Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.
An enzyme that catalyzes the formation of acetylcholine from acetyl-CoA and choline. EC
An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Formation of an acetyl derivative. (Stedman, 25th ed)
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.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
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.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC
An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.
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.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
The 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.
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.
Cellular proteins and protein complexes that transport amino acids across biological membranes.
The rate dynamics in chemical or physical systems.
Established cell cultures that have the potential to propagate indefinitely.
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.
Proteins prepared by recombinant DNA technology.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
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.
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.
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.
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.
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).
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
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.
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.
An essential amino acid. It is often added to animal feed.
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.
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
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.
The functional hereditary units of BACTERIA.
Amino acids containing an aromatic side chain.
Proteins found in any species of bacterium.
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.
The sum of the weight of all the atoms in a molecule.
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.
Amino acids which have a branched carbon chain.
An essential branched-chain amino acid important for hemoglobin formation.
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.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
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.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
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.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
Deletion of sequences of nucleic acids from the genetic material of an individual.
A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
The relationships of groups of organisms as reflected by their genetic makeup.
A member of the p300-CBP transcription factors that was originally identified as a binding partner for ADENOVIRUS E1A PROTEINS.
Transport proteins that carry specific substances in the blood or across cell membranes.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
A 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.
Enzymes that catalyze the transfer of an acetyl group, usually from ACETYL COENZYME A, to the N-terminus of a peptide chain.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
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.
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.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
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.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
Nucleic acid sequences involved in regulating the expression of genes.
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.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).
A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).
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.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
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.
Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
Nerve fibers liberating acetylcholine at the synapse after an impulse.
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
Proteins found in any species of fungus.
Amino acids with side chains that are positively charged at physiological pH.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
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
An essential amino acid that is physiologically active in the L-form.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Proteins found in any species of virus.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC
An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.
A sulfur-containing essential L-amino acid that is important in many body functions.
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.
A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.
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.
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.
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.
A method (first developed by E.M. Southern) for detection of DNA 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.
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.
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
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)
Genes which regulate or circumscribe the activity of other genes; specifically, genes which code for PROTEINS or RNAs which have GENE EXPRESSION REGULATION functions.
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.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
The functional hereditary units of VIRUSES.
Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin.
Cis-acting DNA sequences which can increase transcription of genes. Enhancers can usually function in either orientation and at various distances from a promoter.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
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.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Biochemical identification of mutational changes in a nucleotide sequence.
Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
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
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)
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
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.
Any method used for determining the location of and relative distances between genes on a chromosome.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
The functional hereditary units of FUNGI.
A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.
Amino acids with uncharged R groups or side chains.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
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.
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.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
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).
A group of 6-alkyl SALICYLIC ACIDS that are found in ANACARDIUM and known for causing CONTACT DERMATITIS.
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.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
An enzyme that catalyses the reaction of D-glucosamine 6-phosphate with ACETYL-COA to form N-acetylglucosamine 6-phosphate.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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.
Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.
Elements of limited time intervals, contributing to particular results or situations.
Sequences of DNA in the genes that are located between the EXONS. They are transcribed along with the exons but are removed from the primary gene transcript by RNA SPLICING to leave mature RNA. Some introns code for separate genes.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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)
Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected.
Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
Sites on an antigen that interact with specific antibodies.
A mitochondrial matrix enzyme that catalyzes the synthesis of L-GLUTAMATE to N-acetyl-L-glutamate in the presence of ACETYL-COA.
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.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
The process of cleaving a chemical compound by the addition of a molecule of water.
Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.

A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis: acetylglutamate synthase activity requires complex formation with acetylglutamate kinase. (1/65)

Open reading frame YJL071W of Saccharomyces cerevisiae was shown to be ARG2 and identified as the structural gene for acetylglutamate synthase, first step in arginine biosynthesis. The three Ascomycete acetylglutamate synthases characterized to date appear homologous, but unlike the other enzymes of the yeast arginine biosynthesis pathway, they showed no significant similarity to their prokaryotic equivalents. The measured synthase activity did not increase with the number of ARG2 gene copies unless the number of ARG5,6 gene copies was increased similarly. ARG5,6 encodes a precursor that is maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase, catalyzing the second and third steps in the pathway. The results imply that the synthase must interact stoichiometrically in vivo with the kinase, the reductase, or both to be active. Results obtained with synthetic ARG5 and ARG6 genes suggested that both the kinase and the reductase could be needed. This situation, which has completely escaped notice in yeast until now, is reminiscent of the observation in Neurospora crassa that nonsense arg-6 kinase/reductase mutants lack synthase activity (Hinde, R. W., Jacobson, J. A., Weiss, R. L., and Davis, R. H. (1986) J. Biol. Chem. 261, 5848-5852). In immunoprecipitation experiments, hemagglutinin-tagged synthase coprecipitated with a protein proven by microsequencing to be the kinase. Western blot analyses showed that the synthase has reduced stability in the absence of the kinase/reductase. Our data demonstrate the existence of a new yeast arginine metabolon involving at least the first two, and possibly the first three, enzymes of the pathway. Hypotheses regarding the biological significance of this interaction are discussed.  (+info)

Identification, cloning and expression of the mouse N-acetylglutamate synthase gene. (2/65)

In ureotelic animals, N-acetylglutamate (NAG) is an essential allosteric activator of carbamylphosphate synthetase I (CPSI), the first enzyme in the urea cycle. NAG synthase (NAGS; EC catalyses the formation of NAG from glutamate and acetyl-CoA in liver and intestinal mitochondria. This enzyme is supposed to regulate ureagenesis by producing variable amounts of NAG, thus modulating CPSI activity. Moreover, inherited deficiencies in NAGS have been associated with hyperammonaemia, probably due to the loss of CPSI activity. Although the existence of the NAGS protein in mammals has been known for decades, the gene has remained elusive. We identified the mouse (Mus musculus) and human NAGS genes using their similarity to the respective Neurospora crassa gene. NAGS was cloned from a mouse liver cDNA library and was found to encode a 2.3 kb message, highly expressed in liver and small intestine with lower expression levels in kidney, spleen and testis. The deduced amino acid sequence contains a putative mitochondrial targeting signal at the N-terminus. The cDNA sequence complements an argA (NAGS)-deficient Escherichia coli strain, reversing its arginine auxotrophy. His-tagged versions of the pre-protein and two putative mature proteins were each overexpressed in E. coli, and purified to apparent homogeneity by using a nickel-affinity column. The pre-protein and the two putative mature proteins catalysed the NAGS reaction but one of the putative mature enzymes had significantly higher activity than the pre-protein. The addition of l-arginine increased the catalytic activity of the purified recombinant NAGS enzymes by approx. 2-6-fold.  (+info)

The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis. (3/65)

In Saccharomyces cerevisiae, which uses the nonlinear pathway of arginine biosynthesis, the first two enzymes, N-acetylglutamate synthase (NAGS) and N-acetylglutamate kinase (NAGK), are controlled by feedback inhibition. We have previously shown that NAGS and NAGK associate in a complex, essential to synthase activity and protein level [Abadjieva, A., Pauwels, K., Hilven, P. & Crabeel, M. (2001) J. Biol. Chem.276, 42869-42880]. The NAGKs of ascomycetes possess, in addition to the catalytic domain that is shared by all other NAGKs and whose structure has been determined, a C-terminal domain of unknown function and structure. Exploring the role of these two domains in the synthase/kinase interaction, we demonstrate that the ascomycete-specific domain is required to maintain synthase activity and protein level. Previous results had suggested a participation of the third enzyme of the pathway, N-acetylglutamylphosphate reductase, in the metabolon. Here, genetic analyses conducted in yeast at physiological level, or in a heterologous background, clearly demonstrate that the reductase is dispensable for synthase activity and protein level. Most importantly, we show that the arginine feedback regulation of the NAGS and NAGK enzymes is mutually interdependent. First, the kinase becomes less sensitive to arginine feedback inhibition in the absence of the synthase. Second, and as in Neurospora crassa, in a yeast kinase mutant resistant to arginine feedback inhibition, the synthase becomes feedback resistant concomitantly. We conclude that the NAGS/NAGK metabolon promotes the co-ordination of the catalytic activities and feedback regulation of the first two, flux controlling, enzymes of the arginine pathway.  (+info)

Mammalian N-acetylglutamate synthase. (4/65)

N-Acetylglutamate synthase (NAGS, E.C. is a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG), an essential allosteric activator of carbamylphosphate synthetase I (CPSI). The mouse and human NAGS genes have been identified based on similarity to regions of NAGS from Neurospora crassa and cloned from liver cDNA libraries. These genes were shown to complement an argA- (NAGS) deficient Escherichia coli strain, and enzymatic activity of the proteins was confirmed by a new stable isotope dilution assay. The deduced amino acid sequence of mammalian NAGS contains a putative mitochondrial-targeting signal at the N-terminus. The mouse NAGS preprotein was overexpressed in insect cells to determine post-translational modifications and two processed proteins with different N-terminal truncations have been identified. Sequence analysis using a hidden Markov model suggests that the vertebrate NAGS protein contains domains with a carbamate kinase fold and an acyl-CoA N-acyltransferase fold, and protein crystallization experiments are currently underway. Inherited NAGS deficiency results in hyperammonemia, presumably due to the loss of CPSI activity. We, and others, have recently identified mutations in families with neonatal and late-onset NAGS deficiency and the identification of the gene has now made carrier testing and prenatal diagnosis feasible. A structural analog of NAG, carbamylglutamate, has been shown to bind and activate CPSI, and several patients have been reported to respond favorably to this drug (Carbaglu).  (+info)

Functional characterization of a novel ArgA from Mycobacterium tuberculosis. (5/65)

The Mycobacterium tuberculosis gene Rv2747 encodes a novel 19-kDa ArgA that catalyzes the initial step in L-arginine biosynthesis, namely the conversion of L-glutamate to alpha-N-acetyl-L-glutamate. Initial velocity studies reveal that Rv2747 proceeds through a sequential kinetic mechanism, with K(m) values of 280 mM for L-glutamine and 150 microM for acetyl-coenzyme A and with a k(cat) value of 200 min(-1). Initial velocity studies with L-glutamate showed that even at concentrations of 600 mM, saturation was not observed. Therefore, only a k(cat)/K(m) value of 125 M(-1) min(-1) can be calculated. Inhibition studies reveal that the enzyme is strongly regulated by L-arginine, the end product of the pathway (50% inhibitory concentration, 26 microM). The enzyme was completely inhibited by 500 microM arginine, with a Hill coefficient of 0.60, indicating negatively cooperative binding of L-arginine.  (+info)

Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies. (6/65)

The mitochondrial enzyme N-acetylglutamate synthase (NAGS) produces N-acetylglutamate serving as an allosteric activator of carbamylphosphate synthetase 1, the first enzyme of the urea cycle. Autosomal recessively inherited NAGS deficiency (NAGSD) leads to severe neonatal or late-onset hyperammonemia. To date few patients have been described and the gene involved was described only recently. In this study, another three families affected by NAGSD were analyzed for NAGS gene mutations resulting in the identification of three novel missense mutations (C200R [c.598T > C], S410P [c.1228T > C], A518T [c.1552G > A]). In order to investigate the effects of these three and two additional previously published missense mutations on enzyme activity, the mutated proteins were overexpressed in a bacterial expression system using the NAGS deficient E. coli strain NK5992. All mutated proteins showed a severe decrease in enzyme activity providing evidence for the disease-causing nature of the mutations. In addition, we expressed the full-length NAGS wild type protein including the mitochondrial leading sequence, the mature protein as well as a highly conserved core protein. NAGS activity was detected in all three recombinant proteins but varied regarding activity levels and response to stimulation by l-arginine. In conclusion, overexpression of wild type and mutated NAGS proteins in E. coli provides a suitable tool for functional analysis of NAGS deficiency.  (+info)

Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence. (7/65)

Type I signal-anchor sequences mediate translocation of the N-terminal domain (N-domain) across the endoplasmic reticulum (ER) membrane. To examine the translocation in detail, dihydrofolate reductase (DHFR) was fused to the N-terminus of synaptotagmin II as a long N-domain. Translocation was arrested by the DHFR ligand methotrexate, which stabilizes the folding of the DHFR domain, and resumed after depletion of methotrexate. The targeting of the ribosome-nascent chain complex to the ER requires GTP, whereas N-domain translocation does not require any nucleotide triphosphates. Significant translocation was observed even in the absence of a lumenal hsp70 (BiP). When the nascent polypeptide was released from the ribosomes after the membrane targeting, the N-domain translocation was suppressed and the nascent chain was released from the translocon. Ribosomes have a crucial role in maintaining the translocation-intermediate state. The translocation of the DHFR domain was greatly impaired when it was separated from the signal-anchor sequence. Unfolding and translocation of the DHFR domain must be driven by the stroke of the signal-anchor sequence into translocon.  (+info)

Involvement of LuxR, a quorum sensing regulator in Vibrio harveyi, in the promotion of metabolic genes: argA, purM, lysE and rluA. (8/65)

Quorum sensing, involving signal transduction via the two-component response regulator LuxO to its downstream target LuxR, controls luminescence in the marine bacterium Vibrio harveyi. LuxR is a DNA binding protein that acts as both activator of the lux operon and repressor of its own gene. In order to determine if any other genes are affected by quorum sensing in V. harveyi, an assay for luxR-dependent promotion was devised using a genomic library maintained in a novel luxAB (luciferase) reporter. Screening in Escherichia coli DH-21 (lacI(sq)) entailed the addition of a second plasmid containing luxR under plac control. Four out of 5000 colonies showed luminescence stimulation upon IPTG induction of luxR. The four luxR-dependent promoters were upstream of argA, purM, lysE, and rluA, genes involved in arginine and purine biosyntheses, amino acid efflux, and pseudouridine synthesis, respectively. Based on analysis of luxR-dependent promoters, particularly that of argA, we describe a LuxR binding site, and implicate the coordination of LuxR with ArgR.  (+info)

Some common effects of chromosomal deletions include:

1. Genetic disorders: Chromosomal deletions can lead to a variety of genetic disorders, such as Down syndrome, which is caused by a deletion of a portion of chromosome 21. Other examples include Prader-Willi syndrome (deletion of chromosome 15), and Williams syndrome (deletion of chromosome 7).
2. Birth defects: Chromosomal deletions can increase the risk of birth defects, such as heart defects, cleft palate, and limb abnormalities.
3. Developmental delays: Children with chromosomal deletions may experience developmental delays, learning disabilities, and intellectual disability.
4. Increased cancer risk: Some chromosomal deletions can increase the risk of developing certain types of cancer, such as chronic myelogenous leukemia (CML) and breast cancer.
5. Reproductive problems: Chromosomal deletions can lead to reproductive problems, such as infertility or recurrent miscarriage.

Chromosomal deletions can be diagnosed through a variety of techniques, including karyotyping (examination of the chromosomes), fluorescence in situ hybridization (FISH), and microarray analysis. Treatment options for chromosomal deletions depend on the specific effects of the deletion and may include medication, surgery, or other forms of therapy.

The diagnosis of Rubinstein-Taybi syndrome is based on a combination of clinical findings and genetic testing. Treatment for the condition typically involves a multidisciplinary approach, including physical therapy, speech therapy, and special education to address developmental delays and intellectual disability. In some cases, surgery may be necessary to correct congenital abnormalities or other medical issues.

The prognosis for Rubinstein-Taybi syndrome varies depending on the severity of the condition and the presence of any additional medical issues. Some individuals with the condition may have a relatively mild impact on their quality of life, while others may experience more significant challenges. Early diagnosis and intervention are important to help manage the condition and improve outcomes for affected individuals.

The following is a list of common features and characteristics associated with Rubinstein-Taybi syndrome:

1. Distinctive facial features, such as wide-set eyes, a small head, and a flat nasal bridge
2. Intellectual disability, ranging from mild to severe
3. Speech difficulties, including delayed speech development and difficulty articulating words
4. Congenital abnormalities, such as heart defects or limb differences
5. Short stature and small hands and feet
6. Delayed physical development, including delayed walking and sitting
7. Increased risk of infections due to immune system dysfunction
8. Vision and hearing problems
9. Sleep apnea and other respiratory issues
10. Behavioral challenges, such as anxiety and hyperactivity

It's important to note that every individual with Rubinstein-Taybi syndrome is unique and may experience a different combination of these features and characteristics. Some individuals may also have additional medical conditions or complications that can impact their quality of life. Early diagnosis and intervention are crucial to help manage the condition and improve outcomes for affected individuals.

There are several types of inborn errors of amino acid metabolism, including:

1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.

It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.

Ectromelia can be caused by genetic mutations or exposure to certain chemicals during pregnancy. Treatment for ectromelia typically involves managing the symptoms and addressing any underlying conditions. This may include medication to promote skin growth, physical therapy to improve mobility and strength, and speech and language therapy to improve communication skills. In severe cases, surgery may be necessary to repair malformed limbs or other physical abnormalities.

Ectromelia is also known as ectodermal dysplasia, a group of disorders that affect the ectodermal layers of the body (skin, hair, nails, and nervous system). The condition is relatively rare, occurring in approximately 1 in 100,000 births. With appropriate medical care and support, many individuals with ectromelia are able to lead fulfilling lives despite their physical limitations.

Examples of experimental liver neoplasms include:

1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and can be induced experimentally by injecting carcinogens such as diethylnitrosamine (DEN) or dimethylbenz(a)anthracene (DMBA) into the liver tissue of animals.
2. Cholangiocarcinoma: This type of cancer originates in the bile ducts within the liver and can be induced experimentally by injecting chemical carcinogens such as DEN or DMBA into the bile ducts of animals.
3. Hepatoblastoma: This is a rare type of liver cancer that primarily affects children and can be induced experimentally by administering chemotherapy drugs to newborn mice or rats.
4. Metastatic tumors: These are tumors that originate in other parts of the body and spread to the liver through the bloodstream or lymphatic system. Experimental models of metastatic tumors can be studied by injecting cancer cells into the liver tissue of animals.

The study of experimental liver neoplasms is important for understanding the underlying mechanisms of liver cancer development and progression, as well as identifying potential therapeutic targets for the treatment of this disease. Animal models can be used to test the efficacy of new drugs or therapies before they are tested in humans, which can help to accelerate the development of new treatments for liver cancer.

There are several different types of congenital myasthenic syndromes, each with its own unique set of symptoms and characteristics. Some of the most common include:

* Congenital myasthenic syndrome type 1 (CMS1): This is the most common type of CMS and is caused by a mutation in the CHRNA1 gene. It is characterized by muscle weakness, poor feeding, and delays in development.
* Congenital myasthenic syndrome type 2 (CMS2): This type is caused by a mutation in the CHRNB1 gene and is characterized by muscle weakness, cognitive impairment, and seizures.
* Congenital myasthenic syndrome type 3 (CMS3): This type is caused by a mutation in the MAP2 gene and is characterized by muscle weakness, developmental delays, and intellectual disability.

There is currently no cure for congenital myasthenic syndromes, but various treatments can help manage the symptoms. These may include physical therapy, occupational therapy, speech therapy, and medications such as acetylcholinesterase inhibitors and steroids. In some cases, a bone marrow transplant may be necessary.

The prognosis for individuals with congenital myasthenic syndromes varies depending on the specific type and severity of the disorder. Some individuals may have mild symptoms and lead relatively normal lives, while others may have more severe symptoms and require ongoing medical care and support. With appropriate treatment and management, many individuals with CMS can lead fulfilling lives.

1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.

2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.

3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.

4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.

5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.

6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.

7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.

8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.

9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.

10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.

There are several risk factors for developing HCC, including:

* Cirrhosis, which can be caused by heavy alcohol consumption, viral hepatitis (such as hepatitis B and C), or fatty liver disease
* Family history of liver disease
* Chronic obstructive pulmonary disease (COPD)
* Diabetes
* Obesity

HCC can be challenging to diagnose, as the symptoms are non-specific and can be similar to those of other conditions. However, some common symptoms of HCC include:

* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Loss of appetite
* Abdominal pain or discomfort
* Weight loss

If HCC is suspected, a doctor may perform several tests to confirm the diagnosis, including:

* Imaging tests, such as ultrasound, CT scan, or MRI, to look for tumors in the liver
* Blood tests to check for liver function and detect certain substances that are produced by the liver
* Biopsy, which involves removing a small sample of tissue from the liver to examine under a microscope

Once HCC is diagnosed, treatment options will depend on several factors, including the stage and location of the cancer, the patient's overall health, and their personal preferences. Treatment options may include:

* Surgery to remove the tumor or parts of the liver
* Ablation, which involves destroying the cancer cells using heat or cold
* Chemoembolization, which involves injecting chemotherapy drugs into the hepatic artery to reach the cancer cells
* Targeted therapy, which uses drugs or other substances to target specific molecules that are involved in the growth and spread of the cancer

Overall, the prognosis for HCC is poor, with a 5-year survival rate of approximately 20%. However, early detection and treatment can improve outcomes. It is important for individuals at high risk for HCC to be monitored regularly by a healthcare provider, and to seek medical attention if they experience any symptoms.

1. Activation of oncogenes: Some viruses contain genes that code for proteins that can activate existing oncogenes in the host cell, leading to uncontrolled cell growth.
2. Inactivation of tumor suppressor genes: Other viruses may contain genes that inhibit the expression of tumor suppressor genes, allowing cells to grow and divide uncontrollably.
3. Insertional mutagenesis: Some viruses can insert their own DNA into the host cell's genome, leading to disruptions in normal cellular function and potentially causing cancer.
4. Epigenetic changes: Viral infection can also cause epigenetic changes, such as DNA methylation or histone modification, that can lead to the silencing of tumor suppressor genes and the activation of oncogenes.

Viral cell transformation is a key factor in the development of many types of cancer, including cervical cancer caused by human papillomavirus (HPV), and liver cancer caused by hepatitis B virus (HBV). In addition, some viruses are specifically known to cause cancer, such as Kaposi's sarcoma-associated herpesvirus (KSHV) and Merkel cell polyomavirus (MCV).

Early detection and treatment of viral infections can help prevent the development of cancer. Vaccines are also available for some viruses that are known to cause cancer, such as HPV and hepatitis B. Additionally, antiviral therapy can be used to treat existing infections and may help reduce the risk of cancer development.

Neuroblastoma is caused by a genetic mutation that affects the development and growth of nerve cells. The cancerous cells are often sensitive to chemotherapy, but they can be difficult to remove surgically because they are deeply embedded in the nervous system.

There are several different types of neuroblastoma, including:

1. Infantile neuroblastoma: This type of neuroblastoma occurs in children under the age of one and is often more aggressive than other types of the cancer.
2. Juvenile neuroblastoma: This type of neuroblastoma occurs in children between the ages of one and five and tends to be less aggressive than infantile neuroblastoma.
3. Adult neuroblastoma: This type of neuroblastoma occurs in adults and is rare.
4. Metastatic neuroblastoma: This type of neuroblastoma has spread to other parts of the body, such as the bones or liver.

Symptoms of neuroblastoma can vary depending on the location and size of the tumor, but they may include:

* Abdominal pain
* Fever
* Loss of appetite
* Weight loss
* Fatigue
* Bone pain
* Swelling in the abdomen or neck
* Constipation
* Increased heart rate

Diagnosis of neuroblastoma typically involves a combination of imaging tests, such as CT scans and MRI scans, and biopsies to confirm the presence of cancerous cells. Treatment for neuroblastoma usually involves a combination of chemotherapy, surgery, and radiation therapy. The prognosis for neuroblastoma varies depending on the type of cancer, the age of the child, and the stage of the disease. In general, the younger the child and the more aggressive the treatment, the better the prognosis.

Body weight is an important health indicator, as it can affect an individual's risk for certain medical conditions, such as obesity, diabetes, and cardiovascular disease. Maintaining a healthy body weight is essential for overall health and well-being, and there are many ways to do so, including a balanced diet, regular exercise, and other lifestyle changes.

There are several ways to measure body weight, including:

1. Scale: This is the most common method of measuring body weight, and it involves standing on a scale that displays the individual's weight in kg or lb.
2. Body fat calipers: These are used to measure body fat percentage by pinching the skin at specific points on the body.
3. Skinfold measurements: This method involves measuring the thickness of the skin folds at specific points on the body to estimate body fat percentage.
4. Bioelectrical impedance analysis (BIA): This is a non-invasive method that uses electrical impulses to measure body fat percentage.
5. Dual-energy X-ray absorptiometry (DXA): This is a more accurate method of measuring body composition, including bone density and body fat percentage.

It's important to note that body weight can fluctuate throughout the day due to factors such as water retention, so it's best to measure body weight at the same time each day for the most accurate results. Additionally, it's important to use a reliable scale or measuring tool to ensure accurate measurements.

Explanation: Neoplastic cell transformation is a complex process that involves multiple steps and can occur as a result of genetic mutations, environmental factors, or a combination of both. The process typically begins with a series of subtle changes in the DNA of individual cells, which can lead to the loss of normal cellular functions and the acquisition of abnormal growth and reproduction patterns.

Over time, these transformed cells can accumulate further mutations that allow them to survive and proliferate despite adverse conditions. As the transformed cells continue to divide and grow, they can eventually form a tumor, which is a mass of abnormal cells that can invade and damage surrounding tissues.

In some cases, cancer cells can also break away from the primary tumor and travel through the bloodstream or lymphatic system to other parts of the body, where they can establish new tumors. This process, known as metastasis, is a major cause of death in many types of cancer.

It's worth noting that not all transformed cells will become cancerous. Some forms of cellular transformation, such as those that occur during embryonic development or tissue regeneration, are normal and necessary for the proper functioning of the body. However, when these transformations occur in adult tissues, they can be a sign of cancer.

See also: Cancer, Tumor

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Hartnup disease is a rare genetic disorder that affects the body's ability to absorb vitamin B12 (cobalamin) and other nutrients. It is caused by a mutation in the HCN1 gene, which codes for a protein involved in the transport of cobalamin into the cells.

Symptoms of Hartnup Disease:

The symptoms of Hartnup disease can vary in severity and may include:

* Fatigue
* Weakness
* Pale skin
* Shortness of breath
* Dizziness
* Headaches
* Numbness or tingling in the hands and feet
* Seizures
* Poor appetite
* Diarrhea

Complications of Hartnup Disease:

If left untreated, Hartnup disease can lead to complications such as:

* Anemia (low red blood cell count)
* Nerve damage
* Skin problems
* Eye problems
* Hearing loss
* Increased risk of infections

Treatment of Hartnup Disease:

The treatment of Hartnup disease typically involves a combination of dietary changes and supplements. Patients with the condition may need to follow a strict diet that includes foods high in vitamin B12, such as meat, fish, and dairy products. They may also need to take supplements to ensure they are getting enough of this important nutrient. In some cases, medication may be prescribed to help manage symptoms.

Prognosis of Hartnup Disease:

The prognosis for Hartnup disease is generally good if the condition is diagnosed and treated early. With proper management, most patients with Hartnup disease can lead active and healthy lives. However, if left untreated, the condition can have serious complications that can be difficult to reverse.

Inheritance Pattern of Hartnup Disease:

Hartnup disease is an autosomal recessive disorder, which means that a person must inherit two copies of the mutated HCN1 gene (one from each parent) in order to develop the condition. If a person inherits only one copy of the mutated gene, they will be a carrier of the condition but are unlikely to develop symptoms themselves. Carriers of Hartnup disease can pass the mutated gene on to their children, who have a 25% chance of inheriting two copies of the gene and developing the condition.

Prevention of Hartnup Disease:

There is no known prevention for Hartnup disease. However, if a person knows they are a carrier of the condition, they can work with their healthcare provider to ensure they are getting enough vitamin B12 and monitoring their diet to prevent any complications.

In conclusion, Hartnup disease is a rare genetic disorder that affects the absorption of vitamin B12 in the small intestine. It can cause a range of symptoms, including diarrhea, abdominal pain, and fatigue. Treatment typically involves a combination of dietary changes and supplements, and early diagnosis and management can lead to a good prognosis. However, if left untreated, the condition can have serious complications. If you suspect you or someone you know may be experiencing symptoms of Hartnup disease, it is important to speak with a healthcare provider for proper diagnosis and treatment.

Cystinuria is caused by mutations in the SLC7A9 gene, which codes for a protein involved in the transport of cystine across the brush border membrane of renal tubular cells. The disorder is inherited in an autosomal recessive pattern, meaning that affected individuals must inherit two copies of the mutated gene (one from each parent) to develop symptoms.

There is no cure for cystinuria, but various treatments can help manage its symptoms. These may include medications to reduce the acidity of the urine and prevent infection, as well as surgical procedures to remove stones or repair damaged kidneys. In some cases, a kidney transplant may be necessary.

It's important for individuals with cystinuria to drink plenty of water and maintain good hydration to help flush out the urinary tract and prevent stone formation. They should also avoid certain foods that may increase the risk of stone formation, such as oxalate-rich foods like spinach and rhubarb.

Overall, while there is no cure for cystinuria, with proper management and care, individuals with this disorder can lead relatively normal lives and minimize the complications associated with it.

Some examples of musculoskeletal abnormalities include:

- Carpal tunnel syndrome: Compression of the median nerve in the wrist that can cause numbness, tingling, and weakness in the hand and arm.

- Kyphosis: An exaggerated curvature of the spine, often resulting from osteoporosis or other conditions that affect the bones.

- Osteoarthritis: Wear and tear on the joints, leading to pain, stiffness, and limited mobility.

- Clubfoot: A congenital deformity in which the foot is turned inward or outward.

- Scoliosis: An abnormal curvature of the spine that can be caused by genetics, injury, or other factors.

Musculoskeletal abnormalities can be diagnosed through physical examination, imaging tests such as X-rays and MRIs, and other diagnostic procedures. Treatment options vary depending on the specific condition but may include medication, physical therapy, braces or orthotics, or surgery in severe cases.

Liver neoplasms, also known as liver tumors or hepatic tumors, are abnormal growths of tissue in the liver. These growths can be benign (non-cancerous) or malignant (cancerous). Malignant liver tumors can be primary, meaning they originate in the liver, or metastatic, meaning they spread to the liver from another part of the body.

There are several types of liver neoplasms, including:

1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and arises from the main cells of the liver (hepatocytes). HCC is often associated with cirrhosis and can be caused by viral hepatitis or alcohol abuse.
2. Cholangiocarcinoma: This type of cancer arises from the cells lining the bile ducts within the liver (cholangiocytes). Cholangiocarcinoma is rare and often diagnosed at an advanced stage.
3. Hemangiosarcoma: This is a rare type of cancer that originates in the blood vessels of the liver. It is most commonly seen in dogs but can also occur in humans.
4. Fibromas: These are benign tumors that arise from the connective tissue of the liver (fibrocytes). Fibromas are usually small and do not spread to other parts of the body.
5. Adenomas: These are benign tumors that arise from the glandular cells of the liver (hepatocytes). Adenomas are usually small and do not spread to other parts of the body.

The symptoms of liver neoplasms vary depending on their size, location, and whether they are benign or malignant. Common symptoms include abdominal pain, fatigue, weight loss, and jaundice (yellowing of the skin and eyes). Diagnosis is typically made through a combination of imaging tests such as CT scans, MRI scans, and ultrasound, and a biopsy to confirm the presence of cancer cells.

Treatment options for liver neoplasms depend on the type, size, location, and stage of the tumor, as well as the patient's overall health. Surgery may be an option for some patients with small, localized tumors, while others may require chemotherapy or radiation therapy to shrink the tumor before surgery can be performed. In some cases, liver transplantation may be necessary.

Prognosis for liver neoplasms varies depending on the type and stage of the cancer. In general, early detection and treatment improve the prognosis, while advanced-stage disease is associated with a poorer prognosis.

The symptoms of Alzheimer's disease can vary from person to person and may progress slowly over time. Early symptoms may include memory loss, confusion, and difficulty with problem-solving. As the disease progresses, individuals may experience language difficulties, visual hallucinations, and changes in mood and behavior.

There is currently no cure for Alzheimer's disease, but there are several medications and therapies that can help manage its symptoms and slow its progression. These include cholinesterase inhibitors, memantine, and non-pharmacological interventions such as cognitive training and behavioral therapy.

Alzheimer's disease is a significant public health concern, affecting an estimated 5.8 million Americans in 2020. It is the sixth leading cause of death in the United States, and its prevalence is expected to continue to increase as the population ages.

There is ongoing research into the causes and potential treatments for Alzheimer's disease, including studies into the role of inflammation, oxidative stress, and the immune system. Other areas of research include the development of biomarkers for early detection and the use of advanced imaging techniques to monitor progression of the disease.

Overall, Alzheimer's disease is a complex and multifactorial disorder that poses significant challenges for individuals, families, and healthcare systems. However, with ongoing research and advances in medical technology, there is hope for improving diagnosis and treatment options in the future.

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

Types of Starvation:

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

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

Effects of Starvation on the Body:

Starvation can have severe effects on the body, including:

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

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

Examples of Urogenital Abnormalities:

1. Congenital Anomalies: Conditions that are present at birth and affect the urinary tract or genitalia, such as hypospadias (a condition where the urethra opens on the underside of the penis instead of the tip), undescended testes (testes that fail to descend into the scrotum), or interrupted or absent vas deferens (tubes that carry sperm from the epididymis to the penis).
2. Infections: Bacterial or viral infections that can cause urogenital abnormalities, such as pyelonephritis (a kidney infection) or prostatitis (an inflammation of the prostate gland).
3. Trauma: Injuries to the urinary tract or genitalia, such as those caused by sexual assault or accidents, can lead to urogenital abnormalities.
4. Neurological Conditions: Certain neurological conditions, such as spina bifida (a birth defect that affects the spine and spinal cord), can cause urogenital abnormalities.
5. Cancer: Cancer of the urinary tract or genitalia, such as bladder cancer or prostate cancer, can cause urogenital abnormalities.

Symptoms of Urogenital Abnormalities:

Depending on the specific condition, symptoms of urogenital abnormalities may include:

1. Difficulty urinating or painful urination
2. Blood in the urine or semen
3. Frequent urination or incontinence
4. Pain during sexual activity
5. Abnormalities in the shape or size of the genitalia
6. Testicular atrophy or swelling
7. Discharge from the vagina or penis
8. Foul-smelling urine

Diagnosis and Treatment of Urogenital Abnormalities:

Diagnosis of urogenital abnormalities typically involves a combination of physical examination, medical history, and diagnostic tests such as urinalysis, blood tests, and imaging studies (such as X-rays or ultrasound). Treatment depends on the specific condition causing the abnormality. Some common treatments include:

1. Medications to treat infections or inflammation
2. Surgery to repair or remove damaged tissue
3. Lifestyle changes, such as diet and exercise modifications
4. Pelvic floor exercises to strengthen the muscles that control urination and bowel movements
5. Assistive devices, such as catheters or prosthetic limbs
6. Hormone therapy to treat hormonal imbalances or gender identity issues.

The symptoms of choriocarcinoma can vary depending on the location and size of the tumor, but they may include:

* Abnormal vaginal bleeding
* Pelvic pain
* Abdominal pain
* Weakness and fatigue
* Shortness of breath
* Nausea and vomiting

If choriocarcinoma is suspected, a variety of tests may be performed to confirm the diagnosis. These may include:

* Ultrasound: This imaging test uses high-frequency sound waves to create pictures of the uterus and ovaries. It can help doctors identify any abnormal growths or tumors in the area.
* Hysteroscopy: This procedure involves inserting a thin, lighted tube through the cervix to visualize the inside of the uterus. Doctors may use hysteroscopy to collect samples of tissue for testing.
* Laparoscopy: This procedure involves making small incisions in the abdomen and using a thin, lighted tube to visualize the inside of the pelvis. Doctors may use laparoscopy to collect samples of tissue for testing or to remove any tumors that are found.
* Biopsy: In this test, doctors take a small sample of tissue from the uterus and examine it under a microscope for cancer cells.

If choriocarcinoma is confirmed, treatment may involve a combination of surgery, chemotherapy, and radiation therapy. The specific treatment plan will depend on the stage and location of the cancer, as well as the patient's overall health.

Prognosis for choriocarcinoma varies depending on the stage of the cancer when it is diagnosed. In general, the prognosis is good if the cancer is caught early and treated promptly. However, if the cancer has spread to other parts of the body (metastasized), the prognosis may be poorer.

It's important for women who have had a molar pregnancy or choriocarcinoma to follow up with their healthcare provider regularly to ensure that any remaining tissue is removed and to monitor for any signs of recurrence.

There are several types of PKU, including classic PKU, mild PKU, and hyperphenylalaninemia (HPA). Classic PKU is the most severe form of the disorder and is characterized by a complete deficiency of the enzyme phenylalanine hydroxylase (PAH), which is necessary for the breakdown of Phe. Mild PKU is characterized by a partial deficiency of PAH, while HPA is caused by a variety of other genetic defects that affect the breakdown of Phe.

Symptoms of PKU can vary depending on the severity of the disorder, but may include developmental delays, intellectual disability, seizures, and behavioral problems. If left untreated, PKU can lead to serious health complications such as brain damage, seizures, and even death.

The primary treatment for PKU is a strict diet that limits the intake of Phe. This typically involves avoiding foods that are high in Phe, such as meat, fish, eggs, and dairy products, and consuming specialized medical foods that are low in Phe. In some cases, medication may also be prescribed to help manage symptoms.

PKU is an autosomal recessive disorder, which means that it is inherited in an unusual way. Both parents must carry the genetic mutation that causes PKU, and each child has a 25% chance of inheriting the disorder. PKU can be diagnosed through newborn screening, which is typically performed soon after birth. Early diagnosis and treatment can help prevent or minimize the symptoms of PKU and improve quality of life for individuals with the disorder.

There are two main types of hemolysis:

1. Intravascular hemolysis: This type occurs within the blood vessels and is caused by factors such as mechanical injury, oxidative stress, and certain infections.
2. Extravascular hemolysis: This type occurs outside the blood vessels and is caused by factors such as bone marrow disorders, splenic rupture, and certain medications.

Hemolytic anemia is a condition that occurs when there is excessive hemolysis of RBCs, leading to a decrease in the number of healthy red blood cells in the body. This can cause symptoms such as fatigue, weakness, pale skin, and shortness of breath.

Some common causes of hemolysis include:

1. Genetic disorders such as sickle cell anemia and thalassemia.
2. Autoimmune disorders such as autoimmune hemolytic anemia (AIHA).
3. Infections such as malaria, babesiosis, and toxoplasmosis.
4. Medications such as antibiotics, nonsteroidal anti-inflammatory drugs (NSAIDs), and blood thinners.
5. Bone marrow disorders such as aplastic anemia and myelofibrosis.
6. Splenic rupture or surgical removal of the spleen.
7. Mechanical injury to the blood vessels.

Diagnosis of hemolysis is based on a combination of physical examination, medical history, and laboratory tests such as complete blood count (CBC), blood smear examination, and direct Coombs test. Treatment depends on the underlying cause and may include supportive care, blood transfusions, and medications to suppress the immune system or prevent infection.

Blepharophimosis can be associated with other conditions such as ptosis (drooping eyelid), amblyopia (lazy eye), or astigmatism. Treatment options for blepharophimosis depend on the underlying cause and may include surgery, glasses or contact lenses, or prism lenses to correct vision problems.

Surgical correction of blepharophimosis typically involves removing any excess skin or tissue that is causing the narrowing of the pretarsal fold. This can be done through an incision made on the upper eyelid or through a smaller incision using a laser. In some cases, the condition may be treated with injectable fillers to enhance the appearance of the pretarsal fold.

It's important to note that blepharophimosis is not a common condition and is often associated with other eye problems. If you suspect you or your child may have this condition, it's important to consult an ophthalmologist for proper diagnosis and treatment.

Also known as: aminoacyl-tRNA synthetase deficiency, aminoacyl-tRNA synthetase/tRNA synthetase deficiency, and amino acid transporter defects.

There are several types of melanoma, including:

1. Superficial spreading melanoma: This is the most common type of melanoma, accounting for about 70% of cases. It usually appears as a flat or slightly raised discolored patch on the skin.
2. Nodular melanoma: This type of melanoma is more aggressive and accounts for about 15% of cases. It typically appears as a raised bump on the skin, often with a darker color.
3. Acral lentiginous melanoma: This type of melanoma affects the palms of the hands, soles of the feet, or nail beds and accounts for about 5% of cases.
4. Lentigo maligna melanoma: This type of melanoma usually affects the face and is more common in older adults.

The risk factors for developing melanoma include:

1. Ultraviolet (UV) radiation exposure from the sun or tanning beds
2. Fair skin, light hair, and light eyes
3. A history of sunburns
4. Weakened immune system
5. Family history of melanoma

The symptoms of melanoma can vary depending on the type and location of the cancer. Common symptoms include:

1. Changes in the size, shape, or color of a mole
2. A new mole or growth on the skin
3. A spot or sore that bleeds or crusts over
4. Itching or pain on the skin
5. Redness or swelling around a mole

If melanoma is suspected, a biopsy will be performed to confirm the diagnosis. Treatment options for melanoma depend on the stage and location of the cancer and may include surgery, chemotherapy, radiation therapy, or a combination of these. Early detection and treatment are key to successful outcomes in melanoma cases.

In conclusion, melanoma is a type of skin cancer that can be deadly if not detected early. It is important to practice sun safety, perform regular self-exams, and seek medical attention if any suspicious changes are noticed on the skin. By being aware of the risk factors, symptoms, and treatment options for melanoma, individuals can take steps to protect themselves from this potentially deadly disease.

There are different types of Breast Neoplasms such as:

1. Fibroadenomas: These are benign tumors that are made up of glandular and fibrous tissues. They are usually small and round, with a smooth surface, and can be moved easily under the skin.

2. Cysts: These are fluid-filled sacs that can develop in both breast tissue and milk ducts. They are usually benign and can disappear on their own or be drained surgically.

3. Ductal Carcinoma In Situ (DCIS): This is a precancerous condition where abnormal cells grow inside the milk ducts. If left untreated, it can progress to invasive breast cancer.

4. Invasive Ductal Carcinoma (IDC): This is the most common type of breast cancer and starts in the milk ducts but grows out of them and invades surrounding tissue.

5. Invasive Lobular Carcinoma (ILC): It originates in the milk-producing glands (lobules) and grows out of them, invading nearby tissue.

Breast Neoplasms can cause various symptoms such as a lump or thickening in the breast or underarm area, skin changes like redness or dimpling, change in size or shape of one or both breasts, discharge from the nipple, and changes in the texture or color of the skin.

Treatment options for Breast Neoplasms may include surgery such as lumpectomy, mastectomy, or breast-conserving surgery, radiation therapy which uses high-energy beams to kill cancer cells, chemotherapy using drugs to kill cancer cells, targeted therapy which uses drugs or other substances to identify and attack cancer cells while minimizing harm to normal cells, hormone therapy, immunotherapy, and clinical trials.

It is important to note that not all Breast Neoplasms are cancerous; some are benign (non-cancerous) tumors that do not spread or grow.

There are several factors that can contribute to protein deficiency, including:

1. Poor diet: A diet that is lacking in protein-rich foods, such as meat, poultry, fish, eggs, dairy products, legumes, and nuts, can lead to protein deficiency.
2. Vegetarian or vegan diet: People who follow a vegetarian or vegan diet may be at risk of protein deficiency if they do not consume enough protein-rich plant-based foods.
3. Malabsorption: Certain medical conditions, such as celiac disease, can lead to malabsorption of proteins and other nutrients.
4. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher protein requirement to support the growth and development of their baby.
5. Chronic diseases: Certain chronic diseases, such as kidney disease, can lead to protein deficiency.

Protein deficiency can cause a range of symptoms, including:

1. Fatigue and weakness
2. Muscle wasting and loss of muscle mass
3. Poor wound healing
4. Hair loss
5. Difficulty concentrating and making decisions
6. Mood changes, such as irritability and depression
7. Increased risk of infections

If protein deficiency is not treated, it can lead to a range of complications, including:

1. Stunted growth in children
2. Weakened immune system
3. Poor wound healing
4. Increased risk of infections
5. Nutrient deficiencies
6. Reproductive problems
7. Cardiovascular disease

Treatment for protein deficiency typically involves increasing the intake of protein-rich foods or supplements. The goal is to provide enough protein to support growth and development, as well as overall health and well-being. In some cases, medication may be prescribed to help manage symptoms or address underlying conditions.

In addition to dietary changes, other treatments for protein deficiency may include:

1. Nutritional supplements: Protein supplements can be taken to increase protein intake.
2. Vitamin and mineral supplements: If the protein deficiency is due to a lack of certain vitamins or minerals, supplements may be prescribed.
3. Hormone replacement therapy: In cases where protein deficiency is caused by hormonal imbalances, hormone replacement therapy may be recommended.
4. Medications: Certain medications, such as antidepressants or anti-anxiety drugs, may be prescribed to help manage symptoms of protein deficiency.
5. Addressing underlying conditions: If the protein deficiency is due to an underlying condition, such as kidney disease, treatment will focus on managing that condition.

Preventing protein deficiency is important for maintaining overall health and well-being. Here are some tips for preventing protein deficiency:

1. Eat a balanced diet: Include a variety of protein-rich foods in your diet, such as lean meats, fish, eggs, dairy products, legumes, and nuts.
2. Consult with a healthcare professional: If you are vegetarian or vegan, or if you have certain medical conditions, consult with a healthcare professional to ensure you are getting enough protein.
3. Consider supplements: If you are unable to get enough protein through your diet alone, consider taking protein supplements.
4. Monitor your symptoms: Pay attention to any symptoms of protein deficiency and seek medical attention if they persist or worsen over time.

Overall, preventing protein deficiency is important for maintaining overall health and well-being. If you suspect you or someone you know may have a protein deficiency, it is important to seek medical attention as soon as possible. With proper diagnosis and treatment, protein deficiency can be effectively managed and symptoms can improve.

There are different types of amnesia, including:

1. Retrograde amnesia: loss of memory of events that occurred before the onset of amnesia.
2. Anterograde amnesia: inability to form new memories after the onset of amnesia.
3. Transient global amnesia: temporary and reversible loss of memory due to a specific cause, such as a stroke or a head injury.
4. Korsakoff's syndrome: a condition caused by alcoholism and malnutrition that affects the hippocampus and the ability to form new memories.
5. Dissociative amnesia: loss of memory due to psychological trauma or stress, often accompanied by dissociation from reality.

The symptoms of amnesia can vary depending on the underlying cause and the severity of the condition. Some common symptoms include:

1. Difficulty learning new information
2. Forgetting recent events or conversations
3. Inability to recall past events or experiences
4. Confusion and disorientation
5. Difficulty with problem-solving and decision-making

The diagnosis of amnesia is based on a combination of medical history, physical examination, and neuropsychological tests. Imaging studies such as CT or MRI scans may also be used to rule out other causes of memory loss.

Treatment for amnesia depends on the underlying cause and may include:

1. Medications to manage symptoms such as anxiety, depression, or cognitive impairment.
2. Cognitive rehabilitation therapy to improve memory and problem-solving skills.
3. Behavioral interventions to help the individual adapt to their condition.
4. In some cases, surgery may be necessary to treat the underlying cause of amnesia, such as a tumor or a blood clot.

Overall, amnesia can have a significant impact on an individual's quality of life, but with proper diagnosis and treatment, many people are able to manage their symptoms and lead fulfilling lives.

There are several types of lung neoplasms, including:

1. Adenocarcinoma: This is the most common type of lung cancer, accounting for approximately 40% of all lung cancers. It is a malignant tumor that originates in the glands of the respiratory tract and can be found in any part of the lung.
2. Squamous cell carcinoma: This type of lung cancer accounts for approximately 25% of all lung cancers and is more common in men than women. It is a malignant tumor that originates in the squamous cells lining the airways of the lungs.
3. Small cell lung cancer (SCLC): This is a highly aggressive form of lung cancer that accounts for approximately 15% of all lung cancers. It is often found in the central parts of the lungs and can spread quickly to other parts of the body.
4. Large cell carcinoma: This is a rare type of lung cancer that accounts for only about 5% of all lung cancers. It is a malignant tumor that originates in the large cells of the respiratory tract and can be found in any part of the lung.
5. Bronchioalveolar carcinoma (BAC): This is a rare type of lung cancer that originates in the cells lining the airways and alveoli of the lungs. It is more common in women than men and tends to affect older individuals.
6. Lymphangioleiomyomatosis (LAM): This is a rare, progressive, and often fatal lung disease that primarily affects women of childbearing age. It is characterized by the growth of smooth muscle-like cells in the lungs and can lead to cysts, lung collapse, and respiratory failure.
7. Hamartoma: This is a benign tumor that originates in the tissue of the lungs and is usually found in children. It is characterized by an overgrowth of normal lung tissue and can be treated with surgery.
8. Secondary lung cancer: This type of cancer occurs when cancer cells from another part of the body spread to the lungs through the bloodstream or lymphatic system. It is more common in people who have a history of smoking or exposure to other carcinogens.
9. Metastatic cancer: This type of cancer occurs when cancer cells from another part of the body spread to the lungs through the bloodstream or lymphatic system. It is more common in people who have a history of smoking or exposure to other carcinogens.
10. Mesothelioma: This is a rare and aggressive form of cancer that originates in the lining of the lungs or abdomen. It is caused by asbestos exposure and can be treated with surgery, chemotherapy, and radiation therapy.

Lung diseases can also be classified based on their cause, such as:

1. Infectious diseases: These are caused by bacteria, viruses, or other microorganisms and can include pneumonia, tuberculosis, and bronchitis.
2. Autoimmune diseases: These are caused by an overactive immune system and can include conditions such as sarcoidosis and idiopathic pulmonary fibrosis.
3. Genetic diseases: These are caused by inherited mutations in genes that affect the lungs and can include cystic fibrosis and primary ciliary dyskinesia.
4. Environmental diseases: These are caused by exposure to harmful substances such as tobacco smoke, air pollution, and asbestos.
5. Radiological diseases: These are caused by exposure to ionizing radiation and can include conditions such as radiographic breast cancer and lung cancer.
6. Vascular diseases: These are caused by problems with the blood vessels in the lungs and can include conditions such as pulmonary embolism and pulmonary hypertension.
7. Tumors: These can be benign or malignant and can include conditions such as lung metastases and lung cancer.
8. Trauma: This can include injuries to the chest or lungs caused by accidents or other forms of trauma.
9. Congenital diseases: These are present at birth and can include conditions such as bronchopulmonary foregut malformations and congenital cystic adenomatoid malformation.

Each type of lung disease has its own set of symptoms, diagnosis, and treatment options. It is important to seek medical attention if you experience any persistent or severe respiratory symptoms, as early diagnosis and treatment can improve outcomes and quality of life.

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HATs are enzymes responsible for the acetylation of amino acids. HATs acetylate by converting the lysine side group of amino ... Swank MW, Sweatt JD (May 2001). "Increased histone acetyltransferase and lysine acetyltransferase activity and biphasic ... the amino acid that is modified, and the number of methyl groups added. In the case of lysine methylation, three types of ... The acetylation reaction is most often catalyzed by enzymes that contain histone acetyltransferase (HAT) activity. ...
... peptide acetyltransferase, protein N-terminal acetyltransferase, NAT, Nalpha-acetyltransferase, amino-terminal amino acid- ... Tsunasawa S, Kamitani K, Narita K (February 1980). "Partial purification and properties of the amino-terminal amino acid- ... In enzymology, a peptide alpha-N-acetyltransferase (EC is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:peptide Nalpha-acetyltransferase. Other names in common use include beta ...
The subclasses of proteins with abundances of the amino acids aspartic acid, methionine specifically are acetylated. v t e (All ... NatB acetyltransferase is an enzyme in the Saccharomyces cerevisiae that functions to catalyze the dehydration synthesis of the ...
Transamination, or the transfer of an amine (or NH2) group from an amino acid to a keto acid by an aminotransferase (also known ... Choline acetyltransferase (also known as ChAT or CAT) is an important enzyme which produces the neurotransmitter acetylcholine ... Braunstein AE, Kritzmann MG (1937). "Formation and Breakdown of Amino-acids by Inter-molecular Transfer of the Amino Group". ... the growing amino acid chain from the tRNA molecule in the A-site of the ribosome and its subsequent addition to the amino acid ...
The amino-terminal alpha-helical domain particularly the amino acid residues His158 (histidine in position 158) and Asp143 ( ... This particular enzyme catalyses serine into cysteine which is eventually converted to the essential amino acid methionine. Of ... These transgenic plants would contain more essential sulphur amino acids meaning a healthier diet for humans and animals. ... Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This ...
Lysine is an amino acid with a positive charge when unmodified. Lysines on the amino terminal tails of histones have a tendency ... Histone Acetyltransferases, also known as HATs, are a family of enzymes that acetylate the histone tails of the nucleosome. ... The mechanism for acetylation and deacetylation takes place on the NH3+ groups of lysine amino acid residues. These residues ... Chemical modifications of histone proteins often occur on particular amino acids. This specific addition of single or multiple ...
This protein in 611 amino acids in length and has a molecular weight of 71.1 kilodaltons and an isoelectric point of pI=6.7. ... It also contains a possible substrate of N-acetyltransferase A at Ser2. CCDC37 has a predicted nuclear localization via ... CCDC37 contains a DUF4200 region located from amino acid 151 to 269. There is no known frunction for DUF4200. CCDC37 also ... It contains four possible PEST sequence at amino acids 17-36, 293-304, 337-360, and 360-395. ...
... of amino acids and these enzymes would have been prevalent during the periods on prehistoric earth dominated by rich amino acid ... The E2 subunit, or dihydrolipoyl acetyltransferase, for both prokaryotes and eukaryotes, is generally composed of three domains ... The N-terminal domain (the lipoyl domain), consists of 1-3 lipoyl groups of approximately 80 amino acids each. The peripheral ... polar amino acid residues (Asp, Asn, and Tyr) located on the alpha chain, and the thiamine diphosphate (TPP) cofactor directly ...
The protein encoded on FAM135 is 1406 amino acids long. The protein contains a region called DUF676, believed to be a putative ... FAM135B has shown to interact with KAT5, a gene that encodes for a histone acetyltransferase through yeast two-hybrid ...
This occurs despite the fact that only 4% of the amino acids that comprise those peptide backbones corresponds to one another. ... Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) (EC is an enzyme that encoded by ... with the δ1 ring nitrogen hydrogen bonded to the carbonyl oxygen on the amino acid backbone. Due to the fact that CRAT binds ... "Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport". Cell. ...
... is a lightweight structural protein made of 126 amino acids. Many of these amino acids have a positive charge at ... Acetylation relies on specific histone acetyltransferases that work at gene promoters during transcriptional activation. Adding ... All variants of histone H2B contain the same number of amino acids, and the variations in sequence are few in number. Only two ... Histone H2B's amino acid sequence is highly evolutionarily conserved. Even distantly related species have extremely similar ...
... may refer to: Amino-acid N-acetyltransferase Glutamate N-acetyltransferase This disambiguation page ...
Arylkylamine N-acetyltransferase is a monomeric polypeptide with a length of 207 amino acid residues, and with a molecular ... Molecular modeling and structure-activity relationship studies made it possible to pinpoint the amino acid residue of the ... Peptide combinatorial libraries of tri-, tetra-, and pentapeptides with various amino acid compositions were screened as ... The N-acetyltransferase reaction has been suggested to be the rate-determining step, and thus Serotonin N-acetyltransferase has ...
The protein ATF-2 has 505 amino acids. Studies in mice indicate a role for ATF-2 in the development of nervous system and the ... The protein is also a histone acetyltransferase (HAT) that specifically acetylates histones H2B and H4 in vitro; thus, it may ... Nucleic Acids Res. 26 (16): 3854-61. doi:10.1093/nar/26.16.3854. PMC 147779. PMID 9685505. Sano Y, Tokitou F, Dai P, Maekawa T ... "Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid ...
Each of these different enzyme complexes is specific for different amino acids or amino acid sequences which is shown in the ... A tubulin acetyltransferase is located in the axoneme, and acetylates the α-tubulin subunit in an assembled microtubule. Once ... to the α-amino group of the first amino acid residue of the protein. Different NATs are responsible for the acetylation of ... These amino acids are more frequently expressed in the N-terminal of proteins in eukaryotes, so NatA is the major NAT ...
Proteinogenic amino acids, Glucogenic amino acids, Ketogenic amino acids, Aromatic amino acids, Essential amino acids, ... Melatonin (a neurohormone) is in turn synthesized from serotonin, via N-acetyltransferase and 5-hydroxyindole-O- ... Ikeda M (2002). "Amino acid production processes". Microbial Production of l-Amino Acids. Advances in Biochemical Engineering/ ... is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid ...
... glutamine in the liver involves amino acid acetylation carried out by the enzyme phenylacetyltranferase or glutamine N-acetyl transferase ... circulated and retained in the blood after microbial fermentation of certain proteins and amino acids in the gut. Blood serum ... non-invasive biomarker for gluconeogenesis and citric acid cycle intermediates in the liver. High levels of ... of the substrates phenylacetyl-CoA and L-glutamine to produce CoA and alpha-N-phenylacetyl-L-glutamine and phenylacetic acid. ...
An example of the first mechanism occurs during the acetylation of lysine terminal tail amino acids, which is catalyzed by ... histone acetyltransferases (HATs). HATs are part of a multiprotein complex that is recruited to chromatin when activators bind ... phosphorylation and ubiquitination can be associated with different transcriptional states depending on the specific amino acid ... MNase-seq and DNase-seq both follow the same principles, as they employ lytic enzymes that target nucleic acids to cut the DNA ...
Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring ... Some HAT transcriptional co-activators contain a bromodomain, a 110-amino acid module that recognizes acetylated lysine ... Moreover, a general acid or base have not yet been identified for this HAT. The structures of several HAT domains bound to ... The basic mechanism catalyzed by HATs involves the transfer of an acetyl group from acetyl-CoA to the ε-amino group of a target ...
... may refer to: Amino-acid N-acetyltransferase Glutamate N-acetyltransferase Urea cycle This set ...
... may refer to: Amino-acid N-acetyltransferase Glutamate N-acetyltransferase This set index page ...
These amino acids are positioned on opposite side of the endoplasmic reticulum membrane. His338 resides in the lumen and is ... The topology models of ghrelin O-acyltransferase are similar to those of acetyl-coenzyme A acetyltransferase 1 and glycerol ... The most common is the use of an amino acid and radioactive isotope tags to monitor the formation of reaction products. Also ... Other approaches in the category include altering functional group or amino acid stereochemistry to greatly decrease enzyme ...
The functional CBP is approximately 7362 nucleotides long and encodes 2,441 amino acids. CBP does not directly interact with ... CBP has intrinsic acetyltransferase functions; it is able to add acetyl groups to both transcription factors as well as histone ... Both TAZ1 and TAZ2 domains favor the hydrophobic residues within amphipathic amino acid sequences, and their binding affinity ... Bromodomains (BRD) consist of approximately 110 amino acids, that function to recognize acetylated lysine molecules. They ...
It is 433 amino acids long, from amino acid 80 until amino acid number 512. DUF4641 is a part of pfam15483. The domain is ... This include sites for N-acetyltransferase (NetAcet 1-), glycation of ε amino groups of lysines (NetGlycate 1.0), mucin type ... The protein has 514 amino acids and a molecular mass of 54.4 kDa. The isoelectric point is 9.3. Compared to other human ... DUF4641 has an unusual spacing between lysine residues and positive charged amino acids (Analysis of Protein Sequences, SAPS ...
... amino acid homology, and are each 158 amino acids long.: 98 Glufosinate is a broad-spectrum herbicide that is used to control ... "phosphinothricin acetyltransferase" or "pat".: 98 The two genes and their proteins have 80% homology on the DNA level and 86% ... Phosphinic acids, Ammonium compounds, Amino acids, Glutamine synthetase inhibitors, Eukaryotic selection compounds). ... it consists of two alanine residues and a unique amino acid that is an analog of glutamate that they named "phosphinothricin ...
NAG can be used in the production of ornithine and arginine, two important amino acids, or as an allosteric cofactor for ... a member of the N-acetyltransferase family of enzymes, is present in both prokaryotes and eukaryotes, although its role and ... produce NAG through ornithine acetyltransferase (OAT), which is part of a 'cyclic' ornithine production pathway. NAGS is ...
In a different organism, C. albicans, a similar set of amino acids were found to be essential to the catalytic activity, ... Specifically for this N-acetyltransferase catalysts, studies with S. cerevisiae GNA enzyme have shown that some specific amino ... glucosamine-phosphate N-acetyltransferase, and glucosamine-6-phosphate N-acetyltransferase. This enzyme is part of the ... aminodeoxyglucosephosphate acetyltransferase, glucosamine 6-phosphate acetylase, glucosamine 6-phosphate N-acetyltransferase, N ...
In fatty acid (FA) metabolism, long chain fatty acids in the cytosol cannot cross the mitochondrial membrane because they are ... Meldonium has also been shown by NMR to bind to carnitine acetyltransferase. Carnitine acetyltransferase belongs to a family of ... It is a structural analogue of γ-butyrobetaine, with an amino group replacing the C-4 methylene of γ-butyrobetaine. γ- ... fatty acid transport is reduced and the accumulation of cytotoxic intermediate products of fatty acid beta-oxidation in ...
The α and β-tubulin subunits are ~50% identical at the amino acid level, and both have a molecular weight of approximately 50 ... The nature of the tubulin acetyltransferase remains controversial, but it has been found that in mammals the major ... "αTAT1 is the major α-tubulin acetyltransferase in mice". Nature Communications. 4: 1962. Bibcode:2013NatCo...4.1962K. doi: ... acetyltransferase is ATAT1. however, the reverse reaction is known to be catalyzed by HDAC6. Polyglutamylation: the addition of ...
The catalytic domain of PRMTs consists of a SAM binding domain and substrate binding domain (about 310 amino acids in total). ... Histone-Modifying Enzymes Histone acetyltransferase (HAT) Histone deacetylase (HDAC) RNA polymerase control by chromatin ... composed of approximately 130 amino acids), the pre-SET, and the post-SET domains. The pre-SET and post-SET domains flank the ... Next, a nearby tyrosine residue deprotonates the ε-amino group of the lysine residue. The lysine chain then makes a ...
... and ketogenic amino acids through a series of reactions that metabolize these compounds into acetoacetate, which is the first ... 3-Hydroxyisovaleryl CoA is likely detoxified by carnitine acetyltransferase producing 3HIA-carnitine, which is transported ... β-Hydroxybutyric acid, also known as 3-hydroxybutyric acid or BHB, is an organic compound and a beta hydroxy acid with the ... β-Hydroxybutyric acid is a chiral compound with two enantiomers: D-β-hydroxybutyric acid and L-β-hydroxybutyric acid. Its ...
When mice were created with this single, conservative amino acid substitution in TRβ, synaptic maturation and plasticity in the ... These proteins often have an intrinsic histone acetyltransferase (HAT) activity, which weakens the association of histones to ... Some of these receptors such as FXR, LXR, and PPAR bind a number of metabolic intermediates such as fatty acids, bile acids and ... Two putative orphan receptors, HNF4 and USP were found, via structural and mass spectrometry analysis, to bind fatty acids and ...
The human CASP protein is predicted to contain 678 amino acids, of which 400 are shared with CUTL1. CASP protein is ... "Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein ( ... Dintilhac A, Bernués J (2002). "HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid ... "Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein ( ...
Naltner A, Ghaffari M, Whitsett JA, Yan C (2000). "Retinoic acid stimulation of the human surfactant protein B promoter is ... "Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain ... coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase ...
In mammals, phenethylamine is produced from the amino acid L-phenylalanine by the enzyme aromatic L-amino acid decarboxylase ... "EC - aralkylamine N-acetyltransferase". BRENDA. Technische Universität Braunschweig. July 2014. Retrieved 10 November ... In a resting state, phenethylamine is synthesized in catecholamine neurons from L-phenylalanine by aromatic amino acid ... the gene for aromatic amino acid decarboxylase (AADC), the major enzyme involved in the synthesis of the trace amines, is ...
Rp9 variant is quite common in human and mouse cells, lacks 9 amino acids in the repression domain. Δ324 found at low levels in ... These both have histone acetyltransferase activity, and lead to subsequent transcription activation. In addition, structural ... This interaction has been specifically shown to rely on amino acids 544-607 on the EVI1 protein, a stretch that contains two ... The 145kDa isoform is the most-studied, encoding 1051 amino acids, although there are many EVI1 fusion products detectable in ...
PLP forms an imine with the amino acid derivative. The amine on the pyridine is protonated and acts as an electron sink, ... It has been proposed that histidine residue His122 of serotonin N-acetyl transferase is the catalytic residue that deprotonates ... "Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the ... Lerner AB, Case JD, Takahashi Y (July 1960). "Isolation of melatonin and 5-methoxyindole-3-acetic acid from bovine pineal ...
... is a chemical substance which is naturally created from the amino acid arginine. Agmatine has been shown to exert ... inducer of spermidine/spermine acetyltransferase (SSAT), and inducer of antizyme. Protein ADP-ribosylation. Inhibition of ... Amino Acids. 26 (4): 321-9. doi:10.1007/s00726-004-0078-4. PMID 15290337. S2CID 23116711. Pinthong, D.; Wright, I. K.; Hanmer, ... The term stems from A- (for amino-) + g- (from guanidine) + -ma- (from ptomaine) + -in (German)/-ine (English) suffix with ...
... has 350 amino acids and the amino acid sequence is: MCSQEGEGYSLLKEYANAFMVSQVLFAACELGVFELLAEALEPLDSAAVSSHLGSSPGD ... In 2001, it was argued that another enzyme in the pathway, N-acetyl transferase (NAT) was the limiting reagent in the ... 2006). "From genomics to chemical genomics: new developments in KEGG". Nucleic Acids Res. 34 (90001): D354-357. doi:10.1093/nar ... with 373 amino acids the sequence is: MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHG ...
... a codon for the amino acid aspartic acid GATT This disambiguation page lists articles associated with the title GAT. If an ... an enzyme Galactoside acetyltransferase, an enzyme Generic Associated Types (a feature of the Rust programming language) Gat ( ...
Piskacek, Simona; Gregor, Martin; Nemethova, Maria; Grabner, Martin; Kovarik, Pavel; Piskacek, Martin (2007). "Nine-amino-acid ... the discovery that co-activator complexes were required for transcriptional activation function as histone acetyltransferases, ... Nucleic Acids Research. 29 (15): 3131-6. doi:10.1093/nar/29.15.3131. PMC 55834. PMID 11470869. EntrezGene 5928 Xue, Yutong; ...
... sequences that encode truncated amino acid sequences. C14orf102 interacts with RNPS1, a gene encoding a protein that is known ... The protein contains five HAT (histone acetyltransferase) domains, a coiled coil domain, a domain of unknown function, a lysine ...
The effects of histone methylation are residue dependent (e.g. which amino acid on which histone tail is methylated) therefore ... Histone acetyltransferases (HATs) are enzymes responsible for the addition of acetyl groups, and histone deacetylases (HDACs) ... Valproic acid Valproic acid added to cells from SMA patients increased SMN2 mRNA and protein levels and that the drug directly ... Valpropic Acid Valpropic acid has been shown to have positive results in animal trials, in the mitigation of the disease by ...
The heme domain is composed of 70 amino acids and it appears that the heme only exists in mammalian CBS and is absent in yeast ... Isolation and molecular characterization of cystathionine beta-synthase and serine acetyltransferase from Trypanosoma". The ... The human enzyme cystathionine β-synthase is a tetramer and comprises 551 amino acids with a subunit molecular weight of 61 kDa ... Homocystinuria Cysteine Metabolism Amino acid S-Adenosyl-L-methionine Heme GRCh38: Ensembl release 89: ENSG00000160200 - ...
"Nucleotide and deduced amino acid sequence of human liver microsomal epoxide hydrolase". Nucleic Acids Res. 15 (17): 7188. doi: ... Wormhoudt LW, Commandeur JN, Vermeulen NP (1999). "Genetic polymorphisms of human N-acetyltransferase, cytochrome P450, ... genetic polymorphism and functional expression in vitro of amino acid variants". Hum. Mol. Genet. 3 (3): 421-8. doi:10.1093/hmg ... untranslated region have been identified with length of 455 amino acids. Conversion of epoxides to trans-dihydrodiols presents ...
... three amino acids of the 8-oxoguanine-binding pocket". Nucleic Acids Research. 32 (2): 570-578. doi:10.1093/nar/gkh224. PMC ... and aids in histone acetyltransferase activity. c-Myc is also known as an oncogene, and in certain conditions can become cancer ... TET3o is created by alternative promoter use and contains an additional first N-terminal exon coding for 11 amino acids. TET3o ... Nucleic Acids Research. 29 (10): 2117-2126. doi:10.1093/nar/29.10.2117. PMC 55450. PMID 11353081. Ming X, Matter B, Song M, ...
The FOXP3 gene has 12 exons and its full reading open frame encodes 431 amino-acids. FOXP3 is a member of the FKH family of ... FOXP3 forms complexes with histone deacetylase (HDAC)7, HDAC9, and the histone acetyl transferase TIP60, which alters ... transcription factors and contains a proline‐rich (PRR) amino‐terminal domain, central zinc finger (ZF) and leucine zipper (LZ ...
Human NAT1 preferentially acetylates 4-aminobenzoic acid (PABA), 4 amino salicylic acid, sulfamethoxazole, and sulfanilamide. ... Polymorphisms of NAT2 include the single amino acid substitutions R64Q, I114T, D122N, L137F, Q145P, R197Q, and G286E. These are ... The following is a list of human genes that encode N-acetyltransferase enzymes: Evans DA (1989). "N-acetyltransferase". ... of their amino acid sequence. Both also have an active site cysteine residue (Cys68) in the N-terminal region. Further, all ...
The opines are amino acid derivatives used by the bacterium as a source of carbon and energy. This natural process of ... and phosphinothricin acetyltransferase (which acetylates and deactivates phosphinothricin, a potent inhibitor of glutamine ... Ben-Amar A, Daldoul S, Reustle GM, Krczal G, Mliki A (December 2016). "Reverse Genetics and High Throughput Sequencing ...
... s synthesize the hormone melatonin by first converting the amino acid tryptophan to serotonin. The serotonin is then ... arylalkylamine N-acetyltransferase). The expression of the AANAT gene is controlled by the transcription factor pCREB, and this ...
Since the genes for these receptors are highly edited, i.e. altered to encode proteins with different amino acid sequences, and ... Japanese individuals bearing slow acetylating variants of the N-acetyltransferase 2 gene, (NAT2), viz., NAT2*6A and NAT2*7B, ... different amino acid sequences) T-cell receptors while an individual express only a fraction of these, a drug's or its ... inhibits uric acid production; treatment for gout), mexiletine (treatment for heart arrhythmias), omeprazole (treatment for ...
... selective amino acid sequence conservation of a nuclear hormone receptor in mammals". Human Genetics. 90 (5): 505-10. doi: ... "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and ... Xu XC, Sozzi G, Lee JS, Lee JJ, Pastorino U, Pilotti S, Kurie JM, Hong WK, Lotan R (May 1997). "Suppression of retinoic acid ... Kooistra T, Lansink M, Arts J, Sitter T, Toet K (Sep 1995). "Involvement of retinoic acid receptor alpha in the stimulation of ...
AADC, aromatic-l-amino-acid decarboxylase; AANAT, arylalkylamine N-acetyltransferase; ASMT, N-acetylserotonin methyltransferase ... AADC, aromatic-l-amino-acid decarboxylase; AANAT, arylalkylamine N-acetyltransferase; ASMT, N-acetylserotonin methyltransferase ... the exogenous amino acid tryptophan through the action of tryptophan hydroxylase (TP5H) and aromatic acid decarboxylase (AADC) ... This amino acid is a factor determining a proteins quaternary structure, and is very useful during collagen synthesis and its ...
... by L-aromatic amino acid decarboxylase (AADC). Serotonin is N-acetylated by arylalkylamine N-acetyltransferase (AA-NAT, also ... L-aromatic amino acid decarboxylase; AA-NAT, arylalkylamine N-acetyltransferase; HIOMT, hydroxyindole-O-methyltransferase). ... Melatonin, hormone of darkness, is synthesized from tryptophan, which is an essential amino acid by the pineal gland. The ... Bozkır A, Şimşek B, Güngör A, Torun M. Ascorbic acid and uric acid levels in lung cancer patients. Journal of Clinical Pharmacy ...
The derived amino acid sequences from csiA, B, and E/cskA, B, and E shared ,70% sequence identity with capsule biosynthesis ... The O-acetyltransferases should be termed cssE for serogroup C and cssF for serogroups W and Y; the nomenclature for ctrG, ... The deduced amino acid sequence from cseE shared 83% sequence identity with a 3-deoxy-8-phosphooctulonate synthase belonging to ... The capsule polymerases belonging to serogroups W and Y (csw and csy) are closely related; a single amino acid substitution in ...
Watanabe, M.; Hubberten, H. M.; Saito, K.; Hoefgen, R.: Serine Acetyltransferase. In: Amino Acids in higher plants, S. 195 - ... Watanabe, M.; Hoefgen, R.: Expression Profile of the Serine Acetyltransferase (SERAT) and O-Acetylserine (thiol)lyase (OASTL) ...
glutamate N-acetyltransferase/amino-acid acetyltransferase. codon_start. 1. EC_number. db_xref. GI:87201518. transl_ ... Amino Acids and Derivatives,Arginine. urea cycle, polyamines,Arginine Biosynthesis extended,Glutamate N-acetyltransferase (EC ... Amino Acids and Derivatives,Proline and 4-hydroxyproline,Evolution of Proline Biosynthesis (for review by Fichman et al),N- ... Amino Acids and Derivatives,Arginine. urea cycle, polyamines,Arginine Biosynthesis extended,N-acetylglutamate synthase (EC 2.3. ...
... we identified the N-terminal amino group of the agmatinamic acid as the N-acetylation site. These findings highlight the ... The authors show that the N-acetyltransferase PamZ acts as a self-resistance factor disabling the antibacterial paenilamicin ... Its biosynthetic gene cluster contains a gene coding for the N-acetyltransferase PamZ. We show that PamZ acts as self- ... It contains unusual structural motifs such as galantinamic acid (Glm), agmatinamic acid (Aga), N-methyldiaminopropionic acid ( ...
The process of citrullination modifies an arginine (R) present in the amino acid sequence of a protein into citrulline, whereas ... Acetylation is catalyzed by acetyl transferases. Ac-CoA: acetyl-CoA; H2O2: hydrogen peroxide; MPO: myeloperoxidase [6-8]. ... Presence of these modified sequences of amino acids may provoke specific autoantibody production in RA. Antibodies in the serum ... These alleles code for proteins that contain similar amino acid sequences (QKRAA, QRRAA, or RRRAA), also known as "shared ...
TOGETHER with a seriously excessive amount of glutamic acid (and other amino acids) to the effects of the acetyltransferase. ... It described how phosphinothricin-acetyltransferase also has glutamic acid as a substrate, by mixing the two substances and ... Schulz had been unable to demonstrate ANY reaction product with glutamic acid and thus concluded that glutamic acid was not a ... the acetyltransferase would acetylate the glufosinate using not only the added acetyl source but also acetylated glutamine acid ...
... which changes the encoded amino acid from Asn99 in the rapid acetylator strain to Ile99 in the slow acetylator strain. In this ... Recently, two N-acetyltransferase genes, Nat-1 and Nat-2, were cloned from rapid (C57BL/6J) and slow (A/J) acetylator mouse ... Mice have a similar genetic polymorphism in N-acetyltransferase activity and have been used as models of the human polymorphism ... Cloned mouse N-acetyltransferases: enzymatic properties of expressed Nat-1 and Nat-2 gene products. ...
Amino-acid N-acetyltransferase Synonymes. Amino acid acetyltransferase Amino-acid acetyltransferase N-Acétyl-L-glutamate ... Amino acid acetyltransferase. Amino-acid acetyltransferase. N-Acétyl-L-glutamate synthétase. N-Acétylglutamate synthase. N- ... Amino-acid N-acetyltransferase - Concept préféré Concept UI. M0070469. Terme préféré. ... do not confuse with N-TERMINAL ACETYLTRANSFERASES. Qualificatifs autorisés:. AD administration et posologie. AE effets ...
Amino-Acid N-Acetyltransferase (10) * Ornithine Carbamoyltransferase Deficiency Disease (9) * Xanthomonas campestris (7) ... The functional impact of 1,570 individual amino acid substitutions in human OTC. Lo, Russell S; Cromie, Gareth A; Tang, ...
Specifically, it helps process isoleucine, an amino acid that is a building block of many proteins. This enzyme is also ... acetyl-Coenzyme A acetyltransferase 1. *acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase) ... As a result, chemical byproducts called organic acids can build up to toxic levels in the blood. These substances may cause the ...
Product: chloramphenicol acetyltransferase. confers resistance to chloramphenicol. CmR. 5253 .. 5912 = 660 bp. 219 amino acids ... 286 amino acids = 31.6 kDa. 2 segments. Segment 1: signal sequence 1374 .. 1442 = 69 bp. 23 amino acids = 2.6 kDa. ... 286 amino acids = 31.6 kDa. 2 segments. Segment 2: 582 .. 1373 = 792 bp. 263 amino acids = 28.9 kDa. ...
Amino-Acid N-Acetyltransferase. K. M. Kapheim, Pan, H., Li, C., Salzberg, S. L., Puiu, D., Magoc, T., Robertson, H. M., Hudson ...
D-amino-acid N-acetyltransferase activity. GO:0047835. D-tryptophan N-acetyltransferase activity. ... N-acetyltransferase activity. id: GO:0008080. name: N-acetyltransferase activity. namespace: molecular_function. type: go. ...
Unnatural amino acid for inducing red shift in fluorescent proteins and fluorescent protein-based biosensors. ... Lysine acetyltransferase HBO1 (KAT7) inhibitor. 7368. Cell Counting Kit-8 New. Cell viability and proliferation assay test ...
It is the name of an extract of the cactus known as the nopal. It is loaded with essential amino acids which can lower fluid ... Carnitine Acetyltransferase (CTA) is a cellular organelle in your body that needs carnitine. The machine moves free fatty acids ... Incorporating this amino acid into the form of a supplement to your diet can help reduce fatigue and provide energy to ... L-carnitine fumarate is a naturally occurring amino acid that you discover in green vegetables, nuts and red meat. Like other ...
The NAT hNaa50p preferentially modifies peptides starting with methionine followed by a hydrophobic amino acid. hNaa50p also ... Acetyltransferases. Catalysis. Humans. Hydrophobic and Hydrophilic Interactions. Kinetics. Methionine. *Models, Chemical. ... N-Terminal Acetyltransferase E. Nuclear Magnetic Resonance, Biomolecular. Peptides. Protein Conformation. Biochemistry. Enzymes ... N(alpha)-acetylation is a common protein modification catalyzed by different N-terminal acetyltransferases (NATs). Their ...
N-Acetyltransferase, Acetyl-CoA Arylamine use Arylamine N-Acetyltransferase N-Acetyltransferase, Amino-Acid use Amino-Acid N- ... Na+ Independent Neutral Amino Acid Transporter use Amino Acid Transport Systems, Neutral ... Na+-Independent Neutral Amino Acid Transporter use Amino Acid Transport Systems, Neutral ... N Acetyl L Glutamate Synthetase use Amino-Acid N-Acetyltransferase N Acetyl Muramyl L Alanyl D Glutamic alpha Amide use ...
Glufosinate chemically resembles the amino acid glutamate and acts to inhibit an enzyme, called glutamine synthetase, which is ... Phosphinothricin N-acetyltransferase gene , Streptomyces hygroscopicus (STRHY). Protein coding sequence , Resistance to ... In addition to fertility restoration, the canola expresses Streptomyces hygroscopicus phosphinothricin N-acetyltransferase to ... Further, the expression of phosphinothricin N-acetyltransferase also allowed for selection of modified plants during ...
N-acetyltransferase activity. IEP. Enrichment. BP. GO:0009063. cellular amino acid catabolic process. IEP. Enrichment. ... serine family amino acid metabolic process. IEP. Enrichment. BP. GO:0009071. serine family amino acid catabolic process. IEP. ... carboxylic acid catabolic process. IEP. Enrichment. MF. GO:0051002. ligase activity, forming nitrogen-metal bonds. IEP. ... alpha-amino acid metabolic process. IEP. Enrichment. BP. GO:1901606. alpha-amino acid catabolic process. IEP. Enrichment. ...
... amino acid and derivative metabolic process;0.0171598415794417!GO:0000123;histone acetyltransferase complex;0.0172978092932297! ... acid-amino acid ligase activity;4.27841701028717e-09!GO:0008219;cell death;5.47883239669253e-09!GO:0016265;death; ... amino acid activation;2.29621912647451e-07!GO:0006418;tRNA aminoacylation for protein translation;2.29621912647451e-07!GO: ... protein amino acid lipidation;0.0120257456647832!GO:0008361;regulation of cell size;0.0120799393080815!GO:0051098;regulation of ...
serine O-acetyltransferase activity. IEP. Enrichment. BP. GO:0009070. serine family amino acid biosynthetic process. IEP. ... putative acetyltransferase [Ensembl]. Acetyltransferase.... 0.05. OrthoFinder. AGT26674. N559_5098. putative acetyltransferase ... racemase activity, acting on amino acids and derivatives. IEP. Enrichment. BP. GO:0044249. cellular biosynthetic process. IEP. ... racemase and epimerase activity, acting on amino acids and derivatives. IEP. Enrichment. ...
This structure reveals that WcbI incorporates a previously described 100-amino-acid subdomain into a novel, principally helical ... Structural analysis and biophysical assays suggest that WcbI functions as an acetyltransferase enzyme, whilst biochemical tests ... 310 amino acids). This fold adopts a cradle-like structure, with a deep binding pocket for CoA in the loop-rich cradle. ...
Protein phosphorylation, the addition of a phosphate group to a side chain of an amino acid3 , is an important regulatory ... Histone Acetyl Transferases (HATs) and Histone Deacetylases (HDACs). With few exceptions, such as red blood cells, all of our ... The drug specifically interacts with a key amino acid (a threonine) within the active site (catalytic site) of the proteasome. ... The proteins are then digested into peptides 6 to 9 amino acids in length and released. The peptides can then be recycled. ...
Histone H3 (5-23), derived from histone H3 5-23 amino acids, can be used as a substrate for histone acetyltransferase (HAT) ... Anacardic Acid Hydroginkgolic acid; Ginkgolic Acid C15:0. Histone Acetyltransferase Epigenetic Reader Domain Bacterial ... Histone Acetyltransferase Cancer NiCur is a potent and selective CBP histone acetyltransferase (HAT) inhibitor with an IC50 ... Histone Acetyltransferase Cancer NSC 694623 is a potent histone acetyltransferase (HAT) inhibitor with an IC50 value of 15.9 μM ...
NAT8 Variants, N-Acetylated Amino Acids, and Progression of CKD. Clinical journal of the American Society of Nephrology : CJASN ... N-acetyltransferase 8, a positional candidate for blood pressure and renal regulation: resequencing, association and in silico ...
BCAT2 Branched-chain-amino-acid aminotransferase, mitochondrial O15382 15 47.4 IPO8 Importin-8 O15397 4 4.4 ... mitochondrial O76031 14 27 DLAT Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, ... and fatty acid synthase (FASN) that are involved in the de novo synthesis of fatty acids, CD36, Caveolin (CAV1), and monoacyl ... Figures 7C,D). To note that the synthesis of fatty acids from [U-14C]glucose was reduced in shβcat with respect to shCTR ( ...
Amino Acids, 42:887-898, 2012.. *. Goodwin, A.C., Wu, S., Huso, D.L., Wu, X., Destefano Shields, C.E., Hacker-Prietz, A., ... The catabolism of the polyamines is controlled by the rate limiting enzyme spermidine/spermine N1-acetyltransferase (SSAT) that ...
  • 16 this range (primarily cytochrome P-450 mediated oxidation to fatty acids and alcohols) is slow, while the aromatics are metabolized faster (oxidation of alkyl site and/or ring, sometimes with formation of reactive intermediates, and conjugation with glutathione, glucuronic acid, or glycine) (ATSDR 1999). (cdc.gov)
  • Expression Profile of the Serine Acetyltransferase (SERAT) and O-Acetylserine (thiol)lyase (OASTL) Gene Families in Arabidopsis. (mpg.de)
  • This protein contains the apparently unique amino acid hypusine that is formed by the post-translational modification of a lysine residue catalyzed by deoxyhypusine synthase and deoxyhypusine hydroxylase (DOHH). (biomedcentral.com)
  • 2) The contents of threonine, valerine, leucine, lysine, histidine, essential amino acids, flavor amino acids, aspartic acid, serine, glutamic acid and arginine of the longissimus dorsi muscle in RL2 and RL3 groups were significantly higher than RL1 and RL4 (p (bvsalud.org)
  • GNAT family putative N-acetyltransferase [Ensembl]. (ntu.edu.sg)
  • Acetyltransferase (GNAT) family, Putative thioesterase (yiiD_Cterm) [Interproscan]. (ntu.edu.sg)
  • putative acetyltransferase [Ensembl]. (ntu.edu.sg)
  • Specifically, it helps process isoleucine, an amino acid that is a building block of many proteins. (medlineplus.gov)
  • Its biosynthetic gene cluster contains a gene coding for the N -acetyltransferase PamZ. (nature.com)
  • Cloned mouse N-acetyltransferases: enzymatic properties of expressed Nat-1 and Nat-2 gene products. (cdc.gov)
  • CPI-1612 is a highly potent, orally active EP300/CBP histone acetyltransferase (HAT) inhibitor with an IC 50 of 8.1 nM for EP300 HAT . (medchemexpress.com)
  • CPTH2 hydrochloride is a potent histone acetyltransferase (HAT) inhibitor. (medchemexpress.com)
  • CPTH2 is a potent histone acetyltransferase (HAT) inhibitor. (medchemexpress.com)
  • CPTH2 hydrochloride induces apoptosis and decreases the invasiveness of a clear cell renal carcinoma (ccRCC) cell line through the inhibition of acetyltransferase p300 (KAT3B) . (medchemexpress.com)
  • 1997. Inhibition of L-aromatic amino acid decarboxylase by polychlorinated biphenyls. (cdc.gov)
  • Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study. (umassmed.edu)
  • N(alpha)-acetylation is a common protein modification catalyzed by different N-terminal acetyltransferases (NATs). (umassmed.edu)
  • eIF5A is the only protein known to contain the amino acid hypusine. (biomedcentral.com)
  • Mice have a similar genetic polymorphism in N-acetyltransferase activity and have been used as models of the human polymorphism in many studies of the toxicology and carcinogenicity of arylamines. (cdc.gov)
  • Recently, two N-acetyltransferase genes, Nat-1 and Nat-2, were cloned from rapid (C57BL/6J) and slow (A/J) acetylator mouse strains. (cdc.gov)
  • In this report, the N-acetylation polymorphism in mice was investigated by transiently expressing the cloned N-acetyltransferase genes in COS-1 cells. (cdc.gov)
  • Kinetic constants determined for the expressed enzymes with 2-aminofluorene and p-aminobenzoic acid indicated that Km values were not significantly different between the enzymes, although the Vmax value of NAT-2(99asn) was consistently 2-3-fold higher than that of NAT-1 or NAT-2(99ile). (cdc.gov)
  • Using tandem mass spectrometry, nuclear magnetic resonance spectroscopy and synthetic diastereomers, we identified the N-terminal amino group of the agmatinamic acid as the N -acetylation site. (nature.com)
  • N -acetylation fol owed by N -hydroxyl- lysed hydrolysis to release the was a C8-substituted deoxyguano- ation of the remaining amino function N -hydroxyarylamines, which can sine adduct. (who.int)
  • N-acetyltransferase 8, a positional candidate for blood pressure and renal regulation: resequencing, association and in silico study. (cdc.gov)
  • Further, the expression of phosphinothricin N-acetyltransferase also allowed for selection of modified plants during transformation. (cbd.int)
  • As a result, chemical byproducts called organic acids can build up to toxic levels in the blood. (medlineplus.gov)
  • 1989. Cellular alterations and enhanced induction of cleft palate after coadministration of retinoic acid and TCDD. (cdc.gov)
  • Humans have genetically determined differences in their N-acetyltransferase activities and are phenotypically classified as rapid or slow acetylators. (cdc.gov)
  • The genomic clone encoding NAT-1 is identical in rapid and slow acetylator mouse strains, whereas the clone encoding NAT-2 differs between rapid and slow strains by a single base pair, which changes the encoded amino acid from Asn99 in the rapid acetylator strain to Ile99 in the slow acetylator strain. (cdc.gov)
  • Arylamine N-acetyltransferases (NATs) play an important role in the metabolism of arylamine and hydrazine drugs and many arylamine procarcinogens. (nih.gov)
  • Human arylamine N -acetyltransferases (NATs) are xenobiotic-metabolizing enzymes that play a key role in the biotransformation of AA carcinogens. (nih.gov)
  • In addition, four polymorphisms result in amino acid changes that do not affect activity of the enzyme. (nih.gov)
  • Treatment of bile acid synthesis disorders due to single enzyme defects (SEDs). (nih.gov)
  • A third portion is acetylated to N-acetyl- serotonin by the enzyme serotonin N- acetyltransferase (14). (nih.gov)
  • Large changes in the activity of serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AANAT) in the pineal gland control the rhythmic production of the time-keeping hormone melatonin. (nih.gov)
  • The_ latter amino acid is then decarboxylated by l-aromatic amino acid decarboxylase to form the biogenic amine serotonin. (nih.gov)
  • Computational and experimental analyses of mammalian arylamine N-acetyltransferase structure and function. (nih.gov)
  • The safety and effectiveness of CHOLBAM on extrahepatic manifestations of bile acid synthesis disorders due to SEDs or PDs including Zellweger spectrum disorders have not been established. (nih.gov)
  • isoniazid was a preferred substrate for NAT-1, whereas p-aminobenzoic acid was preferred for NAT-2(99asn) and NAT-2(99ile). (cdc.gov)
  • Specifically, it helps process isoleucine, an amino acid that is a building block of many proteins. (medlineplus.gov)
  • Proteins that may have acetyltransferase activity, but lack experimental evidence for intrinsic activity are listed as putative lysine acetyltransferases. (nih.gov)
  • The two human N-acetyltransferases, NAT1 and NAT2, are widely distributed in human tissues and are highly polymorphic. (nih.gov)
  • 5. Induction of spermidine/spermine N1-acetyltransferase in breast cancer tissues treated with the polyamine analogue N1, N11-diethylnorspermine. (nih.gov)
  • Mice have a similar genetic polymorphism in N-acetyltransferase activity and have been used as models of the human polymorphism in many studies of the toxicology and carcinogenicity of arylamines. (cdc.gov)
  • Shows only trace activity toward L-His and no N-acetyltransferase activity toward other amino acids. (nih.gov)
  • 7. Transgenic mice with activated polyamine catabolism due to overexpression of spermidine/spermine N1-acetyltransferase show enhanced sensitivity to the polyamine analog, N1, N11-diethylnorspermine. (nih.gov)
  • 3. Combination effects of platinum drugs and N1, N11 diethylnorspermine on spermidine/spermine N1-acetyltransferase, polyamines and growth inhibition in A2780 human ovarian carcinoma cells and their oxaliplatin and cisplatin-resistant variants. (nih.gov)
  • Humans have genetically determined differences in their N-acetyltransferase activities and are phenotypically classified as rapid or slow acetylators. (cdc.gov)
  • the balance between acetyltransferase and deacetylase activities. (nih.gov)
  • 10. The role of spermidine/spermine N1-acetyltransferase in determining response to chemotherapeutic agents in colorectal cancer cells. (nih.gov)
  • As a result, chemical byproducts called organic acids can build up to toxic levels in the blood. (medlineplus.gov)
  • 2. Polyamine catabolism in platinum drug action: Interactions between oxaliplatin and the polyamine analogue N1,N11-diethylnorspermine at the level of spermidine/spermine N1-acetyltransferase. (nih.gov)
  • Pyruvate dehydrogenase deficiency is characterized by the buildup of a chemical called lactic acid in the body and a variety of neurological problems. (nih.gov)
  • With decreased function of this complex, pyruvate builds up and is converted in another chemical reaction to lactic acid. (nih.gov)

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