Threonine: 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.Threonine Dehydratase: A pyridoxal-phosphate protein that catalyzes the deamination of THREONINE to 2-ketobutyrate and AMMONIA. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for ISOLEUCINE biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. This enzyme was formerly listed as EC 4.2.1.16.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.Phosphothreonine: The phosphoric acid ester of threonine. Used as an identifier in the analysis of peptides, proteins, and enzymes.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Serine: 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.Phosphoprotein Phosphatases: A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)Isoleucine: 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.Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Amino Acids: 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.Okadaic Acid: A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)Phosphoserine: The phosphoric acid ester of serine.Aspartate Kinase: An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.Protein Phosphatase 2: A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Protein Phosphatase 1: A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.PhosphopeptidesProto-Oncogene Proteins c-pim-1: Serine-threonine protein kinases that relay signals from CYTOKINE RECEPTORS and are involved in control of CELL GROWTH PROCESSES; CELL DIFFERENTIATION; and APOPTOSIS.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.L-Serine Dehydratase: A PYRIDOXAL-phosphate containing enzyme that catalyzes the dehydration and deamination of L-serine to form pyruvate. This enzyme was formerly listed as EC 4.2.1.13.Kinetics: The rate dynamics in chemical or physical systems.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Oxazoles: Five-membered heterocyclic ring structures containing an oxygen in the 1-position and a nitrogen in the 3-position, in distinction from ISOXAZOLES where they are at the 1,2 positions.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Carbon-Oxygen Lyases: Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Calcium-Calmodulin-Dependent Protein Kinases: A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)Phosphoamino Acids: Amino acids that contain phosphorus as an integral part of the molecule.Protein Kinase C: An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.PhosphoproteinsTyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Protein-Tyrosine Kinases: Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.Amino Acid Substitution: 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.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Ethers, Cyclic: Compounds of the general formula R-O-R arranged in a ring or crown formation.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Hydro-Lyases: Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.Threonine-tRNA Ligase: An enzyme that activates threonine with its specific transfer RNA. EC 6.1.1.3.Valine: 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.Casein Kinase II: A ubiquitous casein kinase that is comprised of two distinct catalytic subunits and dimeric regulatory subunit. Casein kinase II has been shown to phosphorylate a large number of substrates, many of which are proteins involved in the regulation of gene expression.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Proto-Oncogene Proteins c-akt: A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Glycine: 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.Proto-Oncogene Proteins: Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.Lysine: An essential amino acid. It is often added to animal feed.Glycine Hydroxymethyltransferase: A pyridoxal phosphate enzyme that catalyzes the reaction of glycine and 5,10-methylene-tetrahydrofolate to form serine. It also catalyzes the reaction of glycine with acetaldehyde to form L-threonine. EC 2.1.2.1.p21-Activated Kinases: A family of serine-threonine kinases that bind to and are activated by MONOMERIC GTP-BINDING PROTEINS such as RAC GTP-BINDING PROTEINS and CDC42 GTP-BINDING PROTEIN. They are intracellular signaling kinases that play a role the regulation of cytoskeletal organization.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Aspartate-Semialdehyde Dehydrogenase: An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.RNA, Transfer, Thr: A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.COS Cells: 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).)Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Alanine: 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.Proto-Oncogene Proteins c-raf: A ubiquitously expressed raf kinase subclass that plays an important role in SIGNAL TRANSDUCTION. The c-raf Kinases are MAP kinase kinase kinases that have specificity for MAP KINASE KINASE 1 and MAP KINASE KINASE 2.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Mucins: High molecular weight mucoproteins that protect the surface of EPITHELIAL CELLS by providing a barrier to particulate matter and microorganisms. Membrane-anchored mucins may have additional roles concerned with protein interactions at the cell surface.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Nutritional Requirements: The amounts of various substances in food needed by an organism to sustain healthy life.3T3 Cells: Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Precipitin Tests: 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.Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Blotting, Western: 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.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Amino Acid Motifs: 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.Phosphotyrosine: An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.HomoserineDNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Glycogen Synthase Kinase 3: A glycogen synthase kinase that was originally described as a key enzyme involved in glycogen metabolism. It regulates a diverse array of functions such as CELL DIVISION, microtubule function and APOPTOSIS.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Protein Conformation: 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).Protein Kinase Inhibitors: Agents that inhibit PROTEIN KINASES.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Phosphotransferases: A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.Peptides: 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.Mitogen-Activated Protein Kinases: A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).Point Mutation: 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.Conserved Sequence: 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.Death-Associated Protein Kinases: A family of calcium/calmodulin-dependent PROETIN-SERINE-THREONINE KINASES. They are ubiquitously expressed in adult and embryonic mammalian tissues, and their functions are tightly related to the early stages of eukaryotic programmed cell death.Intracellular Signaling Peptides and Proteins: Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.Bacterial Proteins: Proteins found in any species of bacterium.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Mitogen-Activated Protein Kinase Kinases: A serine-threonine protein kinase family whose members are components in protein kinase cascades activated by diverse stimuli. These MAPK kinases phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES and are themselves phosphorylated by MAP KINASE KINASE KINASES. JNK kinases (also known as SAPK kinases) are a subfamily.Microcystins: Cyclic heptapeptides found in MICROCYSTIS and other CYANOBACTERIA. Hepatotoxic and carcinogenic effects have been noted. They are sometimes called cyanotoxins, which should not be confused with chemicals containing a cyano group (CN) which are toxic.MAP Kinase Kinase Kinases: Mitogen-activated protein kinase kinase kinases (MAPKKKs) are serine-threonine protein kinases that initiate protein kinase signaling cascades. They phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES; (MAPKKs) which in turn phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs).Proteins: 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.Caseins: A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Aspartokinase Homoserine Dehydrogenase: A bifunctional protein consisting of aspartokinase, and homoserine dehydrogenase activities. It is found primarily in BACTERIA and in PLANTS.Cell Cycle Proteins: Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.Cyclic AMP-Dependent Protein Kinases: A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Activin Receptors: Receptors for ACTIVINS are membrane protein kinases belonging to the family of PROTEIN-SERINE-THREONINE KINASES, thus also named activin receptor-like kinases (ALK's). Activin receptors also bind TRANSFORMING GROWTH FACTOR BETA. As those transmembrane receptors of the TGF-beta superfamily (RECEPTORS, TRANSFORMING GROWTH FACTOR BETA), ALK's consist of two different but related protein kinases, Type I and Type II. Activins initiate cellular signal transduction by first binding to the type II receptors (ACTIVIN RECEPTORS, TYPE II ) which then recruit and phosphorylate the type I receptors (ACTIVIN RECEPTORS, TYPE I ) with subsequent activation of the type I kinase activity.Casein Kinases: A group of protein-serine-threonine kinases that was originally identified as being responsible for the PHOSPHORYLATION of CASEINS. They are ubiquitous enzymes that have a preference for acidic proteins. Casein kinases play a role in SIGNAL TRANSDUCTION by phosphorylating a variety of regulatory cytoplasmic and regulatory nuclear proteins.Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.CDC2 Protein Kinase: Phosphoprotein with protein kinase activity that functions in the G2/M phase transition of the CELL CYCLE. It is the catalytic subunit of the MATURATION-PROMOTING FACTOR and complexes with both CYCLIN A and CYCLIN B in mammalian cells. The maximal activity of cyclin-dependent kinase 1 is achieved when it is fully dephosphorylated.Cell Nucleus: Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Aurora Kinases: A family of highly conserved serine-threonine kinases that are involved in the regulation of MITOSIS. They are involved in many aspects of cell division, including centrosome duplication, SPINDLE APPARATUS formation, chromosome alignment, attachment to the spindle, checkpoint activation, and CYTOKINESIS.14-3-3 Proteins: A large family of signal-transducing adaptor proteins present in wide variety of eukaryotes. They are PHOSPHOSERINE and PHOSPHOTHREONINE binding proteins involved in important cellular processes including SIGNAL TRANSDUCTION; CELL CYCLE control; APOPTOSIS; and cellular stress responses. 14-3-3 proteins function by interacting with other signal-transducing proteins and effecting changes in their enzymatic activity and subcellular localization. The name 14-3-3 derives from numerical designations used in the original fractionation patterns of the proteins.Phosphatidylinositol 3-Kinases: Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.Nuclear Proteins: Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.Immunoprecipitation: The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Aspartic Acid: 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.Cantharidin: A toxic compound, isolated from the Spanish fly or blistering beetle (Lytta (Cantharis) vesicatoria) and other insects. It is a potent and specific inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A). This compound can produce severe skin inflammation, and is extremely toxic if ingested orally.Receptors, Transforming Growth Factor beta: Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behavior of cells. Two types of transforming growth factor receptors have been recognized. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Swine: 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).Acetylglucosamine: The N-acetyl derivative of glucosamine.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.3-Phosphoinositide-Dependent Protein Kinases: Highly conserved protein-serine threonine kinases that phosphorylate and activate a group of AGC protein kinases, especially in response to the production of the SECOND MESSENGERS, phosphatidylinositol 3,4,-biphosphate (PtdIns(3,4)P2) and phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3).Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)Mitosis: A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.Cattle: 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.Apoptosis: One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.Cell Cycle: The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.Tetradecanoylphorbol Acetate: A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.Ribosomal Protein S6 Kinases: A family of protein serine/threonine kinases which act as intracellular signalling intermediates. Ribosomal protein S6 kinases are activated through phosphorylation in response to a variety of HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Phosphorylation of RIBOSOMAL PROTEIN S6 by enzymes in this class results in increased expression of 5' top MRNAs. Although specific for RIBOSOMAL PROTEIN S6 members of this class of kinases can act on a number of substrates within the cell. The immunosuppressant SIROLIMUS inhibits the activation of ribosomal protein S6 kinases.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Membrane Proteins: 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.Staurosporine: An indolocarbazole that is a potent PROTEIN KINASE C inhibitor which enhances cAMP-mediated responses in human neuroblastoma cells. (Biochem Biophys Res Commun 1995;214(3):1114-20)Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Two-Hybrid System Techniques: Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.N-Acetylgalactosaminyltransferases: Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Cercopithecus aethiops: 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.Aurora Kinase A: An aurora kinase that localizes to the CENTROSOME during MITOSIS and is involved in centrosome regulation and formation of the MITOTIC SPINDLE. Aurora A overexpression in many malignant tumor types suggests that it may be directly involved in NEOPLASTIC CELL TRANSFORMATION.Adaptor Proteins, Signal Transducing: A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymesCell Line, Tumor: A cell line derived from cultured tumor cells.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Proline: 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.Culture Media: Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.Lyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Calcineurin: A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Mitogen-Activated Protein Kinase 1: A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.Glutathione Transferase: A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Nitrogen: 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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Protein Isoforms: Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Protein Tyrosine Phosphatases: An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.
AMP-activated protein kinase phosphorylation of endothelial NO synthase. (1/3530)
The AMP-activated protein kinase (AMPK) in rat skeletal and cardiac muscle is activated by vigorous exercise and ischaemic stress. Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Here we show that AMPK co-immunoprecipitates with cardiac endothelial NO synthase (eNOS) and phosphorylates Ser-1177 in the presence of Ca2+-calmodulin (CaM) to activate eNOS both in vitro and during ischaemia in rat hearts. In the absence of Ca2+-calmodulin, AMPK also phosphorylates eNOS at Thr-495 in the CaM-binding sequence, resulting in inhibition of eNOS activity but Thr-495 phosphorylation is unchanged during ischaemia. Phosphorylation of eNOS by the AMPK in endothelial cells and myocytes provides a further regulatory link between metabolic stress and cardiovascular function. (+info)Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C betaII. (2/3530)
Protein kinase C is processed by three phosphorylation events before it is competent to respond to second messengers. Specifically, the enzyme is first phosphorylated at the activation loop by another kinase, followed by two ordered autophosphorylations at the carboxyl terminus (Keranen, L. M., Dutil, E. M., and Newton, A. C. (1995) Curr. Biol. 5, 1394-1403). This study examines the role of negative charge at the first conserved carboxyl-terminal phosphorylation position, Thr-641, in regulating the function and subcellular localization of protein kinase C betaII. Mutation of this residue to Ala results in compensating phosphorylations at adjacent sites, so that a triple Ala mutant was required to address the function of phosphate at Thr-641. Biochemical and immunolocalization analyses of phosphorylation site mutants reveal that negative charge at this position is required for the following: 1) to process catalytically competent protein kinase C; 2) to allow autophosphorylation of Ser-660; 3) for cytosolic localization of protein kinase C; and 4) to permit phorbol ester-dependent membrane translocation. Thus, phosphorylation of Thr-641 in protein kinase C betaII is essential for both the catalytic function and correct subcellular localization of protein kinase C. The conservation of this residue in every protein kinase C isozyme, as well as other members of the kinase superfamily such as protein kinase A, suggests that carboxyl-terminal phosphorylation serves as a key molecular switch for defining kinase function. (+info)Is human thioredoxin monomeric or dimeric? (3/3530)
We have examined the molecular weight and rotational correlation time of human thioredoxin by analytical ultracentrifugation and NMR spectroscopy, respectively. Two variants of human thioredoxin were studied, namely human thioredoxin identical in amino acid sequence to the one whose NMR structure we previously determined (C62A, C69A, C73A, M74T) and human thioredoxin (C62A, C69A, C73A, M74) containing the wild-type amino acid methionine at position 74. In both cases, the experimental data indicate that the predominant species is monomeric and we find no evidence for the existence of a well-defined dimeric form as was observed in the recently reported crystal structure (Weichsel et al., 1996) of human thioredoxin and the C73S mutant. (+info)The nucleoprotein of Marburg virus is target for multiple cellular kinases. (4/3530)
The nucleoprotein (NP) of Marburg virus is phosphorylated at serine and threonine residues in a ratio of 85:15, regardless of whether the protein is isolated from virions or from eukaryotic expression systems. Phosphotyrosine is absent. Although many potential phosphorylation sites are located in the N-terminal half of NP, this part of the protein is not phosphorylated. Analyses of phosphorylation state and phosphoamino acid content of truncated NPs expressed in HeLa cells using the vaccinia virus T7 expression system led to the identification of seven phosphorylated regions (region I*, amino acids 404-432; II*, amino acids 446-472; III*, amino acids 484-511; IV*, amino acids 534-543; V*, amino acid 549; VI*, amino acids 599-604; and VII*, amino acid 619) with a minimum of seven phosphorylated amino acid residues located in the C-terminal half of NP. All phosphothreonine residues and consensus recognition sequences for protein kinase CKII are located in regions I*-V*. Regions VI* and VII* contain only phosphoserine with three of four serine residues in consensus recognition motifs for proline-directed protein kinases. Mutagenesis of proline-adjacent serine residues to alanine or aspartic acid did not influence the function of NP in a reconstituted transcription/replication system; thus it is concluded that serine phosphorylation in the most C-terminal part of NP is not a regulatory factor in viral RNA synthesis. (+info)CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding. (5/3530)
Metabotropic glutamate receptors (mGluRs) are a family of G protein-coupled receptors characterized by a large, extracellular N-terminal domain comprising the glutamate-binding site. In the current study, we examined the pharmacological profile and site of action of the non-amino-acid antagonist 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester (CPCCOEt). CPCCOEt selectively inhibited glutamate-induced increases in intracellular calcium at human mGluR1b (hmGluR1b) with an apparent IC50 of 6.5 microM while having no agonist or antagonist activity at hmGluR2, -4a, -5a, -7b, and -8a up to 100 microM. Schild analysis indicated that CPCCOEt acts in a noncompetitive manner by decreasing the efficacy of glutamate-stimulated phosphoinositide hydrolysis without affecting the EC50 value or Hill coefficient of glutamate. Similarly, CPCCOEt did not displace [3H]glutamate binding to membranes prepared from mGluR1a-expressing cells. To elucidate the site of action, we systematically exchanged segments and single amino acids between hmGluR1b and the related subtype, hmGluR5a. Substitution of Thr815 and Ala818, located at the extracellular surface of transmembrane segment VII, with the homologous amino acids of hmGluR5a eliminated CPCCOEt inhibition of hmGluR1b. In contrast, introduction of Thr815 and Ala818 at the homologous positions of hmGluR5a conferred complete inhibition by CPCCOEt (IC50 = 6.6 microM), i.e., a gain of function. These data suggest that CPCCOEt represents a novel class of G protein-coupled receptor antagonists inhibiting receptor signaling without affecting ligand binding. We propose that the interaction of CPCCOEt with Thr815 and Ala818 of mGluR1 disrupts receptor activation by inhibiting an intramolecular interaction between the agonist-bound extracellular domain and the transmembrane domain. (+info)The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A. (6/3530)
Flexible loops, often referred to as flaps, have been shown to play a role in catalytic mechanisms of different enzymes. Flaps at the active site regions have been observed in the crystal structures of aspartic proteinases and their residues implicated in the catalytic processes. This research investigated the role of the flap residue, threonine 77, in the activation of pepsinogen and the catalytic mechanism of pepsin. Three mutants, T77S, T77V and T77G, were constructed. Differences in amino acid polarity and hydrogen bonding potential were shown to have an influence on the activation and catalytic processes. T77S activated at the same rate and had similar catalytic parameters as the wild-type pepsin. The activation rates of T77V and T77G were slower and their catalytic efficiencies lower than the wild-type. The results demonstrated that the threonine 77 polar side chain played a role in a proteolysis. The contribution of the side chain to zymogen activation was associated with the proteolytic cleavage of the prosegment. It was postulated that the hydroxyl group at position 77 provided an essential hydrogen bond that contributed to proper substrate alignment and, indirectly, to a catalytically favorable geometry of the transition state. (+info)EPR spectroscopy of VO2+-ATP bound to catalytic site 3 of chloroplast F1-ATPase from Chlamydomonas reveals changes in metal ligation resulting from mutations to the phosphate-binding loop threonine (betaT168). (7/3530)
Site-directed mutations were made to the phosphate-binding loop threonine in the beta-subunit of the chloroplast F1-ATPase in Chlamydomonas (betaT168). Rates of photophosphorylation and ATPase-driven proton translocation measured in coupled thylakoids purified from betaT168D, betaT168C, and betaT168L mutants had <10% of the wild type rates, as did rates of Mg2+-ATPase activity of purified chloroplast F1-ATPase (CF1). The EPR spectra of VO2+-ATP bound to Site 3 of CF1 from wild type and mutants showed that EPR species C, formed exclusively upon activation, was altered in CF1 from each mutant in both signal intensity and in 51V hyperfine parameters that depend on the equatorial VO2+ ligands. These data provide the first direct evidence that Site 3 is a catalytic site. No significant differences between wild type and mutants were observed in EPR species B, the predominant form of the latent enzyme. Thus, the phosphate-binding loop threonine is an equatorial metal ligand in the activated conformation but not in the latent conformation of Site 3. The metal-nucleotide conformation that gives rise to species B is consistent with the Mg2+-ADP complex that becomes entrapped in a catalytic site in a manner that regulates enzymatic activity. The lack of catalytic function of CF1 with entrapped Mg2+-ADP may be explained in part by the absence of the phosphate-binding loop threonine as a metal ligand. (+info)Defining the substrate specificity of cdk4 kinase-cyclin D1 complex. (8/3530)
cdk4 kinase-cyclin D1 complex (cdk4/D1) does not phosphorylate all of the sites within retinoblastoma protein (Rb) equally. Comparison of five phosphorylation sites within the 15 kDa C domain of Rb indicates that Ser795 is the preferred site of phosphorylation by cdk4/D1. A series of experiments has been performed to determine the properties of this site that direct preferential phosphorylation. For cdk4/D1, the preferred amino acid at the third position C-terminal to the phosphorylated serine/threonine is arginine. Substitution of other amino acids, including a conservative change to lysine, has dramatic effects on the rates of phosphorylation. This information has been used to mutate less favorable sites in Rb, converting them to sites that are now preferentially phosphorylated by cdk4/D1. A conserved site at Ser842 in the related pocket protein p107 is also preferentially phosphorylated by cdk4/D1. Although Rb and p107 differ significantly in sequence, the Rb Ser795 site can replace the p107 Ser842 site without affecting the rate of phosphorylation. These results suggest that although a determinant of specificity resides in the sequences surrounding the phosphorylated site, the structural context of the site is also a critical parameter of specificity. (+info)
"Threonine Requirement of Pigs Weighing 5 to 15 Kgs." by A. J. Lewis and E. R. Peo, Jr.
Plasma Threonine in Premature Infants | American Academy of Pediatrics
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Threonine: Uses, Side Effects, Interactions, Dosage, and Warning
Plasma Threonine in Premature Infants | American Academy of Pediatrics
KEGG PATHWAY: Glycine, serine and threonine metabolism + T30050
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"Threonine Requirement of Pigs Weighing 5 to 15 Kgs." by A. J. Lewis and E. R. Peo, Jr.
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Needed to determine if threonineAddition of threonineCalled glycineUreaAminoDosesNutrientsPlasmaSymptomsAmountsSuggestsDietDetermineRequireTimesFunctionTyrosineAminoBiosynthesisPhosphatasesProteinsKinaseEscherichiaCatalyzed by serinePhosphatase activityMicroorganismsSynthaseGeneCatabolismMethionineAspartateFermentationDose of threonineAmount of threonineSerine or threonineDeaminaseMolecularAntibodyEnzymes11.1High threonineHydroxylResidueAntibodiesSignal transductionSupplementsPhosphateEvonik IndustriesLysineDehydrogenaseDeficiency includeCottage cheeseRacemicCentersBacterialDefinitionEnzyme that catalyzesAspartic acid
Needed to determine if threonine1
- More evidence is needed to determine if threonine was actually at fault. (webmd.com)
Addition of threonine1
- The addition of threonine increased weight gain (P (unl.edu)
Called glycine1
- Threonine is changed in the body to a chemical called glycine. (webmd.com)
Urea1
- Plasma urea concentrations decreased as threonine was increased in the diet, reaching a plateau at .68% dietary threonine. (unl.edu)
Amino2
Doses2
- Doses of up to 4 grams of threonine daily have been used safely for up to 12 months. (webmd.com)
- At this time there is not enough scientific information to determine an appropriate range of doses for threonine. (webmd.com)
Nutrients1
- The diets (16% crude protein) were composed primarily of grain sorghum, oat groats and soybean meal supplemented with minerals, vitamins, lysine, tryptophan, methionine and isoleucine, and were calculated to be adequate in all nutrients except threonine and crude protein. (unl.edu)
Plasma1
- In the discussion, referring to their previous study in preterm infants, 2 they concluded that their results show a positive correlation between the plasma threonine concentration and the threonine intake but they cannot support our data 3 showing that the ability to metabolize a high threonine intake is impaired in preterm infants as compared with term infants. (aappublications.org)
Symptoms2
- Taking 2 grams to 4 grams of threonine daily for up to 12 months does not seem to slow the progression of ALS or reduce symptoms. (webmd.com)
- Early research suggests that taking 1.5 grams to 2 grams of threonine by mouth three times daily might improve some symptoms in people with familial spastic paraparesis. (webmd.com)
Suggests2
- Multiple sclerosis (MS). Early research suggests that taking 2.5 grams of threonine by mouth three times daily for 8 weeks does not reduce muscle stiffness (spasticity) in people with MS. (webmd.com)
- Early research suggests that taking 2 grams of threonine by mouth three times daily modestly decreases muscle contractions in people with spinal spasticity caused by spinal cord injury. (webmd.com)
Diet1
Determine1
- Weanling crossbred pigs (avg initial wt 6.4 kg) were fed diets containing six levels of threonine to determine the threonine requirement of young pigs fed diets somewhat similar to those used in commercial swine production. (unl.edu)
Require1
Times1
- In one study, ALS patients taking 1 gram of threonine four times per day for 6 months had significantly reduced lung function compared to patients who did not receive threonine. (webmd.com)
Function2
Tyrosine12
- Threonine is an α- amino acid that is common in many proteins and together with serine and tyrosine is one of three proteinogenic amino acids bearing an alcohol group. (newworldencyclopedia.org)
- Phosphorylation is observed on serine, threonine, tyrosine and histidine residues. (abcam.com)
- Protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) is well established as a key regulatory posttranslational modification in eukaryotes, but little is known about its extent and function in prokaryotes. (mcponline.org)
- We identified 103 unique phosphopeptides from 78 B. subtilis proteins and determined 78 phosphorylation sites: 54 on serine, 16 on threonine, and eight on tyrosine. (mcponline.org)
- Eukaryotic cells rely extensively on phosphorylating the hydroxyl group of the side chains of serine/threonine/tyrosine for their signal transduction cascades ( 2 , 3 ). (mcponline.org)
- The importance of serine/threonine/tyrosine kinases and phosphatases for cell physiology has been widely documented in eukaryotes ranging from yeast ( 4 ) to human ( 5 ). (mcponline.org)
- For some time the field of protein phosphorylation maintained this clear-cut picture of eukaryotes using serine/threonine/tyrosine phosphorylation and bacteria using histidine and aspartate phosphorylation instead. (mcponline.org)
- However, in the last 2 decades evidence has accumulated for serine/threonine/tyrosine phosphorylation in bacteria ( 9 ). (mcponline.org)
- Interestingly signaling via serine/threonine/tyrosine phosphorylation is often implicated in the regulation of bacterial virulence ( 12 ), and in some cases it is also known to interfere with eukaryotic signal transduction, thereby rendering the host more prone to infection ( 13 , 14 ). (mcponline.org)
- pro·tein ki·nase/ ( pro´tēn ki´nās ) an enzyme that catalyzes the phosphorylation of serine, threonine, or tyrosine groups in enzymes or other proteins, using ATP as a phosphate donor. (thefreedictionary.com)
- Any of a group of kinases that phosphorylate the amino acids serine, threonine, and tyrosine in certain proteins, that regulate essential aspects of cell growth and movement, and that can cause cancer and other diseases when dysfunctional. (thefreedictionary.com)
- The dephosphorylation and inactivation of ERK1/2 is catalyzed by dual specificity phosphatases, protein-tyrosine specific phosphatases, and protein-serine/threonine phosphatases. (selleckchem.com)
Amino28
- Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. (wikipedia.org)
- Protein involved in the synthesis of the essential amino acid threonine. (uniprot.org)
- Threonine is an essential amino acid . (webmd.com)
- The L-isomer of threonine, which is the only form that is involved in protein synthesis, is one of the 20 standard amino acids common in animal proteins and required for normal functioning in humans . (newworldencyclopedia.org)
- Threonine is also classified as an "essential amino acid" since it cannot be synthesized by the human body from other compounds through chemical reactions and thus has to be taken in with the diet. (newworldencyclopedia.org)
- However, the name L -threonine is used for one single enantiomer , (2 S , 3 R )-2-amino-3-hydroxybutanoic acid. (newworldencyclopedia.org)
- As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine or, more commonly, threonine-containing proteins. (newworldencyclopedia.org)
- Threonine (abbreviated as Thr or T) is an amino acid that is used in the biosynthesis of proteins. (wikipedia.org)
- Threonine was the last of the 20 common proteinogenic amino acids to be discovered. (wikipedia.org)
- The amino acid was named threonine because it was similar in structure to threose, a four-carbon monosaccharide with molecular formula C4H8O4 Threonine is one of two proteinogenic amino acids with two chiral centers, the other being isoleucine. (wikipedia.org)
- citation needed] As an essential amino acid, threonine is not synthesized in humans, and needs to be present in proteins in the diet. (wikipedia.org)
- Threonine is an essential amino acid that the body can not synthesize and therefore must be provided by the diet. (botanical-online.com)
- Although you can take supplements of threonine, it is recommended to cover the needs of this amino acid through a balanced diet . (botanical-online.com)
- Threonine (abbreviated as Thr or T ) is an α- amino acid with the chemical formula HO 2 CCH(NH 2 )CH(OH)CH 3 . (bionity.com)
- As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins. (bionity.com)
- Threonine is an essential amino acid that is found in high concentrations in the heart, skeletal muscles and central nervous system. (herbalremedies.com)
- Amino acid supplements prefaced by the letter L, such as L-Threonine, are more similar to the amino acids in the body than those that start with the letter D, with the exception of D-L phenylalanine, which treats chronic pain. (herbalremedies.com)
- The product under assessment is considered an efficacious source of the amino acid l‐threonine for all animal species. (europa.eu)
- Threonine is an essential amino acid, which animals cannot synthesize. (genome.jp)
- The present aim of the paper is to grow and to study the various properties of L-threonine amino acid single crystal in various aspects. (hindawi.com)
- To learn more about threonine and amino acids, review the accompanying lesson on Threonine Amino Acid: Structure & Function. (study.com)
- L-threonine is an essential amino acid in humans, meaning that it cannot be synthesized in the body. (xtend-life.com)
- L-threonine is one of the 20 common proteinogenic amino acids for humans, which are used to construct proteins. (xtend-life.com)
- The American nutritionist William Cumming Rose discovered threonine during the 1930s, making it the last of the common proteinogenic amino acids to be discovered. (xtend-life.com)
- Evonik Industries produces and markets all four important amino acids for animal nutrition: DL-Methionine, Biolys® (L-Lysine), L-Threonine and L-Tryptophan. (allaboutfeed.net)
- Douglas Labs L-Threonine 500 mg 60 caps supplies 500 mg of this amino acid in each capsule. (integrativepsychiatry.net)
- The remaining three studies deals with the synthesis of C-glycosidic analogues of glycosylated amino acids, hydroxy norvaline, threonine and hydroxylysine.The synthesis of each amino acid required control of several stereogenic centra and utilizes a variety of approaches such as use of stereoselective reactions, chiral auxilaries, chiral templates and asymmetric catalysis. (diva-portal.org)
- In response to the increased use of high fibre co-products, such as wheat mill run in swine rations, researchers with the Prairie Swine Centre, the University of Saskatchewan and the Western College of Veterinary Medicine are evaluating the requirement for the amino acid Threonine, to maintain efficient growth, especially when pigs are challenged by disease. (farmscape.ca)
Biosynthesis7
- Enzymes involved in a typical biosynthesis of threonine include: aspartokinase β-aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase. (wikipedia.org)
- These modules contribute to a molecular circuit that regulates threonine metabolism and buffers deficiency in deoxyribonucleotide biosynthesis. (pnas.org)
- This work tests a model constructed after unexpectedly finding threonine biosynthesis to play a role in buffering growth inhibition with the deoxyribonucleotide (dNTP) biosynthesis inhibitor, hydroxyurea (HU) ( 4 ). (pnas.org)
- 4. The method according to claim 1, wherein an L-threonine biosynthesis enzyme in the microorganism is modified so that the enzyme is not subject to feedback inhibition by L-threonine. (freepatentsonline.com)
- 5. The method according to claim 4, wherein the L-threonine biosynthesis enzyme is selected from the group consisting of aspartokinase, homoserine kinase, threonine synthase, and combinations thereof. (freepatentsonline.com)
- The functional feature 'microorganism which already produces L-threonine' was clear to the skilled person, who would be able to distinguish between L-threonine which results from biosynthesis and production of L-threonine. (epo.org)
- and page 359, section 10.3), which also distinguished between biosynthesis of L-threonine and construction of L-threonine producing strains. (epo.org)
Phosphatases6
- The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. (wikipedia.org)
- Genes coding for phosphoserine/threonine phosphatases are less numerous in vertebrate genomes than those for serine /threonine kinases, and the complexity of phosphatases function arises in part from the interactions of catalytic subunits with other proteins. (sigmaaldrich.com)
- Prior to the knowledge of their sequence, phosphoserine/threonine phosphatases were classified on the basis of their substrate preference and inhibitor sensitivity. (sigmaaldrich.com)
- Molecular cloning revealed that serine/threonine phosphatases belong to two different families of about a dozen of genes each in mammals: the phosphoprotein phosphatase P (PPP) family includes PP1, PP2A, PP2B, and a few related enzymes, PP4, PP5, PP6 and PP7, while the phosphoprotein phosphatase M family (PPM) includes PP2C and related enzymes. (sigmaaldrich.com)
- The serine/threonine phosphatases of the PPP family are mostly regulated by protein-protein interactions. (sigmaaldrich.com)
- The serine/threonine protein phosphatases play an essential role in the cellular signalling, metabolism, and cell cycle control. (mdpi.com)
Proteins8
- These enzymes transfer phosphates to the oxygen atom of a serine or threonine sidechain in proteins . (wikipedia.org)
- Types include those acting directly as receptors ( Receptor protein serine/threonine kinase ) and Intracellular signaling peptides and proteins . (wikipedia.org)
- Like serine, threonine is sometimes in substantial concentrations in the outer regions of soluble proteins due to its hydrophilic nature. (newworldencyclopedia.org)
- Threonine also reflects an element of human responsibility, for one's diet must contain sufficient threonine to synthesize the proteins. (newworldencyclopedia.org)
- Both threonine and serine are very hydrophilic, therefore the outer regions of soluble proteins tend to be rich with them. (newworldencyclopedia.org)
- Fortunately, most proteins contain threonine and so a deficiency is unlikely. (newworldencyclopedia.org)
- This is most likely to occur if you are a strict vegetarian, as the best sources of L-threonine are animal proteins. (xtend-life.com)
- Conservation of an analogous threonine across all RIN4-like proteins suggests a key function for this residue beyond the regulation of RPM1. (nih.gov)
Kinase21
- A serine/threonine protein kinase ( EC 2.7.11.1 ) is a kinase enzyme that phosphorylates the OH group of serine or threonine (which have similar sidechains). (wikipedia.org)
- In enzymology , the term non-specific serine/threonine protein kinase describes a class of enzymes that belong to the family of transferases , specifically protein-serine/threonine kinases . (wikipedia.org)
- Serine/Threonine Kinase receptors play a role in the regulation of cell proliferation, programmed cell death ( apoptosis ), cell differentiation, and embryonic development. (wikipedia.org)
- Nezu, J. Molecular cloning of a novelserine/threonine protein kinase expressed in human fetalliver(unpublished). (nature.com)
- Su, J.-Y., Erikson, E. & Maller, J. L. Cloning and characterization of a novel serine/threonine protein kinase expressed in early Xenopus embryos. (nature.com)
- Here we demonstrate that purified recombinant phytochromes from a higher plant and a green alga exhibit serine/threonine kinase activity similar to that of phytochrome isolated from dark grown seedlings. (pnas.org)
- Based on comparative protein sequence alignments and biochemical cross-talk experiments with the response regulator substrate of the cyanobacterial phytochrome Cph1, we propose that eukaryotic phytochromes are histidine kinase paralogs with serine/threonine specificity whose enzymatic activity diverged from that of a prokaryotic ancestor after duplication of the transmitter module. (pnas.org)
- In this regard, biochemical analysis of purified oat phytochrome A in the mid-1980s ( 10 - 13 ) revealed an associated polycation-stimulated, pyrophosphate-inhibited serine/threonine (Ser/Thr) protein kinase activity implicating phytochrome itself to be the enzyme responsible. (pnas.org)
- Synthetic peptide corresponding to Human Serine/threonine-protein kinase 4 aa 324-388. (abcam.com)
- Your search returned 72 B-Raf proto-oncogene, serine/threonine kinase ELISA ELISA Kit across 10 suppliers. (biocompare.com)
- Identification of a novel serine/threonine kinase that inhibits TNF-induced NF-kappaB activation and p53-induced transcription. (wikigenes.org)
- Serine/Threonine Protein Kinase Pim 1 (Oncogene PIM1 or PIM1 or EC 2.7.11.1) pipeline Target constitutes close to 15 molecules. (researchandmarkets.com)
- Serine/Threonine Protein Kinase Pim 1 (Oncogene PIM1 or PIM1 or EC 2.7.11.1) - Proto-oncogene serine/threonine-protein kinase Pim-1 is an enzyme encoded by the PIM1 gene. (researchandmarkets.com)
- It also reviews key players involved in Serine/Threonine Protein Kinase Pim 1 (Oncogene PIM1 or PIM1 or EC 2.7.11.1) targeted therapeutics development with respective active and dormant or discontinued projects. (researchandmarkets.com)
- It yielded a serine/threonine protein kinase called protein kinase N 1 (PKN1). (nih.gov)
- DUBLIN--( BUSINESS WIRE )--The "Serine Threonine Protein Kinase ATR - Pipeline Review, H2 2019" drug pipelines has been added to ResearchAndMarkets.com's offering. (businesswire.com)
- Serine/Threonine Protein Kinase ATR (Ataxia Telangiectasia And Rad3 Related Protein or FRAP Related Protein 1 or ATR or EC 2.7.11.1) pipeline Target constitutes close to 17 molecules. (businesswire.com)
- Serine/Threonine Protein Kinase ATR (Ataxia Telangiectasia And Rad3 Related Protein or FRAP Related Protein 1 or ATR or EC 2.7.11.1) - Serine/threonine-protein kinase ATR is an enzyme encoded by the ATR gene. (businesswire.com)
- The Bub1 protein is a serine/threonine kinase that acts in the mitotic spindle checkpoint by recruiting components and promoting kinetochore formation in the inner centromere. (rndsystems.com)
- The serine/threonine kinase Pim-2 is a novel anti-apoptotic mediator in myeloma cells. (biomedsearch.com)
- We demonstrate herein that IL-6 and TNF family cytokines, TNFα, BAFF and APRIL, but not IGF-1 cooperatively enhance the expression of the serine/threonine kinase Pim-2 in MM cells. (biomedsearch.com)
Escherichia6
- Threonine synthesis from aspartate in Escherichia coli cell-free extracts: pathway dynamics" (PDF). (wikipedia.org)
- A method for producing L-threonine is described which includes the steps of culturing a microorganism belonging to the genus Escherichia that has an ability to produce L-threonine, in a fermentation medium containing a carbon source, a nitrogen source, and a sulfur source, and collecting L-threonine, wherein the sulfur concentration in the medium is regulated so that it is a predetermined level or lower. (freepatentsonline.com)
- The product subject of this assessment is l‐threonine produced by fermentation with a genetically modified strain of Escherichia coli (CGMCC 7.232). (europa.eu)
- 6. L-threonine-producing microorganisms of the family Enterobacteriaceae, especially of the genus Escherichia, in which one or more genes selected from the group consisting of lpd, aceE and aceF and alleles of the genes which result from the degeneracy of the genetic code or from neutral sense mutations is (are) present in overexpressed form, whereby overexpression is achieved in microorganisms which already produce L-threonine. (epo.org)
- SummaryA rapid method for purifying L-threonine dehydrogenase from Escherichia coli K-12 cells, grown on a medium containing L-threonine as carbon source, has been developed. (umich.edu)
- The following threonine catabolism pathway is initiated by threonine dehydratase which has been cloned and sequenced from Escherichia coli ( Datta et al, 1987 ). (ethz.ch)
Catalyzed by serine1
- The mechanism of the first step is analogous to that catalyzed by serine dehydratase, and the serine and threonine dehydratase reactions are probably catalyzed by the same enzyme. (wikipedia.org)
Phosphatase activity2
- Intriguingly, Eyas harbor a separate threonine (Thr) phosphatase activity, which was previously implicated in innate immunity. (jci.org)
- Abnormal serine/threonine phosphatase activity has been linked with several diseases, including diabetes, cardiovascular disorders, cancer, and Alzheimer's disease. (horizondiscovery.com)
Microorganisms3
- In plants and microorganisms , threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. (newworldencyclopedia.org)
- Many plants and some microorganisms can synthesize L-threonine by using homoserine and alpha-aspartyl-semialdehyde to produce aspartic acid. (xtend-life.com)
- Threonine synthase is a pyridoxal phosphate enzyme which catalyses the last step in the synthesis of threonine in plants and microorganisms. (cea.fr)
Synthase4
- threonine synthase. (bionity.com)
- Amir R, Hacham Y, Galili G (2002) Cystathionine gamma-synthase and threonine synthase operate in concert to regulate carbon flow towards methionine in plants. (springer.com)
- Bartlem D, Lambein I, Okamoto T, Itaya A, Uda Y, Kijima F, Tamaki Y, Nambara E, Naito S (2000) Mutation in the threonine synthase gene results in an over-accumulation of soluble methionine in Arabidopsis. (springer.com)
- Allosteric threonine synthase. (cea.fr)
Gene3
- In humans the gene for threonine dehydrogenase is an inactive pseudogene, so threonine it is converted to α-ketobutyrate. (wikipedia.org)
- Alasdair J Edgar (2005) Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene. (wikipedia.org)
- it is an abundant RNA in cells grown with serine and threonine as nitrogen source, whereas it is not detected when cells are grown on ammonium or proline, i.e., the transcription of the CHA1 gene is induced by serine or threonine. (genetics.org)
Catabolism3
- a central step in threonine catabolism. (drugs.com)
- Molecular genetics of serine and threonine catabolism in Saccharomyces cerevisiae. (genetics.org)
- As both threonine and methionine serve as substrates for isoleucine synthesis, their synthesis and catabolism under different developmental and environmental conditions also influence isoleucine availability. (springer.com)
Methionine2
- The following is a text-format methionine and threonine pathway map. (ethz.ch)
- Together, methionine gamma-lyase and threonine deaminase maintain the isoleucine equilibrium in plants under varied substrate availabilities. (springer.com)
Aspartate1
- Threonine is synthesized from aspartate in bacteria such as E. coli. (wikipedia.org)
Fermentation4
- Following a request from the European Commission, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on l‐threonine produced by fermentation with Corynebacterium glutamicum ■■■■■ when used as a nutritional additive in feed and water for drinking for all animal species and categories. (europa.eu)
- The product l‐threonine, manufactured by fermentation with E. coli CGMCC 7.232, does not raise any safety concern with regard to the genetic modification of the production strain. (europa.eu)
- 本发明涉及生物发酵行业苏氨酸提取工艺领域，具体提供一种苏氨酸母液处理新方法。 The present invention relates (google.com)
- 前，苏氨酸的生产方法主要有发酵法、蛋白质水解法和化学合成法三种，其中微生物发酵法 (google.com)
Dose of threonine2
- The appropriate dose of threonine depends on several factors such as the user's age, health, and several other conditions. (webmd.com)
- A good dose of threonine in the diet ensures the proper production of substances like collagen , essential for proper maintenance of connective tissues, skin and tooth enamel, which are essential to maintain strong, resilient, healthy teeth. (botanical-online.com)
Amount of threonine10
- The basic type of basil is Basil, fresh , where the amount of threonine in 100g is 0.104 g. (dietandfitnesstoday.com)
- For a typical serving size of 2 tbsp, chopped (or 5.3 g) the amount of Threonine is 0.01 g. (dietandfitnesstoday.com)
- 100 calories of basil, fresh is a serving size of 4.35 g, and the amount of Threonine is 0.45 g. (dietandfitnesstoday.com)
- The corresponding Calories for basil ranked by the amount of threonine per 100g is shown below in the basil calories chart. (dietandfitnesstoday.com)
- The average (or more correctly the arithmetic mean) amount of threonine contained in 100g of basil, based on the list below of 2 different items under the general description of basil, is 0.43 g of threonine. (dietandfitnesstoday.com)
- Using the list below for the 2 different basil nutrition entries in our database, the highest amount of threonine is found in Spices, basil, dried which contains 0.76 g of threonine per 100g . (dietandfitnesstoday.com)
- The basic type of pepper is Spices, pepper, black , where the amount of threonine in 100g is 0.244 g. (dietandfitnesstoday.com)
- For a typical serving size of 1 tbsp, ground (or 6.9 g) the amount of Threonine is 0.02 g. (dietandfitnesstoday.com)
- 100 calories of spices, pepper, black is a serving size of 0.4 g, and the amount of Threonine is 0.1 g. (dietandfitnesstoday.com)
- Using the list below for the 1 different pepper nutrition entries in our database, the highest amount of threonine is found in Spices, pepper, black which contains 0.244 g of threonine per 100g . (dietandfitnesstoday.com)
Serine or threonine1
- While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence . (wikipedia.org)
Deaminase2
- The dimeric intermediate substructures of threonine deaminase, which are obtained by alkaline dialysis of the native tetrameric enzyme, are inactive after reassembly unless they are subsequently exposed to maturation-inducing ligands for which the enzyme possesses stereospecific binding sites. (sciencemag.org)
- The catabolic L-serine (L-threonine) deaminase of Saccharomyces cerevisiae allows the yeast to grow on media with L-serine or L-threonine as sole nitrogen source. (genetics.org)
Molecular1
Antibody1
- L-threonine supports the immune system through its role in antibody production. (xtend-life.com)
Enzymes2
- With an easily removed hydrogen on the hydroxyl side chain, threonine is often a hydrogen donor in enzymes . (newworldencyclopedia.org)
- Its hydrogen is easy to remove, so threonine and serine often act as hydrogen donors in enzymes . (newworldencyclopedia.org)
11.11
- This entry represents serine/threonine-protein kinases ( EC:2.7.11.1 ) such as Rio3. (ebi.ac.uk)
High threonine2
- In the discussion, referring to their previous study in preterm infants, 2 they concluded that their results show a positive correlation between the plasma threonine concentration and the threonine intake but they cannot support our data 3 showing that the ability to metabolize a high threonine intake is impaired in preterm infants as compared with term infants. (aappublications.org)
- The method provided by the invention has the advantages of low production cost, high threonine extraction yield and little wastewater discharge, is economical and environment-friendly and has a broad application prospect. (google.com)
Hydroxyl1
- Threonine, like serine , has a short group ended with a hydroxyl group. (newworldencyclopedia.org)
Residue2
- The threonine residue (component) is susceptible to numerous posttranslational modifications. (newworldencyclopedia.org)
- RIN4(142-176) is necessary and, with appropriate localization sequences, sufficient to support effector-triggered RPM1 activation, with the threonine residue at position 166 being critical. (nih.gov)
Antibodies2
- Listed below are anti-Taspase, Threonine Aspartase 1 antibodies from multiple suppliers. (biocompare.com)
- Your search returned 27 Taspase, Threonine Aspartase 1 Antibodies across 10 suppliers. (biocompare.com)
Signal transduction1
- These PP-2A inhibitors could be useful tools for studying serine/threonine-phosphatase-mediated signal transduction. (biochemj.org)
Supplements3
- Additional benefits of L-threonine supplements include the support of bone and liver health as well as the immune system. (xtend-life.com)
- This role means that L-threonine supplements may support the growth of healthy connective tissue, especially in the heart where L-threonine is more concentrated. (xtend-life.com)
- The most significant indication that you may need L-threonine supplements is if your diet is deficient in L-threonine. (xtend-life.com)
Phosphate2
- Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. (wikipedia.org)
- a protein]-serine/threonine phosphate + H 2 O = [a protein]-serine/threonine + phosphate. (uniprot.org)
Evonik Industries1
- The Health & Nutrition Business Unit of Evonik Industries, Germany is raising its prices for L-Threonine feed grade € 0.12/kg in Europe and US$ 0.15/kg in other regions, due to incurred high costs of raw materials, labor and utilities. (allaboutfeed.net)
Lysine5
- 1. Effects of dietary threonine:lysine ratio and sanitary conditions on performance, plasma urea nitrogen, plasma-free threonine and lysine of weaned pigs. (evonik.com)
- Research from the University of Illinois is helping to determine the correct ratio of threonine to lysine in pig diets, and how this ratio is affected by the fiber content of the diets. (thepigsite.com)
- There's been some confusion about the ideal threonine to lysine ratio," says Stein. (thepigsite.com)
- Both low- and high-fiber diets were then supplemented with threonine to achieve a standardized ileal digestible threonine:lysine (SID Thr:Lys) ratio of 0.45, 0.54, 0.63, 0.72, 0.81, or 0.90. (thepigsite.com)
- The paper, " Effects of dietary fiber on the ideal standardized ileal digestible threonine:lysine ratio for twenty-five to fifty kilogram growing gilts ," was co-authored by John Mathai of Illinois, John Htoo of Evonik Nutrition & Care GmbH, John Thomson of Evonik Degussa Corporation in Kennesaw, Georgia, and Kevin Touchette of Ajinomoto Heartland Inc. (thepigsite.com)
Dehydrogenase2
- Threonine is metabolized in two ways: In many animals it is converted to pyruvate via threonine dehydrogenase. (wikipedia.org)
- It is converted to pyruvate via Threonine Dehydrogenase. (bionity.com)
Deficiency include2
- Symptoms of a Threonine deficiency include emotional agitation, mental health deterioration, decreased digestion, intestinal malfunctions, increased liver fat, deterioration of nutrient absorption, and decreased protein uptake. (herbalremedies.com)
- The most common signs of an L-threonine deficiency include a fatty liver, digestion difficulties and emotional agitation. (xtend-life.com)
Cottage cheese1
- Dairy products also contain significant levels of L-threonine, especially cottage cheese. (xtend-life.com)
Racemic2
- Racemic threonine can be prepared from crotonic acid by alpha-functionalization using mercury(II) acetate. (wikipedia.org)
- This procedure yields a racemic mixture of threonine, meaning that it produces both D-threonine and L-threonine. (xtend-life.com)
Centers2
- With two chiral centers, threonine can exist in four possible stereoisomers, or two possible diastereomers (not mirror images) of L -threonine. (newworldencyclopedia.org)
- The two stereogenic centers in the threonine moiety were both established by alkylation of Evans' chiral N -acyloxazolidinone enolates. (diva-portal.org)
Bacterial1
- The method comprises a step of adding an alcohol substance into a threonine mother liquid solution obtained in an extraction process of threonine mother liquid so as to reduce the solubility and separate out threonine, and a compound microbial bacterial agent is added into other impurities to reach the emission standard. (google.com)
Definition1
- Threonine is important to be familiar with in biology and chemistry, and this quiz/worksheet will help you test your understanding of its definition and related components. (study.com)
Enzyme that catalyzes1
- In enzymology, a threonine aldolase (EC 4.1.2.5) is an enzyme that catalyzes the chemical reaction L-threonine ⇌ {\displaystyle \rightleftharpoons } glycine + acetaldehyde Hence, this enzyme has one substrate, L-threonine, and two products, glycine and acetaldehyde. (wikipedia.org)
Aspartic acid1
- Aspartic acid can then be reduced to yield L-threonine. (xtend-life.com)
