheineProtein KinasesGene Expression Regulation, BacterialSirtuinsCarnitine AcyltransferasesMethylationRepetitive Sequences, Nucleic AcidPhenotypeCatalytic DomainHemicholinium 3IsoenzymesChromosome DeletionPropionatesChemistryPlumbaginaceaeMice, TransgenicUridine Diphosphate N-AcetylglucosamineNeuronsCarrier Proteins
SGSHSGSH
... acetyl CoA:alpha-glucosaminide acetyltransferase (type C; MIM 252930); and N-acetylglucosamine 6-sulfatase (type D; MIM 252940 ...
AcetateAcetate
Fermentation acetyl CoA to acetate[edit]. Pyruvate is converted into acetyl-coenzyme A (acetyl-CoA) by the enzyme pyruvate ... Acetate formation requires two enzymes: phosphate acetyltransferase and acetate kinase.[8] The Mixed Acid Fermentation pathway ... This acetyl-CoA is then converted into acetate in E. coli, whilst producing ATP by substrate-level phosphorylation. ... acetyl-phosphate + ADP → acetate + ATP Fermentation of acetate[edit]. Acetic acid can also undergo a dismutation reaction to ...
ACAT1ACAT1
Acetyl-Coenzyme A acetyltransferase 1) gene. Acetyl-Coenzyme A acetyltransferase 1 is an acetyl-CoA C-acetyltransferase enzyme ... Acetyl-CoA acetyltransferase, mitochondrial, also known as acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by ... a mitochondrially localized enzyme that catalyzes the reversible formation of acetoacetyl-CoA from two molecules of acetyl-CoA ... acetyl-Coenzyme A acetyltransferase 1". Kano, M; Fukao, T; Yamaguchi, S; Orii, T; Osumi, T; Hashimoto, T (30 December 1991). " ...
HGSNATHGSNAT
... "acetyl-CoA:heparan-α-D-glucosaminide N-acetyltransferase" and "acetyl-CoA:alpha-glucosaminide N-acetyltransferase") is an ... acetyl-CoA + heparan sulfate α-D-glucosaminide ⇌ {\displaystyle \rightleftharpoons } CoA + heparan sulfate N-acetyl-α-D- ... Pohlmann R, Klein U, Fromme HG, von Figura K (1981). "Localisation of acetyl-CoA: alpha-glucosaminide N-acetyltransferase in ... deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts". Proc. Natl. Acad. Sci. U.S.A. 75 (10): ...
Dihydrolipoyl transacetylaseDihydrolipoyl transacetylase
... lysine S-acetyltransferase. Other names in common use include: acetyl-CoA:dihydrolipoamide S-acetyltransferase, acetyl-CoA: ... acetyl-CoA S-acetyltransferase, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid ... dihydrolipoamide S-acetyltransferase) gene. The systematic name of this enzyme class is acetyl-CoA:enzyme N6-(dihydrolipoyl) ... This involves the transformation of pyruvate from glycolysis into acetyl-CoA which is then used in the citric acid cycle to ...
Mycothiol synthaseMycothiol synthase
... (EC 2.3.1.189, MshD) is an enzyme with systematic name acetyl-CoA:desacetylmycothiol O-acetyltransferase. ... This enzyme catalyses the following chemical reaction desacetylmycothiol + acetyl-CoA ⇌ {\displaystyle \rightleftharpoons } CoA ... encoding the acetyltransferase producing mycothiol in actinomycetes". Arch. Microbiol. 178: 331-337. doi:10.1007/s00203-002- ... from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases". Protein Sci. 12: 1954- ...
Malate synthaseMalate synthase
The systematic name of this enzyme class is acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl- ... CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and CoA. This ... Upon binding, the acetyl-CoA molecule forms a J-shape inserted into the binding pocket, by an intramolecular hydrogen bond ... The active site, where the acetyl-CoA and glyoxylate bind to the enzyme, lie between the TIM barrel and C-terminal plug. ...
BAHD acyltransferaseBAHD acyltransferase
Acetyl-CoA:benzylalcohol acetyltransferase - an enzyme involved in floral scent production in Clarkia breweri. Plant J 14: 297- ... They are CoA-dependent enzymes that transfer acylated moieties (RC(O)R') of an acyl-activated CoA thioester donor to an ... B: Benzyl alcohol O-acetyltransferase (BEAT), an acetyltransferase from the California wild flower Clarkia breweri, also known ... These are benzoyl-CoA:benzyl alcohol O-benzoyltransferase (PtBEBT) that produces benzyl benzoate from benzoyl-CoA and benzyl ...
AlkylacetylglycerophosphataseAlkylacetylglycerophosphatase
Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen". J. Biol. Chem. 261 ( ... Other names in common use include 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase, and alkylacetylglycerophosphate ... 1-alkyl-2-acetyl-sn-glycerol + phosphate Thus, the two substrates of this enzyme are 1-alkyl-2-acetyl-sn-glycero-3-phosphate ... Lee TC, Malone B, Snyder F (1986). "A new de novo pathway for the formation of 1-alkyl-2-acetyl-sn-glycerols, precursors of ...
NAT6NAT6
N-acetyltransferases modify proteins by transferring acetyl groups from acetyl-CoA to the N-termini of protein substrates. The ... N-acetyltransferase 6 (GCN5-related) is a protein that in humans is encoded by the NAT6 gene. This gene encodes a member of the ... Zegerman P, Bannister AJ, Kouzarides T (January 2000). "The putative tumour suppressor Fus-2 is an N-acetyltransferase". ... N-acetyltransferase 6 (GCN5-related)". Shuttleworth TL, Wilson MD, Wicklow BA, Wilkins JA, Triggs-Raine BL (June 2002). " ...
AcetylcholineAcetylcholine
... is synthesized in certain neurons by the enzyme choline acetyltransferase from the compounds choline and acetyl-CoA. ... which causes dysfunction of the enzyme choline acetyltransferase. This inhibition may lead to acetylcholine deficiency, and can ...
Mixed acid fermentationMixed acid fermentation
Acetate formation requires two enzymes: phosphate acetyltransferase and acetate kinase. acetyl-CoA + phosphate → acetyl- ... NAD+ Pyruvate is converted into acetyl-coenzyme A (acetyl-CoA) by the enzyme pyruvate dehydrogenase. This acetyl-CoA is then ... pyruvate + CoA → acetyl-CoA + formate Succinate is formed in E. coli in several steps. Phosphoenolpyruvate (PEP), a glycolysis ... This two-step reaction requires the enzyme alcohol dehydrogenase (ADHE). acetyl-CoA + NADH + H+ → acetaldehyde + NAD+ + CoA ...
Homocitrate synthaseHomocitrate synthase
The systematic name of this enzyme class is acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl ... CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and 2-oxoglutarate, whereas its two products are (R)-2-hydroxybutane-1 ... In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O + 2- ... acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, and homocitrate synthetase. This enzyme participates in lysine ...
2-ethylmalate synthase2-ethylmalate synthase
The systematic name of this enzyme class is acetyl-CoA:2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl ... CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and 2-oxobutanoate, whereas its two products are (R)-2-ethylmalate and ... In enzymology, a 2-ethylmalate synthase (EC 2.3.3.6) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O + 2- ... Strassman M, Ceci LN (1967). "A study of acetyl-CoA condensation with alpha-keto acids". Arch. Biochem. Biophys. 119 (1): 420-8 ...
ATP citrate synthaseATP citrate synthase
... acetyl-CoA], (ATP-dephosphorylating), acetyl-CoA:oxaloacetate acetyltransferase (isomerizing, ADP-phosphorylating), adenosine ... The systematic name of this enzyme class is acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP- ... CoA The 4 substrates of this enzyme are ADP, phosphate, acetyl-CoA, and oxaloacetate, whereas its 3 products are ATP, citrate, ... In enzymology, an ATP citrate synthase (EC 2.3.3.8) is an enzyme that catalyzes the chemical reaction ADP + phosphate + acetyl- ...
MelatoninMelatonin
... but is also converted into N-acetylserotonin by serotonin N-acetyltransferase and acetyl-CoA. Hydroxyindole O-methyltransferase ... which allows the lone pair on the amine to attack acetyl-CoA, forming a tetrahedral intermediate. The thiol from coenzyme A ... Melatonin, also known as N-acetyl-5-methoxy tryptamine, is a hormone that is produced by the pineal gland in animals and ... It has been proposed that histidine residue His122 of serotonin N-acetyl transferase is the catalytic residue that deprotonates ...
Hemicholinium-3Hemicholinium-3
Acetylcholine is synthesized from choline and a donated acetyl group from acetyl-CoA, by the action of choline ... acetyltransferase (ChAT). Thus, decreasing the amount of choline available to a neuron will decrease the amount of ...
Pyruvate dehydrogenase (NADP+)Pyruvate dehydrogenase (NADP+)
... acetyltransferase) EC 1.2.4.1. It catalyzes the following reaction: Pyruvate + Coenzyme A + NADP+ ⇒ acetyl-CoA + NADPH + H+ + ...
SalutaridinolSalutaridinol
"Acetyl coenzyme A: salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures: The enzyme catalyzing the ... an esterification of the hydroxyl group previously reduced in the conversion of salutaridine to salutaridinol with acetyl-CoA. ... This step is mediated by the enzyme salutaridinol 7-O-acetyltransferase. The second step is a ring closure achieved by a ... "Molecular characterization of the salutaridinol 7-O-acetyltransferase involved in morphine biosynthesis in opium poppy Papaver ...
AcetyllysineAcetyllysine
Histone acetyltransferases (HATs) catalyze the addition of acetyl groups from acetyl-CoA onto certain lysine residues of ... There are multiple forms of acetyllysine - this article refers to N-ε-acetyl-L-lysine. The other form is N-α-acetyl-L-lysine. ... Histone deacetylases (HDACs) catalyze the removal of acetyl groups from acetylated lysines. Acetyllysine can be synthesized ... Acetyllysine (or acetylated lysine) is an acetyl-derivative of the amino acid lysine. ...
AcecainideAcecainide
N-Acetyltransferase is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines and aromatic amines ... These studies claim that ABT is a more potent inhibitor of N-acetyltransferase 2 compared with N-acetyltransferase 1. Strong JM ... This reaction is known as an acetylation reaction, that refers to the process of introducing an acetyl group (resulting in an ... Procainamide is metabolized in the liver to acecainide by N-acetyltransferase, an enzyme that is genetically determined. ...
T-complex 1T-complex 1
Ashworth A (1994). "Two acetyl-CoA acetyltransferase genes located in the t-complex region of mouse chromosome 17 partially ...
TransferaseTransferase
... which converts pyruvate to acetyl CoA. Transferases are also utilized during translation. In this case, an amino acid chain is ... Choline acetyltransferase (also known as ChAT or CAT) is an important enzyme which produces the neurotransmitter acetylcholine ... Succinyl-CoA:3-ketoacid CoA transferase deficiency (or SCOT deficiency) leads to a buildup of ketones. Ketones are created upon ... ChAT functions to transfer an acetyl group from acetyl co-enzyme A to choline in the synapses of nerve cells and exists in two ...
MelatoninMelatonin
... but is also converted into N-acetylserotonin by serotonin N-acetyltransferase with acetyl-CoA.[54] Hydroxyindole O- ... which allows the lone pair on the amine to attack acetyl-CoA, forming a tetrahedral intermediate. The thiol from coenzyme A ... N1-acetyl-N2-formyl-5-methoxykynuramine (AFMK), and N1-acetyl-5-methoxykynuramine (AMK).[44][48] ... It has been proposed that histidine residue His122 of serotonin N-acetyl transferase is the catalytic residue that deprotonates ...
Acetoin dehydrogenaseAcetoin dehydrogenase
... is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction ... acetoin + CoA + NAD+ ⇌ {\displaystyle \rightleftharpoons } acetaldehyde + acetyl-CoA + NADH + H+ This enzyme requires thiamine ...
HADHBHADHB
Acetyl-CoA C-acyltransferase. *Beta-galactoside transacetylase. *Chloramphenicol acetyltransferase. *N-acetyltransferase * ... 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ... The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons ...
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsTechnology, Industry, AgricultureInformation Science
Acetyl Coenzyme AAcetyltransferasesAcetyl-CoA CarboxylaseCoenzyme AHistone AcetyltransferasesCholine O-AcetyltransferasePyruvate CarboxylaseAcetylationChloramphenicol O-AcetyltransferaseAcetate-CoA LigaseAcetatesATP Citrate (pro-S)-LyaseCarnitine O-AcetyltransferaseLigasesBiotinp300-CBP Transcription FactorsAcetylcarnitineAcetyl-CoA C-AcetyltransferaseMolecular Sequence DataSerine O-AcetyltransferaseN-Terminal Acetyltransferase AMagnesium CompoundsN-Terminal Acetyltransferase EMalonyl Coenzyme ADihydrolipoyllysine-Residue AcetyltransferaseLiverPromoter Regions, GeneticFatty Acid SynthasesBase SequenceRhizobium etliTranscription, GeneticFatty AcidsKineticsCarbon IsotopesCitratesAmino Acid SequenceMevalonic AcidHistonesCaprylatesAcetylesteraseEscherichia coliRNA, MessengerAMP-Activated Protein KinasesPhosphate AcetyltransferasePyruvate Dehydrogenase ComplexMultienzyme ComplexesLipid MetabolismAcyl Coenzyme APlasmidsSaccharomyces cerevisiae ProteinsCREB-Binding ProteinCitric Acid CycleTransfectionCloning, MolecularN-Terminal AcetyltransferasesTranscription FactorsE1A-Associated p300 ProteinGlucoseAcyltransferasesOrganophosphatesGene Expression RegulationCytosolMitochondria, LiverSpermineCatalysisCell LineN-Terminal Acetyltransferase BSubstrate SpecificityBinding SitesNuclear ProteinsLysineCarbon RadioisotopesAdenosine TriphosphateCarnitineRats, Inbred StrainsVesicular Acetylcholine Transport ProteinsSpermidineRegulatory Sequences, Nucleic AcidMutationAdipose TissuePolyaminesTranscriptional ActivationDNA-Binding ProteinsGene Expression Regulation, EnzymologicCholinergic FibersCoenzyme A-TransferasesProtein BindingDietary CarbohydratesCoenzyme A LigasesEnzyme ActivationRestriction MappingRecombinant Fusion ProteinsTrans-ActivatorsCysteine SynthaseLipidsOxidation-ReductionChromatinSaccharomyces cerevisiaeAcetylcholinesteraseEnhancer Elements, GeneticPhosphorylationInsulinRecombinant ProteinsGlucosamine 6-Phosphate N-AcetyltransferasePlatelet Activating FactorSequence Homology, Amino AcidHydroxymethylglutaryl CoA ReductasesAmino-Acid N-AcetyltransferaseHeLa CellsDNAAcetate KinaseGenes, ReporterCells, CulturedHistone DeacetylasesEnergy MetabolismAnacardic AcidsChloramphenicol ResistanceProtein Structure, TertiaryChloramphenicolDietary FatsArylamine N-AcetyltransferaseGenes, RegulatorGenesPhenylacetatesGenes, BacterialGene ExpressionTumor Cells, CulturedMuscle, SkeletalEnzyme InductionCholineCell NucleusBacterial ProteinsMutagenesis, Site-DirectedBiogenic PolyaminesNucleosomesAcetylcholineCell Cycle ProteinsSequence AlignmentDNA PrimersPantothenic AcidCholinergic NeuronsRepressor ProteinsSubstantia InnominataPutrescineGeobacillus stearothermophilusEuonymusSequence Homology, Nucleic AcidBlotting, NorthernElectrophoresis, Polyacrylamide GelMolecular WeightSequence DeletionFungal ProteinsGene Expression Regulation, FungalModels, MolecularPalmitoyl Coenzyme AStructure-Activity RelationshipProtein BiosynthesisDNA, ComplementaryAcetyl-CoA C-AcyltransferaseEstersOrnithine DecarboxylaseOligodeoxyribonucleotidesHydroxamic AcidsGene Expression Regulation, ViralGenetic Complementation TestThioctic AcidTime FactorsChromatin Assembly and DisassemblyProtein Processing, Post-TranslationalParasympathetic Nervous SystemGenetic VectorsCrystallography, X-RayGenes, ViralNitrophenolsPyruvatesThiolester HydrolasesChromatography, High Pressure LiquidHydrogen-Ion ConcentrationGene DeletionN-Terminal Acetyltransferase FPolymerase Chain ReactionDrug Resistance, MicrobialPantetheineProtein KinasesGene Expression Regulation, BacterialSirtuinsCarnitine AcyltransferasesMethylationRepetitive Sequences, Nucleic AcidPhenotypeCatalytic DomainHemicholinium 3IsoenzymesChromosome DeletionPropionatesChemistryPlumbaginaceaeMice, TransgenicUridine Diphosphate N-AcetylglucosamineNeuronsCarrier Proteins
Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast,...Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast,...
keywords = "3-ketoacyl-CoA thiolase, Acetoacetyl-CoA thiolase, Candida tropicalis, Cytosol, Mevalonate, Peroxisome", ... Ueda M, Kanayama N, Tanaka A. Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane- ... Ueda, M, Kanayama, N & Tanaka, A 2000, Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n- ... Ueda, M., Kanayama, N., & Tanaka, A. (2000). Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes ...
okayama.pure.elsevier.com
Defining the extreme substrate specificity of Euonymus alatus diacylglycerol acetyltransferase, an unusual membrane-bound O...Defining the extreme substrate specificity of Euonymus alatus diacylglycerol acetyltransferase, an unusual membrane-bound O...
EaDAcT transfers the acetyl group from acetyl-CoA to sn-1,2-diacylglycerol (DAG) to produce acetyl-TAG. In vitro assays ... Keywords: Acetyl-Tags; Acetyltransferase; Mboat; Substrate Specificity; Triacylglycerols; Positional-Species Composition. ... Euonymus alatus diacylglycerol acetyltransferase (EaDAcT) synthesizes the unusually structured 3-acetyl-1,2-diacylglycerols ( ... This improved understanding of EaDAcT specificity confirms that the enzyme preferentially utilizes acetyl-CoA to acetylate sn-1 ...
krex.k-state.edu
Acetyl-CoA C-acetyltransferase - WikipediaAcetyl-CoA C-acetyltransferase - Wikipedia
CoA + acetoacetyl-CoA Hence, this enzyme has one substrate, acetyl-CoA, and two products, CoA and acetoacetyl-CoA. Acetyl-CoA C ... acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA:N-acetyltransferase, and thiolase II. This enzyme ... In enzymology, an acetyl-CoA C-acetyltransferase (EC 2.3.1.9) is an enzyme that catalyzes the chemical reaction 2 acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:acetyl-CoA C-acetyltransferase. Other names in common use include ...
en.wikipedia.org
phaA - Acetyl-CoA acetyltransferase - Zoogloea ramigera - phaA gene & proteinphaA - Acetyl-CoA acetyltransferase - Zoogloea ramigera - phaA gene & protein
2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation. ,p>Manual validated information which has been generated by ... mevalonate from acetyl-CoA.. Proteins known to be involved in the 3 steps of the subpathway in this organism are:. *Acetyl-CoA ... sp,P07097,THIL_ZOORA Acetyl-CoA acetyltransferase OS=Zoogloea ramigera GN=phaA PE=1 SV=4 ... mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis. ...
uniprot.org
Acetyl-CoA:N-acetyltransferase | definition of acetyl-CoA:N-acetyltransferase by Medical dictionaryAcetyl-CoA:N-acetyltransferase | definition of acetyl-CoA:N-acetyltransferase by Medical dictionary
What is acetyl-CoA:N-acetyltransferase? Meaning of acetyl-CoA:N-acetyltransferase medical term. What does acetyl-CoA:N- ... N-acetyltransferase in the Medical Dictionary? acetyl-CoA:N-acetyltransferase explanation free. ... redirected from acetyl-CoA:N-acetyltransferase) a·ce·tyl-CoA a·ce·tyl·trans·fer·ase. an acetyltransferase forming acetoacetyl- ... Acetyl-CoA:N-acetyltransferase , definition of acetyl-CoA:N-acetyltransferase by Medical dictionary https://medical-dictionary. ...
medical-dictionary.thefreedictionary.com
Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D | Disease page | IUPHAR/BPS Guide to PHARMACOLOGYAcetyl-CoA acetyltransferase-2 deficiency; ACAT2D | Disease page | IUPHAR/BPS Guide to PHARMACOLOGY
Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D disease page. Quantitative data and detailed annnotation of the targets of ... Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D. GtoPdb Disease Summaries. This section gives an overview of the disease, and ... No ligand related data available for Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D ...
guidetopharmacology.org
Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac...Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac...
Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ...
biochemj.org
Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat...Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat...
In addition, the enzyme preferred acetyl-CoA to palmitoyl-CoA or oleoyl-CoA as substrate. ... acetyl-CoA acetyltransferase from rat spleen. J Gomez-Cambronero, S Velasco, M Sanchez-Crespo, F Vivanco, J M Mato ... The enzyme 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine: acetyl-CoA acetyltransferase (EC 2.3.1.67) was purified from rat ... Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat ...
biochemj.org
ACAT1 elisa kit | Mouse Acetyl-CoA acetyltransferase ELISA Kit-NP 659033.1ACAT1 elisa kit | Mouse Acetyl-CoA acetyltransferase ELISA Kit-NP 659033.1
Mouse Acetyl-CoA acetyltransferase ELISA Kit-NP_659033.1 (MBS285428) product datasheet at MyBioSource, ELISA Kits ... Biological Process: acetyl-CoA biosynthetic process; acetyl-CoA catabolic process; coenzyme A biosynthetic process; coenzyme A ... Molecular Function: acetyl-CoA C-acetyltransferase activity; carbon-carbon lyase activity; catalytic activity; coenzyme binding ... 1. Data show that microRNA miR-467b regulates the acetyl-CoA acetyltransferase 1 (ACAT1) expression via targeting ACAT1 3 ...
mybiosource.com
Acetyl CoA-deacetylcephalosporin C acetyltransferase: Definition with Acetyl CoA-deacetylcephalosporin C acetyltransferase...Acetyl CoA-deacetylcephalosporin C acetyltransferase: Definition with Acetyl CoA-deacetylcephalosporin C acetyltransferase...
Definition of Acetyl CoA-deacetylcephalosporin C acetyltransferase with photos and pictures, translations, sample usage, and ... acetyl-CoA c-acyltransferase. acetyl-CoA carboxylase. acetyl-CoA deacylase. acetyl-CoA hydrolase. acetyl-CoA ligase. acetyl-CoA ... Lexicographical Neighbors of Acetyl CoA-deacetylcephalosporin C Acetyltransferase. acetyl-CoA acylase. acetyl-CoA ... acetyl CoA carboxylase phosphatase. acetyl chloride. acetyl group. acetyl methylcarbinol. acetyl phosphate. acetyl radical. ...
lexic.us
Antibody Database - Reagents for the antigen ACAT1 / acetyl-CoA acetyltransferase 1 stained with Alkaline Phosphatase (AP)Antibody Database - Reagents for the antigen 'ACAT1 / acetyl-CoA acetyltransferase 1' stained with 'Alkaline Phosphatase (AP)'
... acetyl-CoA acetyltransferase 1 stained with Alkaline Phosphatase (AP) in the Antibody Database ... acetyl-CoA acetyltransferase 1 Alkaline Phosphatase (AP) Antibodies. Antibodies in the Chromocyte database for ACAT1 / acetyl- ...
chromocyte.com
Rv3546 Probable acetyl-CoA acetyltransferase FadA5 (EC 2.3.1.9) | MTB Network PortalRv3546 Probable acetyl-CoA acetyltransferase FadA5 (EC 2.3.1.9) | MTB Network Portal
Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. ... Probable acetyl-CoA acetyltransferase FadA5 (EC 2.3.1.9) CDS 3985557 3986732 + 1 176 391 FALSE ... Rv3546 (Probable acetyl-CoA acetyltransferase FadA5 (EC 2.3.1.9)) is predicted to be co-regulated in modules bicluster_0166 ... Acetyl-CoA C-acetyltransferase Reductive carboxylate cycle (CO2 fixation), Lysine degradation, Butanoate metabolism, Pyruvate ...
networks.systemsbiology.net
ACAT1 Gene - GeneCards | THIL Protein | THIL AntibodyACAT1 Gene - GeneCards | THIL Protein | THIL Antibody
Acetyl-CoA Acetyltransferase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... ACAT1 (Acetyl-CoA Acetyltransferase 1) is a Protein Coding gene. Diseases associated with ACAT1 include Alpha-Methylacetoacetic ... 2 acetyl-CoA = CoA + acetoacetyl-CoA. *THIL_HUMAN,P24752. UniProtKB/Swiss-Prot EnzymeRegulation: Activated by potassium ions, ... a mitochondrially localized enzyme that catalyzes the reversible formation of acetoacetyl-CoA from two molecules of acetyl-CoA ...
genecards.org
Frontiers | In Salmonella enterica, OatA (Formerly YjgM) Uses O-Acetyl-Serine and Acetyl-CoA to Synthesize N,O-Diacetylserine,...Frontiers | In Salmonella enterica, OatA (Formerly YjgM) Uses O-Acetyl-Serine and Acetyl-CoA to Synthesize N,O-Diacetylserine,...
... consistent with the conclusion that OatA is an N-acetyltransferase, not an O-acetyltransferase. Binding of OAS to OatA appears ... at the expense of acetyl-CoA. We isolated OatA to homogeneity and performed its initial biochemical characterization. The ... at the expense of acetyl-CoA. We isolated OatA to homogeneity and performed its initial biochemical characterization. The ... consistent with the conclusion that OatA is an N-acetyltransferase, not an O-acetyltransferase. Binding of OAS to OatA appears ...
frontiersin.org
Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA :: MPG.PuRe Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA :: MPG.PuRe
Atomic resolution structure of human alpha-tubulin acetyltransferase,br/, bound to acetyl-CoA ... Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA ... human alpha-tubulin acetyltransferase bound to acetyl-CoA. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES ... we present the structure of the human alpha-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at ...
pubman.mpdl.mpg.de
Acetyl CoA acetyltransferase 2 deficiency | Genetic and Rare Diseases Information Center (GARD) - an NCATS ProgramAcetyl CoA acetyltransferase 2 deficiency | Genetic and Rare Diseases Information Center (GARD) - an NCATS Program
... resources and questions answered by our Genetic and Rare Diseases Information Specialists for Acetyl CoA acetyltransferase 2 ... Acetyl CoA acetyltransferase 2 deficiency Title Other Names:. ACAT2; Acetocoenzyme A acetyltransferase 2; Acetoacetyl CoA ... PubMed is a searchable database of medical literature and lists journal articles that discuss Acetyl CoA acetyltransferase 2 ...
phgkb.cdc.gov
pta - Phosphate acetyltransferase - Helicobacter pylori (strain J99 / ATCC 700824) - pta gene & proteinpta - Phosphate acetyltransferase - Helicobacter pylori (strain J99 / ATCC 700824) - pta gene & protein
... acetyl-CoA biosynthesis. This protein is involved in step 2 of the subpathway that synthesizes acetyl-CoA from acetate.. ... Phosphate acetyltransferase (pta). This subpathway is part of the pathway acetyl-CoA biosynthesis, which is itself part of ... Acetyl-CoA + phosphate = CoA + acetyl phosphate.. ,p>This subsection of the ,a href="http://www.uniprot.org/help/function_ ... View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from acetate, ...
uniprot.org
Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts. - Test catalog - Centro de...Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts. - Test catalog - Centro de...
Acetyl-CoA:alpha-glucosaminide N-acetyltransferase 50 - 171. nmol/h/mg prot.. ... Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts.. Fee code: 16025 ... Home > Test catalog > Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts. ...
cdb.hospitalclinic.org
Zeitschrift für Naturforschung CZeitschrift für Naturforschung C
Acetyl-CoA:4-Hydroxybutinylbithiophene O-Acetyltransferase Isoenzymes from Tagetes patula Seedlings. Metschulat, Gernot / ...
degruyter.com
Integrated metabolome and transcriptome analysis of Magnolia champaca identifies biosynthetic pathways for floral volatile...Integrated metabolome and transcriptome analysis of Magnolia champaca identifies biosynthetic pathways for floral volatile...
... acetyl-CoA acetyltransferase; HMGS, hydroxymethylglutaryl-CoA synthase; HMGR, hydroxymethylglutaryl-CoA reductase; MVK, ... 4-coumaroyl-CoA ligase; CCoAOMT, caffeoyl-CoA 3-O-methyltransferase; CCR, cinnamoyl-CoA reductase; CAD, cinnamyl alcohol ...
ncbi.nlm.nih.gov
ACAT1 gene: MedlinePlus GeneticsACAT1 gene: MedlinePlus Genetics
acetyl-CoA acetyltransferase 1 To use the sharing features on this page, please enable JavaScript.. ... It converts a molecule called 2-methyl-acetoacetyl-CoA into two smaller molecules, propionyl-CoA and acetyl-CoA, that can be ... The enzyme converts a molecule called acetoacetyl-CoA into two molecules of acetyl-CoA, which can be used to produce energy. In ... Structure and expression of the human mitochondrial acetoacetyl-CoA thiolase-encoding gene. Gene. 1991 Dec 30;109(2):285-90. ...
medlineplus.gov
CHAT gene: MedlinePlus GeneticsCHAT gene: MedlinePlus Genetics
acetyl CoA:choline O-acetyltransferase. *CHOACTASE. *choline acetylase. *CLAT_HUMAN. *CMS1A. Additional Information & Resources ... The CHAT gene provides instructions for making a protein called choline acetyltransferase. This protein is located at the ends ... Choline acetyltransferase facilitates the production of a molecule called acetylcholine. Acetylcholine is essential for normal ... The mutations lead to decreased production of choline acetyltransferase or the production of a protein with decreased ability ...
medlineplus.gov
RCSB PDB - 2WKV: BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316D MUTANT WITH COENZYME A.RCSB PDB - 2WKV: BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316D MUTANT WITH COENZYME A.
ACETYL-COA ACETYLTRANSFERASE. A, B, C, D. 392. Zoogloea ramigera. Mutation(s): 1 Gene Names: phaA, phbA. EC: 2.3.1.9. ... The latter intermediate is formed when the alpha-carbanion of acetyl-CoA enolate reacts with the carbonyl carbon of acetyl- ... COA. Query on COA. Download CCD File A, B, C, D. COENZYME A. C21 H36 N7 O16 P3 S. RGJOEKWQDUBAIZ-IBOSZNHHSA-N. Ligand ... The biosynthetic thiolase catalyzes a Claisen condensation reaction between acetyl-CoA and the enzyme acetylated at Cys89. Two ...
rcsb.org
Treesearch - scientific articles written or published by the U.S. Forest ServiceTreesearch - scientific articles written or published by the U.S. Forest Service
acetoacetyl-CoA, acetyl-CoA acetyltransferase, b-oxidation, ectomycorrhizae, Laccaria bicolor, Pinus resinosa, symbiosis ... Symbiosis-regulated expression of an acetyl-CoA acetyltransferase gene in the ectomycorrhizal fungus Laccaria bicolor. The ...
fs.usda.gov
CELL-FREE PREPARATION OF CARBAPENEMS - GreenLight Biosciences, Inc.CELL-FREE PREPARATION OF CARBAPENEMS - GreenLight Biosciences, Inc.
... an acetyl-CoA acetyltransferase, a beta-oxidation multi-enzyme, a crotonyl-CoA reductase, an acetyl-CoA carboxylase, a malonyl- ... an acetyl-CoA acetyltransferase, a beta-oxidation multi-enzyme, a crotonyl-CoA reductase, an acetyl-CoA carboxylase, a malonyl- ... an acetyl-CoA acetyltransferase, a beta-oxidation multi-enzyme, a crotonyl-CoA reductase, an acetyl-CoA carboxylase, a malonyl- ... an acetyl-CoA acetyltransferase, a beta-oxidation multi-enzyme, a crotonyl-CoA reductase, an acetyl-CoA carboxylase, a malonyl- ...
freepatentsonline.com
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsTechnology, Industry, AgricultureInformation Science
Acetyl Coenzyme AAcetyltransferasesAcetyl-CoA CarboxylaseCoenzyme AHistone AcetyltransferasesCholine O-AcetyltransferasePyruvate CarboxylaseAcetylationChloramphenicol O-AcetyltransferaseAcetate-CoA LigaseAcetatesATP Citrate (pro-S)-LyaseCarnitine O-AcetyltransferaseLigasesBiotinp300-CBP Transcription FactorsAcetylcarnitineAcetyl-CoA C-AcetyltransferaseMolecular Sequence DataSerine O-AcetyltransferaseN-Terminal Acetyltransferase AMagnesium CompoundsN-Terminal Acetyltransferase EMalonyl Coenzyme ADihydrolipoyllysine-Residue AcetyltransferaseLiverPromoter Regions, GeneticFatty Acid SynthasesBase SequenceRhizobium etliTranscription, GeneticFatty AcidsKineticsCarbon IsotopesCitratesAmino Acid SequenceMevalonic AcidHistonesCaprylatesAcetylesteraseEscherichia coliRNA, MessengerAMP-Activated Protein KinasesPhosphate AcetyltransferasePyruvate Dehydrogenase ComplexMultienzyme ComplexesLipid MetabolismAcyl Coenzyme APlasmidsSaccharomyces cerevisiae ProteinsCREB-Binding ProteinCitric Acid CycleTransfectionCloning, MolecularN-Terminal AcetyltransferasesTranscription FactorsE1A-Associated p300 ProteinGlucoseAcyltransferasesOrganophosphatesGene Expression RegulationCytosolMitochondria, LiverSpermineCatalysisCell LineN-Terminal Acetyltransferase BSubstrate SpecificityBinding SitesNuclear ProteinsLysineCarbon RadioisotopesAdenosine TriphosphateCarnitineRats, Inbred StrainsVesicular Acetylcholine Transport ProteinsSpermidineRegulatory Sequences, Nucleic AcidMutationAdipose TissuePolyaminesTranscriptional ActivationDNA-Binding ProteinsGene Expression Regulation, EnzymologicCholinergic FibersCoenzyme A-TransferasesProtein BindingDietary CarbohydratesCoenzyme A LigasesEnzyme ActivationRestriction MappingRecombinant Fusion ProteinsTrans-ActivatorsCysteine SynthaseLipidsOxidation-ReductionChromatinSaccharomyces cerevisiaeAcetylcholinesteraseEnhancer Elements, GeneticPhosphorylationInsulinRecombinant ProteinsGlucosamine 6-Phosphate N-AcetyltransferasePlatelet Activating FactorSequence Homology, Amino AcidHydroxymethylglutaryl CoA ReductasesAmino-Acid N-AcetyltransferaseHeLa CellsDNAAcetate KinaseGenes, ReporterCells, CulturedHistone DeacetylasesEnergy MetabolismAnacardic AcidsChloramphenicol ResistanceProtein Structure, TertiaryChloramphenicolDietary FatsArylamine N-AcetyltransferaseGenes, RegulatorGenesPhenylacetatesGenes, BacterialGene ExpressionTumor Cells, CulturedMuscle, SkeletalEnzyme InductionCholineCell NucleusBacterial ProteinsMutagenesis, Site-DirectedBiogenic PolyaminesNucleosomesAcetylcholineCell Cycle ProteinsSequence AlignmentDNA PrimersPantothenic AcidCholinergic NeuronsRepressor ProteinsSubstantia InnominataPutrescineGeobacillus stearothermophilusEuonymusSequence Homology, Nucleic AcidBlotting, NorthernElectrophoresis, Polyacrylamide GelMolecular WeightSequence DeletionFungal ProteinsGene Expression Regulation, FungalModels, MolecularPalmitoyl Coenzyme AStructure-Activity RelationshipProtein BiosynthesisDNA, ComplementaryAcetyl-CoA C-AcyltransferaseEstersOrnithine DecarboxylaseOligodeoxyribonucleotidesHydroxamic AcidsGene Expression Regulation, ViralGenetic Complementation TestThioctic AcidTime FactorsChromatin Assembly and DisassemblyProtein Processing, Post-TranslationalParasympathetic Nervous SystemGenetic VectorsCrystallography, X-RayGenes, ViralNitrophenolsPyruvatesThiolester HydrolasesChromatography, High Pressure LiquidHydrogen-Ion ConcentrationGene DeletionN-Terminal Acetyltransferase FPolymerase Chain ReactionDrug Resistance, MicrobialPantetheineProtein KinasesGene Expression Regulation, BacterialSirtuinsCarnitine AcyltransferasesMethylationRepetitive Sequences, Nucleic AcidPhenotypeCatalytic DomainHemicholinium 3IsoenzymesChromosome DeletionPropionatesChemistryPlumbaginaceaeMice, TransgenicUridine Diphosphate N-AcetylglucosamineNeuronsCarrier Proteins
ThiolaseACAT1CholineDehydrogenaseMitochondrial acetoacetyl-CoA thiolaseEnoyl-CoA hydraDeficiencyGeneAcyltransferaseSynthaseReactionSubpathway that synthesizesGenesHydrolaseFatty acid oxidCarnitineRecombinantAcetateSerineMoleculeBiosynthesisChloramphenicolLyaseSystematicLipidDiagramTrifunctional protein
Thiolase2
ACAT14
Choline16
Dehydrogenase9
Mitochondrial acetoacetyl-CoA thiolase1
Enoyl-CoA hydra3
  • LCHAD activity resides in a membrane-bound multienzyme complex that also contains long-chain 3-enoyl-CoA hydratase and longchain 3-ketoacyl-CoA thiolase activities (trifunctional protein) [10, (thefreedictionary.com)
  • 11. The recombinant cell of claim 9 or claim 10 wherein the cell exhibits increased activity compared to a wild-type control of one or more of: a thiolase, 3-hydroxy-3-methyl-glutaryl (HMG)-CoA synthase, HMG-CoA reductase, acyl-CoA ligase, or enoyl-CoA hydratase. (sumobrain.com)
  • 22. The recombinant cell of claim 11 wherein the enoyl-CoA hydratase comprises SidH. (sumobrain.com)
Deficiency2
Gene5
Acyltransferase1
Synthase1
Reaction6
Subpathway that synthesizes2
Genes2
Hydrolase1
Fatty acid oxid1
Carnitine19
  • The role of carnitine acetyltransferase (CrAT) in regulating cardiac energy metabolism is poorly understood. (biochemj.org)
  • The purpose of this study is to determine whether Acetyl L-carnitine can prevent the development of nerve damage, known as neuropathy, in individuals taking anti-HIV drugs over a 48-week p. (bioportfolio.com)
  • Acetyl L-carnitine is an amino acid that is an acetylated derivative of L-carnitine. (xtend-life.com)
  • Acetyl L-carnitine is only found in animal products, especially red meat. (xtend-life.com)
  • Mutton is the one of the most abundant dietary sources of acetyl L-carnitine. (xtend-life.com)
  • An acetyl group is transferred from acetyl co-enzyme A (CoA) to L-carnitine within cell mitochondria during strenuous exercise, primarily in the liver and kidneys. (xtend-life.com)
  • This process results in the conversion of acetyl-CoA to CoA and L-carnitine to acetyl L-carnitine. (xtend-life.com)
  • The acetyl L-carnitine is then transported outside the mitochondria, where it provides chemical energy when it breaks back down into L-carnitine and an acetyl group. (xtend-life.com)
  • In addition to its use in storing and transporting chemical energy, acetyl-L-carnitine has significant antioxidant activity. (xtend-life.com)
  • Acetyl L-carnitine is also a common dietary supplement. (xtend-life.com)
  • The primary advantage of using acetyl L-carnitine instead of L-carnitine is that acetyl L-carnitine has great bioavailability. (xtend-life.com)
  • The support of healthy energy levels is one of the most common reasons for taking acetyl L-carnitine. (xtend-life.com)
  • Acetyl-L-carnitine may be able to support normal memory functioning, especially in older people. (xtend-life.com)
  • Daily supplementation with acetyl L-carnitine may help support the central nervous system. (xtend-life.com)
  • Acetyl-L-carnitine may be able to manage the discomfort of chronic conditions affecting connective tissue. (xtend-life.com)
  • Athletes are one of the groups most likely to need acetyl-L-carnitine supplements, especially if they are distance runners or bodybuilders. (xtend-life.com)
  • The most common signs that acetyl L-carnitine may benefit you include discomfort in the chest and muscles. (xtend-life.com)
  • Low blood pressure and fatigue may also indicate that you need acetyl-L-carnitine. (xtend-life.com)
  • Mental conditions that may benefit from acetyl-L-carnitine include low moods and poor memory. (xtend-life.com)
Recombinant3
Acetate3
  • S. enterica synthesizes L -Cys de novo using a pathway that reduces sulfate (oxidation state 6 + ) to sulfide (oxidation state 2 - ) and then condenses O -acetyl-serine (OAS) with sulfide to yield L -Cys and acetate (Figure 1 ) ( Kredich, 2008 ). (frontiersin.org)
  • Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate. (rcsb.org)
  • The abbreviation "Ac" (or "AC") is also sometimes encountered in chemical formulas to indicate the acetate ion (CH 3 CO 2 − ), or the acetyl group (CH 3 CO). This abbreviation is not to be confused with the symbol of actinium , the first element of the actinide series. (wikipedia.org)
Serine3
  • Results from previous studies by others, suggested that OAS undergoes a spontaneous O - to N- migration to produce N -acetyl-serine (NAS), and that NAS is the true signal sensed by CysB. (frontiersin.org)
  • Work reported herein characterizes a S. enterica N -acetyltransferase, OatA (formerly YjgM), which acetylates the N α -amino group of OAS, producing N,O- diacetyl-serine (DAS) at the expense of acetyl-CoA. (frontiersin.org)
  • Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine. (cathdb.info)
Molecule2
Biosynthesis1
Chloramphenicol1
Lyase2
Systematic1
Lipid1
  • Platelet Activating Factor (PAF, 1-alkyl-2-acetyl- sn -glycero-3-phosphocholine) was first identified as a lipid mediator of inflammation and immunological response. (springer.com)
Diagram1
  • The acetyl group (indicated in blue in the structural diagram on the right) of acetyl-CoA is linked to the sulfhydryl substituent of the β-mercaptoethylamine group. (wikipedia.org)
Trifunctional protein1