A sulfur-containing essential L-amino acid that is important in many body functions.
Reductases that catalyze the reaction of peptide-L-methionine -S-oxide + thioredoxin to produce peptide-L-methionine + thioredoxin disulfide + H(2)O.
An enzyme that catalyzes the synthesis of S-adenosylmethionine from methionine and ATP. EC 2.5.1.6.
An enzyme that catalyzes the formation of methionine by transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine. It requires a cobamide coenzyme. The enzyme can act on mono- or triglutamate derivatives. EC 2.1.1.13.
Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
Aminopeptidases that remove METHIONINE from the amino-terminus of a peptide chain, such as the initiator METHIONINE found on nascent peptide chains.
A thiol-containing amino acid formed by a demethylation of METHIONINE.
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.
One of the endogenous pentapeptides with morphine-like activity. It differs from LEU-ENKEPHALIN by the amino acid METHIONINE in position 5. Its first four amino acid sequence is identical to the tetrapeptide sequence at the N-terminal of BETA-ENDORPHIN.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
2-Amino-4-(ethylthio)butyric acid. An antimetabolite and methionine antagonist that interferes with amino acid incorporation into proteins and with cellular ATP utilization. It also produces liver neoplasms.
A cobalt-containing coordination compound produced by intestinal micro-organisms and found also in soil and water. Higher plants do not concentrate vitamin B 12 from the soil and so are a poor source of the substance as compared with animal tissues. INTRINSIC FACTOR is important for the assimilation of vitamin B 12.
An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
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.
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.
A ZINC metalloenzyme that catalyzes the transfer of a methyl group from BETAINE to HOMOCYSTEINE to produce dimethylglycine and METHIONINE, respectively. This enzyme is a member of a family of ZINC-dependent METHYLTRANSFERASES that use THIOLS or selenols as methyl acceptors.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
Nucleosides in which the base moiety is substituted with one or more sulfur atoms.
A multifunctional pyridoxal phosphate enzyme. In the second stage of cysteine biosynthesis it catalyzes the reaction of homocysteine with serine to form cystathionine with the elimination of water. Deficiency of this enzyme leads to HYPERHOMOCYSTEINEMIA and HOMOCYSTINURIA. EC 4.2.1.22.
Unstable isotopes of sulfur that decay or disintegrate spontaneously emitting radiation. S 29-31, 35, 37, and 38 are radioactive sulfur isotopes.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)
A member of the vitamin B family that stimulates the hematopoietic system. It is present in the liver and kidney and is found in mushrooms, spinach, yeast, green leaves, and grasses (POACEAE). Folic acid is used in the treatment and prevention of folate deficiencies and megaloblastic anemia.
An enzyme that catalyzes the METHYLATION of GLYCINE using S-ADENOSYLMETHIONINE to form SARCOSINE with the concomitant production of S-ADENOSYLHOMOCYSTEINE.
An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to METHIONINE, however it does not contain SULFUR.
Diagnostic aid in pancreas function determination.
The rate dynamics in chemical or physical systems.
A vitamin found in green vegetables. It is used in the treatment of peptic ulcers, colitis, and gastritis and has an effect on secretory, acid-forming, and enzymatic functions of the intestinal tract.
A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Compounds based on 5,6,7,8-tetrahydrofolate.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Autosomal recessive inborn error of methionine metabolism usually caused by a deficiency of CYSTATHIONINE BETA-SYNTHASE and associated with elevations of homocysteine in plasma and urine. Clinical features include a tall slender habitus, SCOLIOSIS, arachnodactyly, MUSCLE WEAKNESS, genu varus, thin blond hair, malar flush, lens dislocations, an increased incidence of MENTAL RETARDATION, and a tendency to develop fibrosis of arteries, frequently complicated by CEREBROVASCULAR ACCIDENTS and MYOCARDIAL INFARCTION. (From Adams et al., Principles of Neurology, 6th ed, p979)
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.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341)
Condition in which the plasma levels of homocysteine and related metabolites are elevated (>13.9 µmol/l). Hyperhomocysteinemia can be familial or acquired. Development of the acquired hyperhomocysteinemia is mostly associated with vitamins B and/or folate deficiency (e.g., PERNICIOUS ANEMIA, vitamin malabsorption). Familial hyperhomocysteinemia often results in a more severe elevation of total homocysteine and excretion into the urine, resulting in HOMOCYSTINURIA. Hyperhomocysteinemia is a risk factor for cardiovascular and neurodegenerative diseases, osteoporotic fractures and complications during pregnancy.
Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.
A condition produced by a deficiency of CHOLINE in animals. Choline is known as a lipotropic agent because it has been shown to promote the transport of excess fat from the liver under certain conditions in laboratory animals. Combined deficiency of choline (included in the B vitamin complex) and all other methyl group donors causes liver cirrhosis in some animals. Unlike compounds normally considered as vitamins, choline does not serve as a cofactor in enzymatic reactions. (From Saunders Dictionary & Encyclopedia of Laboratory Medicine and Technology, 1984)
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
The amounts of various substances in food needed by an organism to sustain healthy life.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.
A basic constituent of lecithin that is found in many plants and animal organs. It is important as a precursor of acetylcholine, as a methyl donor in various metabolic processes, and in lipid metabolism.
Regular course of eating and drinking adopted by a person or animal.
The sum of the weight of all the atoms in a molecule.
An essential branched-chain amino acid important for hemoglobin formation.
Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.
Organic compounds that have the general formula R-SO-R. They are obtained by oxidation of mercaptans (analogous to the ketones). (From Hackh's Chemical Dictionary, 4th ed)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).
Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.
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.
Stable sulfur atoms that have the same atomic number as the element sulfur, but differ in atomic weight. S-33, 34, and 36 are stable sulfur isotopes.
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.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
An essential amino acid. It is often added to animal feed.
Inorganic or organic compounds that contain sulfur as an integral part of the molecule.
A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.
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.
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.
An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.
An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.
A flavoprotein amine oxidoreductase that catalyzes the reversible conversion of 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. This enzyme was formerly classified as EC 1.1.1.171.
Proteins found in any species of bacterium.
The first enzyme in the METHIONINE biosynthetic pathway, this enzyme catalyzes the succinylation reaction of L-homoserine to O-succinyl-L-homoserine and COENZYME A using succinyl-CoA.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
Adenosine molecules which can be substituted in any position, but are lacking one hydroxyl group in the ribose part of the molecule.
Measurement of this acid in the urine after oral administration of histidine provides the basis for the diagnostic test of folic acid deficiency and of megaloblastic anemia of pregnancy.
A conditionally essential nutrient, important during mammalian development. It is present in milk but is isolated mostly from ox bile and strongly conjugates bile acids.
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.
Sulfur compounds in which the sulfur atom is attached to three organic radicals and an electronegative element or radical.
VITAMIN B 6 refers to several PICOLINES (especially PYRIDOXINE; PYRIDOXAL; & PYRIDOXAMINE) that are efficiently converted by the body to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, and aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into PYRIDOXAMINE phosphate. Although pyridoxine and Vitamin B 6 are still frequently used as synonyms, especially by medical researchers, this practice is erroneous and sometimes misleading (EE Snell; Ann NY Acad Sci, vol 585 pg 1, 1990). Most of vitamin B6 is eventually degraded to PYRIDOXIC ACID and excreted in the urine.
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.
Proteins prepared by recombinant DNA technology.
Inorganic salts of sulfuric acid.
A nutritional condition produced by a deficiency of VITAMIN B 12 in the diet, characterized by megaloblastic anemia. Since vitamin B 12 is not present in plants, humans have obtained their supply from animal products, from multivitamin supplements in the form of pills, and as additives to food preparations. A wide variety of neuropsychiatric abnormalities is also seen in vitamin B 12 deficiency and appears to be due to an undefined defect involving myelin synthesis. (From Cecil Textbook of Medicine, 19th ed, p848)
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A nutritional condition produced by a deficiency of FOLIC ACID in the diet. Many plant and animal tissues contain folic acid, abundant in green leafy vegetables, yeast, liver, and mushrooms but destroyed by long-term cooking. Alcohol interferes with its intermediate metabolism and absorption. Folic acid deficiency may develop in long-term anticonvulsant therapy or with use of oral contraceptives. This deficiency causes anemia, macrocytic anemia, and megaloblastic anemia. It is indistinguishable from vitamin B 12 deficiency in peripheral blood and bone marrow findings, but the neurologic lesions seen in B 12 deficiency do not occur. (Merck Manual, 16th ed)
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 characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
An oxyacid of chlorine (HClO) containing monovalent chlorine that acts as an oxidizing or reducing agent.
Compounds containing the -SH radical.
A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)
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.
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.
An FAD-dependent oxidoreductase found primarily in BACTERIA. It is specific for the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. This enzyme was formerly listed as EC 1.1.1.68 and 1.1.99.15.
Nitrogen oxide (N2O). A colorless, odorless gas that is used as an anesthetic and analgesic. High concentrations cause a narcotic effect and may replace oxygen, causing death by asphyxia. It is also used as a food aerosol in the preparation of whipping cream.
Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.
An essential amino acid that is required for the production of HISTAMINE.

Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. (1/5837)

Recent results have shown that the ability of farnesyltransferase inhibitors (FTIs) to inhibit malignant cell transformation and Ras prenylation can be separated. We proposed previously that farnesylated Rho proteins are important targets for alternation by FTIs, based on studies of RhoB (the FTI-Rho hypothesis). Cells treated with FTIs exhibit a loss of farnesylated RhoB but a gain of geranylgeranylated RhoB (RhoB-GG), which is associated with loss of growth-promoting activity. In this study, we tested whether the gain of RhoB-GG elicited by FTI treatment was sufficient to mediate FTI-induced cell growth inhibition. In support of this hypothesis, when expressed in Ras-transformed cells RhoB-GG induced phenotypic reversion, cell growth inhibition, and activation of the cell cycle kinase inhibitor p21WAF1. RhoB-GG did not affect the phenotype or growth of normal cells. These effects were similar to FTI treatment insofar as they were all induced in transformed cells but not in normal cells. RhoB-GG did not promote anoikis of Ras-transformed cells, implying that this response to FTIs involves loss-of-function effects. Our findings corroborate the FTI-Rho hypothesis and demonstrate that gain-of-function effects on Rho are part of the drug mechanism. Gain of RhoB-GG may explain how FTIs inhibit the growth of human tumor cells that lack Ras mutations.  (+info)

Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica. (2/5837)

Entamoeba histolytica is a microaerophilic protozoan parasite in which neither mitochondria nor mitochondrion-derived organelles have been previously observed. Recently, a segment of an E. histolytica gene was identified that encoded a protein similar to the mitochondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins after passage through organellar membranes. The possible function and localization of the amebic Hsp60 were explored here. Like Hsp60 of mitochondria, amebic Hsp60 RNA and protein were both strongly induced by incubating parasites at 42 degreesC. 5' and 3' rapid amplifications of cDNA ends were used to obtain the entire E. histolytica hsp60 coding region, which predicted a 536-amino-acid Hsp60. The E. histolytica hsp60 gene protected from heat shock Escherichia coli groEL mutants, demonstrating the chaperonin function of the amebic Hsp60. The E. histolytica Hsp60, which lacked characteristic carboxy-terminal Gly-Met repeats, had a 21-amino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo. This presequence was necessary to target Hsp60 to one (and occasionally two or three) short, cylindrical organelle(s). In contrast, amebic alcohol dehydrogenase 1 and ferredoxin, which are bacteria-like enzymes, were diffusely distributed throughout the cytosol. We suggest that the Hsp60-associated, mitochondrion-derived organelle identified here be named "crypton," as its structure was previously hidden and its function is still cryptic.  (+info)

The biosynthesis of transfer RNA in insects. II. Isolation of transfer RNA precursors from the posterior silk gland of Bombyx mori. (3/5837)

The occurrence of precursors to tRNA in the post-polysomal fraction of the posterior silk gland of Bombyx mori was demonstrated by pulse-chase labeling and DNA-RNA hybridization competition experiments. These precursors had molecular sizes ranging from 4S to 5S on polyacrylamide gel electrophoresis. Analysis of the incorporation of the methyl group from [methyl-14C]methionine revealed that a radioactive peak on polyacrylamide gel appeared in the 4.5S region during brief labeling. This suggested that some methylation occurred at the 4.5S precursor step.  (+info)

Purification and characterization of initiation factor IF-E2 from rabbit reticulocytes. (4/5837)

Initiation factor IF-E2 was isolated from rabbit reticulocytes and purified 120-fold to near homogeneity by ammonium sulfate fractionation, column chromatography on DEAE-cellulose and phosphocellulose, and, when suitable, by sucrose density gradient centrifugation. The factor is a complex protein containing three nonidentical polypeptides of molecular weight 57,000, 52,000, and 36,000. It behaves as a complex throughout its purification and during polyacrylamide gel electrophoresis in nondenaturing buffer but its thress components are readily separated by electrophoresis in denaturing buffers. None of its components corresponds to any of the polypeptides of the other initiation factors or to any proteins of ribosomes washed in buffers containing a high salf concentration. A stoichiometric ratio of 1:1:1 was determined for the three polypeptides; based on the assumption of one copy each per complex, the calculated factor molecular weight is 145,000, a value in agreement with the measured value of 160,000. Initiation factor IF-E2 was radioactively labeled in vitro by reductive alkylation or by phosphorylation with a protein kinase also isolated from rabbit reticulocytes. Neither procedure causes a measurable change in the ability of the factor to form a ternary complex with GTP and the initiator methionyl-tRNA. 5'-Guanylyl-methylenediphosphonate may substitute for GTP, but only at relatively high concentrations. The binding of labeled initiation factor IF-E2 and methionyl-tRNA to the 40 S ribosomal subunit was studied by sucrose density gradient centrifugation. Appreciable binding of the factor is seen only when all three components of the ternary complex are included in the reaction mixture. The binding of either the factor or methionyl-tRNA was not stimulated by the addition of globin messenger RNA and initiation factor IF-E3. It was shown that all three polypeptide components of initiation factor IF-E2 are bound to these nascent initiation complexes.  (+info)

Endothelial dysfunction by acute hyperhomocyst(e)inaemia: restoration by folic acid. (5/5837)

Recent evidence demonstrates that hyperhomocyst(e)inaemia is a novel risk factor for cardiovascular diseases. In patients with chronic hyperhomocyst(e)inaemia, endothelial function is impaired. However, whether hyperhomocyst(e)inaemia per se is a cause or an epiphenomenon of endothelial dysfunction remains unknown. In this study, we examined the effects of methionine-induced acute hyperhomocyst(e)inaemia on human endothelial function. In healthy volunteers we administered methionine (0.1 g/kg body weight, per os), a substrate of homocyst(e)ine, with or without folic acid (20 mg, per os) and examined flow-mediated vasodilatation of the brachial artery by high-resolution ultrasonography as a non-invasive measure of endothelial function. We also measured plasma levels of homocyst(e)ine before and 3, 8 and 24 h after methionine loading. Methionine administration increased plasma levels of homocyst(e)ine by four times the basal level at 8 h (P<0.0001, ANOVA). The plasma levels returned to baseline at 24 h. Flow-mediated vasodilatation was significantly decreased to half of the baseline value at 8 h and returned to baseline at 24 h (P<0.0001, ANOVA), whereas endothelium-independent vasodilatation by glyceryl trinitrate was not affected by the methionine loading. Co-administration of folic acid did not attenuate methionine-induced hyperhomocyst(e)inaemia but completely prevented endothelial dysfunction. Our results suggest that in humans a methionine-rich diet may acutely impair endothelial function, which can be prevented by folic acid supplementation.  (+info)

cAMP inhibits translation by inducing Ca2+/calmodulin-independent elongation factor 2 kinase activity in IPC-81 cells. (6/5837)

Treatment of IPC-81 cells led to inhibition of protein synthesis, which was accompanied by an increase in the average size of polysomes and a decreased rate of elongation, indicating that it involved inhibition of peptide chain elongation. This inhibition was also associated with increased phosphorylation of elongation factor eEF2 (which inhibits its activity) and enhanced Ca2+/calmodulin-independent activity of eEF2 kinase. Previous work has shown that phosphorylation of eEF2 kinase by cAMP-dependent protein kinase (cAPK) in vitro induces such activator-independent activity, and the present data show that such a mechanism can occur in intact cells to link physiological levels of cAPK activation with inhibition of protein synthesis.  (+info)

Insulin and TSH promote growth in size of PC Cl3 rat thyroid cells, possibly via a pathway different from DNA synthesis: comparison with FRTL-5 cells. (7/5837)

In the rat thyroid cell lines PC Cl3, FRTL- 5 and WRT, proliferation is mainly regulated by insulin or IGF, and TSH. However, the mechanism regulating cell mass doubling prior to division is still unknown. Our laboratory has shown that in dog thyroid cells insulin promotes growth in size while TSH in the presence of insulin triggers DNA replication. In the absence of insulin, TSH has no effect on cell growth. In this report we investigated insulin action on both cell mass and DNA synthesis and its modulation by TSH and insulin in PC Cl3 and FRTL-5 cells. In PC Cl3 cells, insulin activated not only DNA synthesis but also protein synthesis and accumulation. Although TSH potentiated the stimulation of DNA synthesis induced by insulin, enhancement of protein synthesis by both agents was additive. All TSH effects were reproduced by forskolin. Similar effects were also obtained in FRTL-5 cells. This suggests that insulin and TSH, via cAMP, modulate both growth in size and DNA replication in these cell lines. Lovastatin, which blocks 3-hydroxy-3-methylglutaryl coenzyme A reductase, decreased the induction of DNA synthesis, but not of protein synthesis induced by insulin or TSH in PC Cl3 cells. In FRTL-5 cells, lovastatin reduced protein and DNA synthesis stimulated by insulin but not TSH-induced protein synthesis. Taking these data together, we propose that insulin and/or TSH both modulate cell mass doubling and DNA synthesis in these cell lines, presumably via different pathways, and that there are at least two pathways which regulate growth in size in FRTL-5 thyroid cells: one triggered by insulin, which is lovastatin sensitive, and the other activated by TSH, which is not sensitive to lovastatin.  (+info)

Is human thioredoxin monomeric or dimeric? (8/5837)

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)

Treatment for homocystinuria typically involves a combination of dietary modifications and nutritional supplements to manage the symptoms and prevent long-term complications. In some cases, medication may also be prescribed to reduce the levels of homocysteine in the blood.

The prognosis for individuals with homocystinuria varies depending on the severity of the condition and the effectiveness of treatment. Some individuals with mild forms of the disorder may experience few or no symptoms, while those with more severe forms may have significant developmental delays and disabilities. With appropriate management, however, many individuals with homocystinuria can lead active and fulfilling lives.

There are several factors that can contribute to hyperhomocysteinemia, including:

1. Genetic mutations: Some individuals may have genetic mutations that affect the enzymes involved in homocysteine metabolism, leading to elevated levels of homocysteine.
2. Vitamin deficiencies: Deficiencies in vitamins B6, B12, and folate can interfere with the metabolism of homocysteine, leading to elevated levels.
3. Kidney disease: The kidneys play a critical role in removing homocysteine from the body. Any damage to the kidneys or impairment in their function can lead to hyperhomocysteinemia.
4. Other medical conditions: Certain medical conditions, such as thyroid disorders and autoimmune diseases, can also contribute to hyperhomocysteinemia.

Elevated levels of homocysteine have been linked to several health problems, including:

1. Cardiovascular disease: High levels of homocysteine have been associated with an increased risk of heart disease and stroke.
2. Blood clots: Homocysteine can interfere with the normal blood clotting process, leading to an increased risk of blood clots and deep vein thrombosis.
3. Bone loss: Elevated levels of homocysteine have been linked to bone loss and an increased risk of osteoporosis.
4. Cognitive decline: Some studies suggest that high levels of homocysteine may be associated with cognitive decline and an increased risk of dementia.

Treatment for hyperhomocysteinemia typically involves addressing any underlying medical conditions, such as kidney disease or thyroid disorders, and making dietary changes to increase the intake of vitamin B6, folate, and other nutrients that help regulate homocysteine levels. In some cases, medications may be prescribed to lower homocysteine levels. Regular monitoring of homocysteine levels can help healthcare providers track the effectiveness of treatment and make any necessary adjustments.

Choline deficiency can cause a range of health problems, including:

1. Fatty liver disease: Choline is important for the transport of fat from the liver to other parts of the body, and a deficiency can lead to fat accumulation in the liver, which can cause fatty liver disease.
2. Brain function problems: Choline is crucial for the synthesis of the neurotransmitter acetylcholine, which is involved in memory, attention, and cognitive function. A deficiency can lead to problems with brain development and function.
3. Mood disorders: Low choline levels have been linked to an increased risk of depression and anxiety.
4. Insulin resistance: Choline helps regulate glucose metabolism, and a deficiency can lead to insulin resistance, which can increase the risk of developing type 2 diabetes.
5. Skin and eye problems: Choline is important for the health of the skin and eyes, and a deficiency can lead to conditions such as acne, eczema, and dry eye syndrome.
6. Reproductive problems: Choline is important for fertility and fetal development during pregnancy, and a deficiency can increase the risk of miscarriage, birth defects, and preterm labor.

If you suspect that you or your child may have a choline deficiency, it's important to speak with a healthcare provider who can perform tests to determine if low choline levels are causing any health problems. Treatment for choline deficiency typically involves dietary changes and supplementation with choline-rich foods or supplements.

Causes:

* Dietary deficiency due to a lack of animal products in the diet
* Malabsorption due to gastrointestinal disorders such as Crohn's disease or celiac disease
* Pernicious anemia, an autoimmune condition that affects the absorption of vitamin B12 in the gut.
* Surgical removal of part of the small intestine
* Certain medications such as metformin and proton pump inhibitors

Symptoms:

* Fatigue, weakness, and shortness of breath
* Pale skin and mouth sores
* Difficulty walking or balance problems
* Numbness or tingling sensations in the hands and feet
* Memory loss and depression
* Poor appetite and weight loss

Diagnosis:

* Blood tests to measure vitamin B12 levels and other related markers such as homocysteine
* Physical examination and medical history to identify risk factors or signs of deficiency

Treatment:

* Dietary changes to include more animal products such as meat, fish, eggs, and dairy products.
* Vitamin B12 supplements in the form of tablets, lozenges, or injections.
* Addressing underlying conditions that may be contributing to the deficiency such as gastrointestinal disorders.

Prevention:

* Consuming animal products as part of a balanced diet
* Avoiding medications that can interfere with vitamin B12 absorption.

1. Anemia: Folic acid plays a critical role in the production of red blood cells, so a deficiency can lead to anemia, which can cause fatigue, weakness, and shortness of breath.
2. Birth defects: Folic acid is crucial for fetal development during pregnancy, and a deficiency can increase the risk of birth defects such as spina bifida and cleft palate.
3. Heart disease: Folic acid helps to regulate homocysteine levels in the blood, which are associated with an increased risk of heart disease and stroke.
4. Neurological problems: Folic acid is important for the health of the nervous system, and a deficiency can lead to neurological problems such as cognitive impairment, mood disturbances, and seizures.
5. Poor wound healing: Folic acid is necessary for the production of collagen, which is important for wound healing. A deficiency can lead to slow or poor wound healing.
6. Increased risk of cancer: Some studies suggest that a folic acid deficiency may increase the risk of certain types of cancer, such as colon cancer.
7. Hair loss: Folic acid is important for hair growth, and a deficiency can lead to hair loss.
8. Skin problems: Folic acid is important for skin health, and a deficiency can lead to skin problems such as dry, flaky skin and mouth sores.
9. Mood changes: Folic acid plays a role in the production of neurotransmitters, which are chemicals that regulate mood. A deficiency can lead to mood changes such as depression and anxiety.
10. Fatigue: Folic acid is important for energy metabolism, and a deficiency can lead to fatigue and weakness.

Folic acid deficiency can be caused by a number of factors, including:

1. Poor diet: A diet that is low in folate-rich foods can lead to a deficiency.
2. Malabsorption: Certain medical conditions such as celiac disease and Crohn's disease can lead to malabsorption of folic acid.
3. Pregnancy and lactation: Women who are pregnant or breastfeeding have a higher need for folic acid, and may be at risk for deficiency if they do not consume enough.
4. Alcoholism: Heavy alcohol consumption can interfere with the absorption of folic acid.
5. Certain medications: Some medications, such as antacids and proton pump inhibitors, can interfere with the absorption of folic acid.

To diagnose a folic acid deficiency, a healthcare provider may perform a physical exam, take a medical history, and order blood tests to measure folic acid levels. Treatment for a folic acid deficiency typically involves dietary changes and supplements. Dietary changes may include consuming more folate-rich foods, such as leafy green vegetables, legumes, and whole grains. Supplements may include folic acid tablets or liquid supplements. In severe cases of deficiency, injections of folic acid may be necessary. It is important to seek medical attention if you suspect a folic acid deficiency, as untreated deficiencies can lead to serious health problems.

"Methionine". WebMD. Cavuoto P, Fenech MF (2012). "A review of methionine dependency and the role of methionine restriction in ... which must ingest methionine or methionine-containing proteins. In plants and microorganisms, methionine biosynthesis belongs ... The methionine-derivative S-adenosyl methionine (SAM-e) is a cofactor that serves mainly as a methyl donor. SAM-e is composed ... DL-Methionine is sometimes given as a supplement to dogs; It helps reduce the chances of kidney stones in dogs. Methionine is ...
Methionine(protein)+ H2O2→ Methionine Sulfoxide(protein)+ H2O Methionine Sulfoxide(protein)+ NADPH+H+→ Methionine(protein)+ ... Oxidation of methionine results in a mixture of the two diastereomers methionine-S-sulfoxide and methionine-R-sulfoxide, which ... Oxidation of the sulfur of methionine results in methionine sulfoxide or methionine sulfone. The sulfur-containing amino acids ... Methionine sulfoxide (MetO), the oxidized form of the amino acid methionine (Met), increases with age in body tissues, which is ...
D-methionine Hence, this enzyme has one substrate, L-methionine, and one product, D-methionine. This enzyme belongs to the ... In enzymology, a methionine racemase (EC 5.1.1.2) is an enzyme that catalyzes the chemical reaction L-methionine ⇌ {\ ... The systematic name of this enzyme class is methionine racemase. It employs one cofactor, pyridoxal phosphate. McElroy WD, ...
... (EC 2.6.1.88, methionine-oxo-acid transaminase) is an enzyme with systematic name L-methionine:2-oxo- ... Methionine+transaminase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.6.1). ... Heilbronn J, Wilson J, Berger BJ (March 1999). "Tyrosine aminotransferase catalyzes the final step of methionine recycling in ... This enzyme catalyses the following chemical reaction L-methionine + 2-oxo carboxylate ⇌ {\displaystyle \rightleftharpoons } 2- ...
... is composed of two different diastereomers, which are L-S-Methionine sulfoximine and L-R-Methionine ... Methionine sulfoximine (MSO) is an irreversible glutamine synthetase inhibitor. It is the sulfoximine derivative of methionine ... Rowe, WB; Meister, A (June 1970). "Identification of L-methionine-S-sulfoximine as the convulsant isomer of methionine ... Since methionine sulfoximine inhibits glutamate production in the brain, it prevents excitotoxicity. Thus, increasing the ...
The enzyme methionine decarboxylase (EC 4.1.1.57) catalyzes the chemical reaction L-methionine ⇌ {\displaystyle \ ... Other names in common use include L-methionine decarboxylase and L-methionine carboxy-lyase. Hagion H, Nakayama K (1968). " ... L-Methionine decarboxylase produced by Streptomyces strain". Agric. Biol. Chem. 32: 727-733. doi:10.1080/00021369.1968.10859127 ... The systematic name of this enzyme class is L-methionine carboxy-lyase (3-methylthiopropyl amine-forming). ...
... also known as MS, MeSe, MTR is responsible for the regeneration of methionine from homocysteine. In humans ... Methionine synthase catalyzes the final step in the regeneration of methionine (Met) from homocysteine (Hcy). Both the ... As a secondary effect, methionine synthase also serves to maintain low levels of Hcy and, because methionine synthase is one of ... Wolthers KR, Scrutton NS (June 2007). "Protein interactions in the human methionine synthase-methionine synthase reductase ...
... methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine The 3 products of this enzyme are methionine ... Methionine synthase] reductase, or Methionine synthase reductase, encoded by the gene MTRR, is an enzyme that is responsible ... Other names in common use include methionine synthase cob(II)alamin reductase (methylating), methionine synthase reductase, [ ... and S-adenosyl-L-methionine. Physiologically speaking, one crucial enzyme participated in the folate cycle is methionine ...
a 63-68-3 EINECS for L-Methionine ^a CID 876 from PubChem ^a CID 6137 from PubChem (PubChem ID (CID) not in Wikidata, Chemical ...
In enzymology, a methionine-tRNA ligase (EC 6.1.1.10) is an enzyme that catalyzes the chemical reaction ATP + L-methionine + ... methionine translase, and MetRS. This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid ... During oxidative stress, methionine-tRNA ligase might be phosphorylated, which results in promiscuity of this enzyme, where it ... This in turn leads to substitution of amino acids in proteins with methionine, which helps relieve oxidative stress in the cell ...
Other names in common use include S-adenosyl methionine:methionine methyl transferase, methionine methyltransferase, S- ... S-methyl-L-methionine Thus, the two substrates of this enzyme are S-adenosyl methionine and L-methionine, whereas its two ... Karr D, Tweto J, Albersheim P (1967). "S-adenosyl methionine: methionine methyl transferase from wheat germ". Arch. Biochem. ... The systematic name of this enzyme class is S-adenosyl-L-methionine:L-methionine S-methyltransferase. ...
... is a photo-reactive amino acid derivative of L-methionine that was synthetically formed in 2005. Protein are ... Photo-methionine can be used to label recombinant proteins in Escherichia coli cells; though methionine in general is a rare ... which led to the synthesis of L-photo-methionine and in that same study, L-photo-leucine. Racemic Photo-Methionine is ... Once the cytochrome b5 complex had photo-methionine incorporated (meaning photo-met was substituted in place of methionine and ...
... consists of the adenosyl cation attached to the sulfur of methionine. It is synthesized from ATP and ... It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by ... S-adenosyl-L-methionine The sulfonium functional group present in S-adenosyl methionine is the center of its peculiar ... S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved ...
... methionine lyase, methioninase, methionine dethiomethylase, L-methionine γ-lyase, and L-methionine methanethiol-lyase ( ... In enzymology, a methionine gamma-lyase (EC 4.4.1.11) is an enzyme that catalyzes the chemical reaction L-methionine + H2O ⇌ {\ ... The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing ... Therefore, methionine depletion arises as a relevant therapeutical approach to treat cancer. For that reason, MGL has been ...
... may refer to: Methionine-S-oxide reductase L-methionine (S)-S-oxide reductase This set index ...
In enzymology, a methionine-glyoxylate transaminase (EC 2.6.1.73) is an enzyme that catalyzes the chemical reaction L- ... Other names in common use include methionine-glyoxylate aminotransferase, and MGAT. Glover JR, Chapple CC, Rothwell S, Tober I ... The systematic name of this enzyme class is L-methionine:glyoxylate aminotransferase. ... the two substrates of this enzyme are L-methionine and glyoxylate, whereas its two products are 4-methylthio-2-oxobutanoate and ...
... (EC 1.8.4.5, methyl sulfoxide reductase I and II, acetylmethionine sulfoxide reductase, methionine ... Ejiri SI, Weissbach H, Brot N (July 1979). "Reduction of methionine sulfoxide to methionine by Escherichia coli". Journal of ... Methionine-S-oxide+reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.8.4) ... Black, S.; Harte, E.M.; Hudson, B.; Wartofsky, L. (1960). "A specific enzymatic reduction of L-(-)methionine sulfoxide and a ...
Mepron is the brand name for a time-released, rumen-protected DL-Methionine capsule for dairy cattle. It is a registered ... Dairy-herd milk production may be limited by the amino acid methionine; therefore, the amino acid is included in cattle rations ... Further studies are needed to determine if cows may respond to lysine supply once the methionine requirements are met." Mepron ... According to a 2006 study, results "suggest that RPM [rumen-protected methionine] may be needed to improve milk production in ...
... may refer to: Protein-methionine-S-oxide reductase Peptide-methionine (S)-S-oxide ...
Other names in common use include D-methionine transaminase, and D-methionine aminotransferase. This enzyme participates in d- ... In enzymology, a D-methionine-pyruvate transaminase (EC 2.6.1.41) is an enzyme that catalyzes the chemical reaction D- ... 4-methylmercapto-2-oxobutyric acid: an intermediate in the formation from methionine". Biochem. J. 115 (4): 653-61. PMC 1185190 ... The systematic name of this enzyme class is D-methionine:pyruvate aminotransferase. ...
S-methyl-methionine Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c methionine, whereas its ... The systematic name of this enzyme class is S-adenosyl-L-methionine:[cytochrome c]-methionine S-methyltransferase. Farooqui JZ ... is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + [cytochrome c]-methionine ⇌ {\displaystyle \ ... In enzymology, a [cytochrome-c]-methionine S-methyltransferase (EC 2.1.1.123) ...
... methionine S-oxide reductase (ambiguous), selenoprotein R, methionine S-oxide reductase (R-form oxidizing), methionine ... The systematic name of this enzyme class is peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide- ... peptide-L-methionine (R)-S-oxide + thioredoxin The 3 substrates of this enzyme are peptide-L-methionine, thioredoxin disulfide ... "Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine". J. ...
... may refer to: Methionine-S-oxide reductase L-methionine (S)-S-oxide ... reductase This disambiguation page lists articles associated with the title L-methionine:oxidized-thioredoxin S-oxidoreductase ...
The systematic name of this enzyme class is L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (R)-S-oxide- ... This enzyme participates in methionine metabolism. Etienne F, Spector D, Brot N, Weissbach H (2003). "A methionine sulfoxide ... L-methionine (R)-S-oxide + thioredoxin The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H2O, ... In enzymology, a L-methionine (R)-S-oxide reductase (EC 1.8.4.14) is an enzyme that catalyzes the chemical reaction L- ...
L-methionine:oxidized-thioredoxin S-oxidoreductase, methionine-S-oxide reductase, and free-methionine (S)-S-oxide reductase. ... Ejiri SI, Weissbach H, Brot N (1979). "Reduction of methionine sulfoxide to methionine by Escherichia coli". J. Bacteriol. 139 ... L-methionine (S)-S-oxide + thioredoxin The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H2O, ... In enzymology, a L-methionine (S)-S-oxide reductase (EC 1.8.4.13) is an enzyme that catalyzes the chemical reaction L- ...
... (EC 1.8.4.11, MsrA, methionine sulphoxide reductase A, methionine S-oxide reductase (S ... oxidizing), methionine sulfoxide reductase A, peptide methionine sulfoxide reductase, formerly protein-methionine-S-oxide ... L-methionine (S)-S-oxide-forming). This enzyme catalyses the following chemical reaction (1) peptide-L-methionine + thioredoxin ... L-methionine + thioredoxin disulfide + H2O ⇌ {\displaystyle \rightleftharpoons } L-methionine (S)-S-oxide + thioredoxin The ...
... may refer to: 5-hydroxyfuranocoumarin 5-O-methyltransferase Bergaptol O- ...
... may refer to: 8-hydroxyfuranocoumarin 8-O-methyltransferase Xanthotoxol ...
... may refer to: Kaempferol 4'-O-methyltransferase Flavonoid 4'-O- ...
... may refer to: Sarcosine/dimethylglycine N-methyltransferase ... Dimethylglycine N-methyltransferase This disambiguation page lists articles associated with the title S-adenosyl-L-methionine:N ...
Description: Methionine MFN Duty Rate: Free. Previous Tariff (2930.30.60 - Thiuram mono-, di- or tetrasulfides, other than ... 1995 NY 807746 - The tariff classification of DL-Methionine (CAS No. 59-51-8) from China. ...
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Methionine in proteins, apart from its role in the initiation of translation, is assumed to play a simple structural role in ... Methionine in proteins: The Cinderella of the proteinogenic amino acids Protein Sci. 2019 Oct;28(10):1785-1796. doi: 10.1002/ ... Methionine in proteins, apart from its role in the initiation of translation, is assumed to play a simple structural role in ... Despite all these evidences, the role of methionine in protein structure and function is largely overlooked by most biochemists ...
Methionine Market is projected to reach USD 4.45 Billion by 2022. Report provides crucial industry insights that will help your ... The main types of methionine are L-Methionine, DL-Methionine, and Methionine Hydroxy Analog (MHA). Majorly, DL-methionine is ... 6.2 DL-Methionine. 6.3 Methionine Hydroxy Analogue (Mha). 6.4 L-Methionine. 7 Methionine Market, By Application (Page No. - 45) ... Methionine Market by Type (L-Methionine, MHA, Dl-Methionine), Application (Animal Feed, Food & Dietary Supplements, ...
L-Methionine is rich in sulfur, a must for healthy joint function. Our formulations are ideal for dry preparation food-based ... CapsuDar® Methionine 85. Specification. min. 85% l-methionine L- Methionine content: min 83%, max 88% ... L-Methionine is rich in sulfur, a must for healthy joint function. It also has the ability to combine with other chemicals in ... Methionine. An important partner.. This powerful amino acid works to detoxify heavy metals within the body while also ...
Methionine with 14 results, Browse our large selection of products and Save Big at VitaNet®, LLC ... L-Methionine Powder 100 gm SOURCE NATURALS SN0145 3.53 oz *. $ 23.75. 30% OFF MSRP $ 16.64 Add to cart and Save additional 14% ... Free-Form, L-Methionine, OptiZinc, Monomethionine, S-adenosyl-L-methionine, 400mg, Selenium, L-Selenomethionine, Tags Forums: ... SAMe (S-adenosyl-L-methionine) 200 mg SOURCE NATURALS SN1237 20 tabs *. $ 22.75. 30% OFF MSRP $ 15.93 Add to cart and Save ...
A Double-Blind, Randomized, Placebo-Controlled Clinical Trial of S-Adenosyl-l-Methionine (SAMe) Versus Escitalopram in Major ... Objective: To examine the comparative antidepressant efficacy of S-adenosyl-l-methionine (SAMe) and escitalopram in a placebo- ...
Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L - 1 kit is backordered and will ship as ... Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L ... Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L. ... Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L. ...
In our study we aimed assessing the correlation of metabolic information on 11C-methionine PET and biological data in patients ... Introduction: In our study we aimed assessing the correlation of metabolic information on 11C-methionine PET and biological ... Learning Objectives: To understand metabolic heterogeneity of primary brain tumors and the relevance of 11C-methionine PET in ... Patients underwent pre-surgical 11C-methionine PET performed according to standard procedure and in all cases semi-quantitative ...
... methionine), while a third low-protein high-methionine diet (LP-MET: 9% casein, 1.0% methionine) was employed as a positive ... of methionine appears to disrupt one-carbon metabolism at the level of homocysteine remethylation to methionine. This may place ... The Effect of Unbalanced Dietary Methionine fed to Pregnant Rats on Maternal and Fetal One-Carbon Metabolism. ... Pregnant Wistar rats were fed casein-based diets ad libitum varying in casein (18% or 9%) and methionine content (0.5% or 1.0 ...
We and others have previously demonstrated delayed Aβ aggregation as a consequence of oxidizing a single methionine residue at ... Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation. In: Neuroreport. 18(6), pp. 559-563. ISSN ... We and others have previously demonstrated delayed Aβ aggregation as a consequence of oxidizing a single methionine residue at ... We and others have previously demonstrated delayed Aβ aggregation as a consequence of oxidizing a single methionine residue at ...
抗氧化劑,屬水溶性物質,主要守護生物體細胞外與細胞間隙的組織液
Methionine cat-item-58. An essential amino acid for dogs and cats. ...
peptidyl-methionine oxidation. id: GO:0018159. name: peptidyl-methionine oxidation. namespace: biological_process. type: go. ... Description: The oxidation of peptidyl-L-methionine to peptidyl-L-methionine sulfone. ...
DL-Methionine - SDS French. Posted on February 7, 2022 at 5:21 pm by admin ...
Buy Methionine Poultry Feed Additives at best price. ... exporter and supplier of Methionine Poultry Feed Additives ... Methionine Poultry Feed Additives are prepared in our ultra-advanced production division making the best use of pioneering ... Methionine Poultry Feed Additives come in a preventative packaging that keeps impurities and contaminants at bay. ...
L-methionine & L-Cysteine. by Shopify API January 10, 2018. An essential amino acid and is a precursor of L-Cysteine and L- ...
Chemlyte solutions L-Methionine-S-methyl Sulfonium Chloride ... L-METHIONINE S-METHYLSULFONIUM CHLORIDE;_x000D_ DL-METHIONINE ... L-Methionine-S-methyl Sulfonium Chloride. For more information please contact us at [email protected] or Inquire with ...
Other sources of methionine are cheese, eggs, chicken, and beef.. Benefits of methionine. It is used for treating endometriosis ... Home » Methionine Benefits, Sources, Deficiency, Dosage. Methionine Benefits, Sources, Deficiency, Dosage. *. July 20, 2008. ... Excessive methionine intake, with an inadequate intake of folic acid, vitamin B6 and vitamin B12, may increase the rate of ... The daily dosage of methionine is about 12 mg per kilogram of body weight per day - which would translate to about 840 mg for a ...
OBJECTIVE: Previously, we demonstrated that lifelong methionine (Met) restriction (MR) increases lifespan, decreases the ... Tissue glutathione and cysteine levels in methionine-restricted rats. Sep 1, 2004 , Publications ...
... which is integral in the production of DL-methionine. ... "This investment is a building block of our global methionine ... "With this investment, Evonik is strengthening the European methionine network to safeguard the long-term supply of MMP to our ... From that facility, the company supplies its U.S. milk and dairy customers with Mepron - a special methionine formulation which ... "The move underscores our commitment to serving and expanding the global DL-methionine market and secures the best possible ...
... Add to DIY report I havent create reports, create a new report right ... HomeContent byte Hebang Biotech discloses methionine revenue in Q1-Q3 2022 ...
We further conducted a 16-week MR intervention (0.17% methionine, w/w) on APP/PS1 AD model mice. Although MR reduced Aß ... Effects of methionine intake on cognitive function in mild cognitive impairment patients and APP/PS1 Alzheimers Disease model ... Here we sought to investigate the neuroprotective effects of low methionine intake in mild cognitive impairment (MCI) patients ... As a dietary intervention, methionine restriction (MR) has been reported to increase longevity and improve metabolism disorders ...
In this study, we have designed three peptides from copper binding regions of CTR1 which are rich in histidine and methionine. ... Peptides Derived from Histidine and Methionine Rich Regions of Copper transporter 1 Exhibit Anti-angiogenic Property by ...
... you will learn more about the unique qualities of amino acids methionine, particularly its metabolic performance. ... How does methionine work efficiently by way of metabolism and are amino acids methionine unique in terms of supporting bodily ... Amino Acids Methionine and Metabolism. Methionine, as stated, cannot be manufactured in animal bodies. Alternatively, it should ... Among plants as well as microbes, methionine could be made through an ongoing process known as methionine biosynthesis. This ...
... find China methionine-powder factory, suppliers from Loyal Bio-Chemical Manufacture Co.,Ltd. ... Quality methionine-powder supplier on sales from methionine-powder manufacturer - ... Methionine. (11). Calcium Carbide. (10). Paraffin Wax. (11). Mandelic Acid. (10). Tartaric Acid. (12). 2-Azobis(2- ...
and S.-Con.T.; literature analysis and search, H.-Con.Y. enhance the treatment outcome of individuals significantly. Sensitive biomarkers are necessary in early recognition of disease aswell concerning monitor the condition activity and improvement. This review seeks to go over the pathogenic part of various immune system cells and immunological substances in RA. This review also shows the need for understanding the immune system cells in dealing with RA and in discovering book biomarkers. gene that disrupts the BCR signaling pathway in central B-cell tolerance checkpoint [15]. The impairment of such tolerance checkpoint in RA sufferers cannot be successfully treated with medications that reduces irritation and alleviates various other clinical presentations because of the irreversible hereditary defect [16]. The impaired peripheral tolerance checkpoint can be evident as proven by the raised levels of older naive B-cells that exhibit both polyreactive and individual epithelial (HEP-2)-reactive ...
Monitoring of Methionine Sulfoxide Content and Methionine Sulfoxide Reductase Activity. Selenoproteins. Methods in Molecular ...
  • Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L - 1 kit is backordered and will ship as soon as it is back in stock. (dnamethsoc.com)
  • Moreover, homocysteine is a type of advanced metabolite resulting from the methionine conversion into cysteine. (aminoacidstoday.com)
  • Moreover, methionine is a significant sulfur source for varying functions in your body which can be needed for liver detox together with the synthesis of numerous amino acids like proteins, cysteine , and enzymes. (aminoacidstoday.com)
  • Hydroxyl will be replaced by yet another amino acid just like cysteine or another methionine derivative. (aminoacidstoday.com)
  • Methionine in proteins, apart from its role in the initiation of translation, is assumed to play a simple structural role in the hydrophobic core, in a similar way to other hydrophobic amino acids such as leucine, isoleucine, and valine. (nih.gov)
  • Amino Acids Methionine: Is It Metabolically Unique? (aminoacidstoday.com)
  • By reading this article, you will learn more about the unique qualities of amino acids methionine, particularly its metabolic performance. (aminoacidstoday.com)
  • How does methionine work efficiently by way of metabolism and are amino acids methionine unique in terms of supporting bodily functions? (aminoacidstoday.com)
  • Amino acids methionine perform a range of functions. (aminoacidstoday.com)
  • More recently, looking into the research community, there have been truths discovered concerning a lessened amount in fundamental amino acids methionine as principal triggers in sweeping transformations in line with metabolism. (aminoacidstoday.com)
  • It is essential to get ample dietary amino acids methionine intake in foods. (aminoacidstoday.com)
  • We used SPOTscan analysis with overlapping octapeptides to identify the binding regions for the antibodies and then methionine substitution analysis to further define the critical amino acids (aa) in each epitope. (cdc.gov)
  • Both, top-down and bottom-up approaches have been used to estimate and validate the size of the global methionine market and to estimate the size of various other dependent sub-markets. (marketsandmarkets.com)
  • Some of the major market players in the global methionine market include Evonik (Germany), Adisseo (France), Novus International (US), CJ CHEILJEDANG (South Korea), Sumitomo Chemical (Japan), AJINOMOTO (Japan), Phibro (US), Prinova Group (US), Sunrise Nutrachem (China), and Chongqing Unisplendour Chemical (China). (marketsandmarkets.com)
  • This investment is a building block of our global methionine asset strategy with the clear goal of being the cost and technology leader in all regions, and the reliable partner for our customers," he added. (feedstrategy.com)
  • However, research from a number of laboratories supports the concept that methionine serves as an important cellular antioxidant, stabilizes the structure of proteins, participates in the sequence-independent recognition of protein surfaces, and can act as a regulatory switch through reversible oxidation and reduction. (nih.gov)
  • The oxidation of peptidyl-L-methionine to peptidyl-L-methionine sulfone. (systemsbiology.net)
  • More specifically, vitamin B12 and folate deficiency will not only lead to impaired fetal are necessary cofactors for the conversion of growth in utero but may also make the fetus homocysteine to methionine, the latter being an susceptible to a multitude to chronic diseases important methyl donor required for the synthesis of including diabetes mellitus, fatty liver disease, neurotransmitters and phospholipids. (who.int)
  • In the mother methionine, for which B12 and folate are classical cobalamin deficiency features may be necessary cofactors. (who.int)
  • The aim of this project was thus to clarify the roles of protein reduction and methionine elevation within this model, especially within the context of amino acid and one-carbon metabolism. (uwaterloo.ca)
  • Thus, ingestion of low-protein diets with a relative (0.5%) or overt excess (1.0%) of methionine appears to disrupt one-carbon metabolism at the level of homocysteine remethylation to methionine. (uwaterloo.ca)
  • Methionine also enhances liver functions, lipid metabolism, as well as detoxification. (aminoacidstoday.com)
  • As a dietary intervention, methionine restriction (MR) has been reported to increase longevity and improve metabolism disorders. (bvsalud.org)
  • Our client, a top American agricultural processor and food ingredient provider, was keen to understand the market for methionine for applications such as animal feed, food & dietary supplements, and pharmaceuticals across major geographic regions. (marketsandmarkets.com)
  • 1 Source: Fetrow CW, Avila JR. "Efficacy of the dietary supplement S-adenosyl-L-methionine. (lycored.com)
  • Together, our study indicated that lower dietary methionine intake is associated with improved cognitive function , in which CBS/H2S pathway plays an essential role . (bvsalud.org)
  • 2 Source: Larsson SC, Giovannucci E, Wolk A. "Methionine and vitamin B6 intake and risk of pancreatic cancer: a prospective study of Swedish women and men. (lycored.com)
  • Excessive methionine intake, with an inadequate intake of folic acid, vitamin B6 and vitamin B12, may increase the rate of conversion of methionine to homocysteine - both these theories have not been proven in humans. (3r-medical.com)
  • Appropriate intake for folic acid, vitamin B6, vitamin B12, as well as betaine all are essential to ensuring the right methionine recycling takes place in a way that homocysteine levels will not raise methionine. (aminoacidstoday.com)
  • Here we sought to investigate the neuroprotective effects of low methionine intake in mild cognitive impairment (MCI) patients and APP/PS1 AD model mice , and to uncover the underlying mechanisms. (bvsalud.org)
  • In a cohort composed of 45 individuals diagnosed with MCI and 61 healthy controls without cognitive impairment , methionine intake was found to be positively associated with the increased risk of MCI, where no sex differences were observed. (bvsalud.org)
  • Evonik will develop and expand its German plant that produces methylmercapto-propionaldehyde (MMP), an organic compound that is integral in the production of DL-methionine. (feedstrategy.com)
  • With this investment, Evonik is strengthening the European methionine network to safeguard the long-term supply of MMP to our MetAMINO production hub in Antwerp, Belgium," said Gaetano Blanda, head of Evonik's animal nutrition business line, in a press release. (feedstrategy.com)
  • The amino acid methionine is also a great antioxidant as the sulfur it supplies inactivates free radicals. (3r-medical.com)
  • People suffering from schizophrenia could require extra methionine since it reduces the level of histidine in the body, a level normally higher in people suffering from schizophrenia. (3r-medical.com)
  • In this study, we have designed three peptides from copper binding regions of CTR1 which are rich in histidine and methionine. (researcher-app.com)
  • L-Methionine is rich in sulfur, a must for healthy joint function. (lycored.com)
  • Currently the effects of protein restriction in the Southampton low-protein diet are confounded by a relative elevation of the amino acid methionine. (uwaterloo.ca)
  • Despite all these evidences, the role of methionine in protein structure and function is largely overlooked by most biochemists. (nih.gov)
  • LP: 9% casein, 0.5% methionine), while a third low-protein high-methionine diet (LP-MET: 9% casein, 1.0% methionine) was employed as a positive control for methionine stress. (uwaterloo.ca)
  • In dams and fetuses, methionine was significantly elevated in both low-protein groups. (uwaterloo.ca)
  • Maternal homocysteine was significantly elevated only in dams fed the low-protein high-methionine diet. (uwaterloo.ca)
  • Further investigations into levels of other one-carbon metabolites in dams and fetuses are necessary to fully characterize the effect of low-protein high-methionine diets, particularly within the context of the Southampton model of developmental programming. (uwaterloo.ca)
  • Functional variant in methionine synthase reductase decreases the risk of Down syndrome in China. (cdc.gov)
  • Pregnant Wistar rats were fed casein-based diets ad libitum varying in casein (18% or 9%) and methionine content (0.5% or 1.0%) from day 0 through 20 of pregnancy. (uwaterloo.ca)
  • From that facility, the company supplies its U.S. milk and dairy customers with Mepron - a special methionine formulation which prevents degradation in the rumen and fosters balanced nutrient supply of dairy cows. (feedstrategy.com)
  • In our study we aimed assessing the correlation of metabolic information on 11C-methionine PET and biological data in patients affected by primary brain tumor and eligible for surgical resection. (cns.org)
  • Patients underwent pre-surgical 11C-methionine PET performed according to standard procedure and in all cases semi-quantitative and quantitative analyses were obtained considering SUVmax, SUVratio, and whole tumor metabolic activity (WTMA), expressed as a product of metabolic tumor volume and lesion SUVmean. (cns.org)
  • In cases of acetaminophen poisoning, methionine can help decrease or prevent liver damage. (lycored.com)
  • People with liver problems, pancreatitis, HIV/AIDS as well as Parkinson's disease may require high amounts of methionine in their diet but they should consult their physician before taking higher doses. (3r-medical.com)
  • Objective: To examine the comparative antidepressant efficacy of S-adenosyl-l-methionine (SAMe) and escitalopram in a placebo-controlled, randomized, double-blind clinical trial. (psychiatrist.com)
  • Semi-quantitative and quantitative information obtained by 11C-methionine PET significantly correlated with histological grading in primary brain tumors. (cns.org)
  • The methionine market is driven by the rise in the consumption of animal-based products, increasing health issues, and implementation of innovative animal husbandry practices to improve meat quality. (marketsandmarkets.com)
  • It also has the ability to combine with other chemicals in the body to remove toxins and convert into SAMe (S-Adenosyl Methionine), a chemical used to treat depression and reduce osteoarthritic pain. (lycored.com)
  • RIGAMONTI, R. Oral S-adenosyl-L-methionine in depression. (bvsalud.org)
  • It gets changed into S-adenosylmethionine, considered to be the active methionine type. (aminoacidstoday.com)
  • MnM identified all the leading methionine manufacturers for animal nutrition globally and provided a competitive benchmarking of these companies in terms of strength of product portfolio, geographic presence, operational performance, and excellence in strategy execution. (marketsandmarkets.com)
  • reduced methionine levels as part of pregnancy have now been connected with neural tube defects. (aminoacidstoday.com)
  • This helped the client to benchmark industry best practices and realign its operations and marketing strategy for methionine. (marketsandmarkets.com)
  • The client was able to grow its methionine business across target regions such as Asia Pacific, Europe, and North America. (marketsandmarkets.com)
  • Exactly how much homocysteine is found in the blood directly associates to just how much methionine becomes drawn in by way of food and just how much becomes metabolized. (aminoacidstoday.com)
  • The daily dosage of methionine is about 12 mg per kilogram of body weight per day - which would translate to about 840 mg for a 70 kg male. (3r-medical.com)
  • We and others have previously demonstrated delayed Aβ aggregation as a consequence of oxidizing a single methionine residue at position 35 (Met-35). (uni-konstanz.de)
  • To be safe, never take methionine-or any single amino acid for that matter-for longer than three months unless you are under the direction of a doctor familiar with its use. (3r-medical.com)
  • Some studies have also indicated that methionine might improve memory recall. (3r-medical.com)
  • MnM also assisted the client in identifying the price range and production cost of methionine offered by different competitors. (marketsandmarkets.com)
  • Interviews with senior management and CXO level executives from competitors were conducted to understand what best practices they follow in terms of production or sales/distribution of methionine to target customers. (marketsandmarkets.com)
  • Methionine Poultry Feed Additives are prepared in our ultra-advanced production division making the best use of pioneering tools and techniques. (shaktiayurvedic.com)
  • Facility in Wesseling, Germany, produces methylmercapto-propionaldehyde, which is integral in the production of DL-methionine. (feedstrategy.com)
  • The company said it has invested EUR25 million (US$27.3 million) in the plant in Wesseling, Germany, in a move to strengthen its methionine production network. (feedstrategy.com)
  • In October 2020, it said it would close its plant in Wesseling, Germany - the smallest of its DL-methionine production plants - and invest in upgrades at the facility. (feedstrategy.com)
  • Among plants as well as microbes, methionine could be made through an ongoing process known as methionine biosynthesis. (aminoacidstoday.com)
  • The move underscores our commitment to serving and expanding the global DL-methionine market and secures the best possible supply security for our customers. (feedstrategy.com)
  • 1 Some studies even suggest that methionine may reduce the risk of pancreatic cancer. (lycored.com)
  • The client was also interested in a comprehensive analysis of competitors, as well as the cost and price of methionine. (marketsandmarkets.com)