5 methyltetrahydrofolate homocysteine s methyltransferase. Medical search

Compounds based on 5,6,7,8-tetrahydrofolate.

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 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.

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.

Cell surface receptors that bind to and transport FOLIC ACID, 5-methyltetrahydrofolate, and a variety of folic acid derivatives. The receptors are essential for normal NEURAL TUBE development and transport folic acid via receptor-mediated endocytosis.

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.

An enzyme that catalyzes the transfer of a methyl group from S-ADENOSYLMETHIONINE to the 5-position of CYTOSINE residues in DNA.

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.

Tetrahydrofolates which are substituted by a formyl group at either the nitrogen atom in the 5 position or the nitrogen atom in the 10 position. N(5)-Formyltetrahydrofolate is leukovorin (citrovorum factor) while N(10)-formyltetrahydrofolate is an active coenzyme which functions as a carrier of the formyl group in a number of enzymatic reactions.

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)

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.

Derivatives of folic acid (pteroylglutamic acid). In gamma-glutamyl linkage they are found in many tissues. They are converted to folic acid by the action of pteroylpolyglutamate hydrolase or synthesized from folic acid by the action of folate polyglutamate synthetase. Synthetic pteroylpolyglutamic acids, which are in alpha-glutamyl linkage, are active in bacterial growth assays.

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)

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.

An enzyme that catalyzes the METHYLATION of GLYCINE using S-ADENOSYLMETHIONINE to form SARCOSINE with the concomitant production of S-ADENOSYLHOMOCYSTEINE.

5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions.

A sulfur-containing essential L-amino acid that is important in many body functions.

A thiol-containing amino acid formed by a demethylation of METHIONINE.

Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.

Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.

A ubiquitously expressed folic acid transporter that functions via an antiporter mechanism which is coupled to the transport of organic phosphates.

An enzyme that transfers methyl groups from O(6)-methylguanine, and other methylated moieties of DNA, to a cysteine residue in itself, thus repairing alkylated DNA in a single-step reaction. EC 2.1.1.63.

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.

Anemia characterized by larger than normal erythrocytes, increased mean corpuscular volume (MCV) and increased mean corpuscular hemoglobin (MCH).

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)

An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC 2.1.1.43.

Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.

A group of water-soluble vitamins, some of which are COENZYMES.

An antineoplastic antimetabolite with immunosuppressant properties. It is an inhibitor of TETRAHYDROFOLATE DEHYDROGENASE and prevents the formation of tetrahydrofolate, necessary for synthesis of thymidylate, an essential component of DNA.

Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs, primarily brain and spleen.

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)

Injectable form of VITAMIN B 12 that has been used therapeutically to treat VITAMIN B 12 DEFICIENCY.

Cyclic TETRAPYRROLES based on the corrin skeleton.

Methylases that are specific for CYTOSINE residues found on DNA.

The active metabolite of FOLIC ACID. Leucovorin is used principally as an antidote to FOLIC ACID ANTAGONISTS.

A PROTEIN O-METHYLTRANSFERASE that recognizes and catalyzes the methyl esterification of ISOASPARTIC ACID and D-ASPARTIC ACID residues in peptides and proteins. It initiates the repair of proteins damaged by the spontaneous decomposition of normal L-aspartic acid and L-asparagine residues.

Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the host-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognized by the restriction endonucleases of similar specificity and destroyed by cleavage. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms.

An enzyme responsible for producing a species-characteristic methylation pattern on adenine residues in a specific short base sequence in the host cell DNA. The enzyme catalyzes the methylation of DNA adenine in the presence of S-adenosyl-L-methionine to form DNA containing 6-methylaminopurine and S-adenosyl-L-homocysteine. EC 2.1.1.72.

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)

Inhibitors of the enzyme, dihydrofolate reductase (TETRAHYDROFOLATE DEHYDROGENASE), which converts dihydrofolate (FH2) to tetrahydrofolate (FH4). They are frequently used in cancer chemotherapy. (From AMA, Drug Evaluations Annual, 1994, p2033)

Addition of methyl groups to DNA. DNA methyltransferases (DNA methylases) perform this reaction using S-ADENOSYLMETHIONINE as the methyl group donor.

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.

Compounds based on 2-amino-4-hydroxypteridine.

A peptide that is a homopolymer of glutamic acid.

Products in capsule, tablet or liquid form that provide dietary ingredients, and that are intended to be taken by mouth to increase the intake of nutrients. Dietary supplements can include macronutrients, such as proteins, carbohydrates, and fats; and/or MICRONUTRIENTS, such as VITAMINS; MINERALS; and PHYTOCHEMICALS.

A subtype of GPI-anchored folate receptors that is expressed in tissues of epithelial origin. This protein is also identified as an ovarian-tumor-specific antigen.

A symporter protein that couples the transport of FOLIC ACID with HYDROGEN IONS. The transporter functions most effectively under acidic conditions.

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.

Transport proteins that carry specific substances in the blood or across cell membranes.

Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.

Catalyzes the hydrolysis of pteroylpolyglutamic acids in gamma linkage to pterolylmonoglutamic acid and free glutamic acid. EC 3.4.19.9.

The rate dynamics in chemical or physical systems.

Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.

A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.

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.

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.

The extent to which the active ingredient of a drug dosage form becomes available at the site of drug action or in a biological medium believed to reflect accessibility to a site of action.

The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy generally occurring between days 18-29 of gestation. Ectodermal and mesodermal malformations (mainly involving the skull and vertebrae) may occur as a result of defects of neural tube closure. (From Joynt, Clinical Neurology, 1992, Ch55, pp31-41)

A megaloblastic anemia occurring in children but more commonly in later life, characterized by histamine-fast achlorhydria, in which the laboratory and clinical manifestations are based on malabsorption of vitamin B 12 due to a failure of the gastric mucosa to secrete adequate and potent intrinsic factor. (Dorland, 27th ed)

A natural product that has been considered as a growth factor for some insects.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

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.

Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.

An enzyme that catalyses three sequential METHYLATION reactions for conversion of phosphatidylethanolamine to PHOSPHATIDYLCHOLINE.

Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.

The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.

An enzyme that catalyzes the transfer of methyl groups from S-adenosylmethionine to free carboxyl groups of a protein molecule forming methyl esters. EC 2.1.1.-.

This enzyme catalyzes the last step of CREATINE biosynthesis by catalyzing the METHYLATION of guanidinoacetate to CREATINE.

An enzyme that catalyzes the METHYLATION of phosphatidyl-N-methylethanolamine to produce phosphatidyl-N-dimethylethanolamine. This enzyme can also methylate phosphatidyl-N-dimethylethanolamine to produce phosphatidyl-N-trimethylethanolamine (PHOSPHATIDYLCHOLINE).

An enzyme that catalyzes the demethylation of L-homocysteine to L-METHIONINE.

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)

Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.

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.

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 pyrimidine analogue that inhibits DNA methyltransferase, impairing DNA methylation. It is also an antimetabolite of cytidine, incorporated primarily into RNA. Azacytidine has been used as an antineoplastic agent.

The regular and simultaneous occurrence in a single interbreeding population of two or more discontinuous genotypes. The concept includes differences in genotypes ranging in size from a single nucleotide site (POLYMORPHISM, SINGLE NUCLEOTIDE) to large nucleotide sequences visible at a chromosomal level.

Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.

An individual in which both alleles at a given locus are identical.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.

A multisubunit polycomb protein complex that catalyzes the METHYLATION of chromosomal HISTONE H3. It works in conjunction with POLYCOMB REPRESSIVE COMPLEX 1 to effect EPIGENETIC REPRESSION.

An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.

The white liquid secreted by the mammary glands. It contains proteins, sugar, lipids, vitamins, and minerals.

A malonic acid derivative which is a vital intermediate in the metabolism of fat and protein. Abnormalities in methylmalonic acid metabolism lead to methylmalonic aciduria. This metabolic disease is attributed to a block in the enzymatic conversion of methylmalonyl CoA to succinyl CoA.

Established cell cultures that have the potential to propagate indefinitely.

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.

An essential amino acid. It is often added to animal feed.

A genetic process by which the adult organism is realized via mechanisms that lead to the restriction in the possible fates of cells, eventually leading to their differentiated state. Mechanisms involved cause heritable changes to cells without changes to DNA sequence such as DNA METHYLATION; HISTONE modification; DNA REPLICATION TIMING; NUCLEOSOME positioning; and heterochromatization which result in selective gene expression or repression.

A pyrimidine base that is a fundamental unit of nucleic acids.

Interruption or suppression of the expression of a gene at transcriptional or translational levels.

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).

Elements of limited time intervals, contributing to particular results or situations.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

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.

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.

A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

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 method of studying a drug or procedure in which both the subjects and investigators are kept unaware of who is actually getting which specific treatment.

A mass spectrometry technique using two (MS/MS) or more mass analyzers. With two in tandem, the precursor ions are mass-selected by a first mass analyzer, and focused into a collision region where they are then fragmented into product ions which are then characterized by a second mass analyzer. A variety of techniques are used to separate the compounds, ionize them, and introduce them to the first mass analyzer. For example, for in GC-MS/MS, GAS CHROMATOGRAPHY-MASS SPECTROMETRY is involved in separating relatively small compounds by GAS CHROMATOGRAPHY prior to injecting them into an ionization chamber for the mass selection.

DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.

An enzyme which catalyzes the catabolism of S-ADENOSYLHOMOCYSTEINE to ADENOSINE and HOMOCYSTEINE. It may play a role in regulating the concentration of intracellular adenosylhomocysteine.

The 4-methanol form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. 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).

Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.

Areas of increased density of the dinucleotide sequence cytosine--phosphate diester--guanine. They form stretches of DNA several hundred to several thousand base pairs long. In humans there are about 45,000 CpG islands, mostly found at the 5' ends of genes. They are unmethylated except for those on the inactive X chromosome and some associated with imprinted genes.

Highly reactive compounds produced when oxygen is reduced by a single electron. In biological systems, they may be generated during the normal catalytic function of a number of enzymes and during the oxidation of hemoglobin to METHEMOGLOBIN. In living organisms, SUPEROXIDE DISMUTASE protects the cell from the deleterious effects of superoxides.

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.

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

Nucleic acid structures found on the 5' end of eukaryotic cellular and viral messenger RNA and some heterogeneous nuclear RNAs. These structures, which are positively charged, protect the above specified RNAs at their termini against attack by phosphatases and other nucleases and promote mRNA function at the level of initiation of translation. Analogs of the RNA caps (RNA CAP ANALOGS), which lack the positive charge, inhibit the initiation of protein synthesis.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

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.

An amino acid intermediate in the metabolism of choline.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

An aspect of personal behavior or lifestyle, environmental exposure, or inborn or inherited characteristic, which, on the basis of epidemiologic evidence, is known to be associated with a health-related condition considered important to prevent.

Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.

An antineoplastic agent. It has significant activity against melanomas. (from Martindale, The Extra Pharmacopoeia, 31st ed, p564)

A class of drugs that differs from other alkylating agents used clinically in that they are monofunctional and thus unable to cross-link cellular macromolecules. Among their common properties are a requirement for metabolic activation to intermediates with antitumor efficacy and the presence in their chemical structures of N-methyl groups, that after metabolism, can covalently modify cellular DNA. The precise mechanisms by which each of these drugs acts to kill tumor cells are not completely understood. (From AMA, Drug Evaluations Annual, 1994, p2026)

Myeloid-lymphoid leukemia protein is a transcription factor that maintains high levels of HOMEOTIC GENE expression during development. The GENE for myeloid-lymphoid leukemia protein is commonly disrupted in LEUKEMIA and combines with over 40 partner genes to form FUSION ONCOGENE PROTEINS.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

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.

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).

The parts of a macromolecule that directly participate in its specific combination with another molecule.

A condition due to deficiency in any member of the VITAMIN B COMPLEX. These B vitamins are water-soluble and must be obtained from the diet because they are easily lost in the urine. Unlike the lipid-soluble vitamins, they cannot be stored in the body fat.

A group of carrier proteins which bind with VITAMIN B12 in the BLOOD and aid in its transport. Transcobalamin I migrates electrophoretically as a beta-globulin, while transcobalamins II and III migrate as alpha-globulins.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

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.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

An ASPARTIC ACID residue in polypeptide chains that is linked at the beta-carboxyl group instead of at the normal, alpha-carboxyl group, polypeptide linkage. It is a result of the spontaneous decomposition of aspartic acid or ASPARAGINE residues.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

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.

The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.

A nutritional condition produced by a deficiency of VITAMIN B 6 in the diet, characterized by dermatitis, glossitis, cheilosis, and stomatitis. Marked deficiency causes irritability, weakness, depression, dizziness, peripheral neuropathy, and seizures. In infants and children typical manifestations are diarrhea, anemia, and seizures. Deficiency can be caused by certain medications, such as isoniazid.

A hydrocarbon used as an industrial solvent. It has been used as an aerosal propellent, as a refrigerant and as a local anesthetic. (From Martindale, The Extra Pharmacopoeia, 31st ed, p1403)

An antibiotic purine ribonucleoside that readily substitutes for adenosine in the biological system, but its incorporation into DNA and RNA has an inhibitory effect on the metabolism of these nucleic acids.

A methylated nucleotide base found in eukaryotic DNA. In ANIMALS, the DNA METHYLATION of CYTOSINE to form 5-methylcytosine is found primarily in the palindromic sequence CpG. In PLANTS, the methylated sequence is CpNpGp, where N can be any base.

Folate and homocysteine metabolism in copper-deficient rats. (1/254)

To investigate the effect of copper deficiency on folate and homocysteine metabolism, we measured plasma, red-cell and hepatic folate, plasma homocysteine and vitamin B-12 concentrations, and hepatic methionine synthase activities in rats. Two groups of male Sprague-Dawley rats were fed semi-purified diets containing either 0. 1 mg (copper-deficient group) or 9.2 mg (control group) of copper per kg. After 6 weeks of dietary treatment, copper deficiency was established as evidenced by markedly decreased plasma and hepatic copper concentrations in rats fed the low-copper diet. Plasma, red-cell, hepatic folate, and plasma vitamin B-12 concentrations were similar in both groups, whereas plasma homocysteine concentrations in the copper-deficient group were significantly higher than in the control group (P<0.05). Copper deficiency resulted in a 21% reduction in hepatic methionine synthase activity as compared to the control group (P<0.01). This change most likely caused the increased hepatic 5-methyltetrahydrofolate and plasma homocysteine concentrations in the copper-deficient group. Our results indicate that hepatic methionine synthase may be a cuproenzyme, and plasma homocysteine concentrations are influenced by copper nutriture in rats. These data support the concept that copper deficiency can be a risk factor for cardiovascular disease. (+info)

Co-ordinate variations in methylmalonyl-CoA mutase and methionine synthase, and the cobalamin cofactors in human glioma cells during nitrous oxide exposure and the subsequent recovery phase. (2/254)

We investigated the co-ordinate variations of the two cobalamin (Cbl)-dependent enzymes, methionine synthase (MS) and methylmalonyl-CoA mutase (MCM), and measured the levels of their respective cofactors, methylcobalamin (CH3Cbl) and adenosylcobalamin (AdoCbl) in cultured human glioma cells during nitrous oxide exposure and during a subsequent recovery period of culture in a nitrous oxide-free atmosphere (air). In agreement with published data, MS as the primary target of nitrous oxide was inactivated rapidly (initial rate of 0.06 h(-1)), followed by reduction of CH3Cbl (to <20%). Both enzyme activity and cofactor levels recovered rapidly when the cells were subsequently cultured in air, but the recovery was completely blocked by the protein-synthesis inhibitor, cycloheximide. During MS inactivation, there was a reduction of cellular AdoCbl and holo-MCM activity (measured in the absence of exogenous AdoCbl) to about 50% of pre-treatment levels. When the cells were transferred to air, both AdoCbl and holo-MCM activity recovered, albeit more slowly than the MS system. Notably, the regain of the holo-MCM and AdoCbl was enhanced rather than inhibited by cycloheximide. These findings confirm irreversible damage of MS by nitrous oxide; hence, synthesis of the enzyme is required to restore its activity. In contrast, restoration of holo-MCM activity is only dependent on repletion of the AdoCbl cofactor. We also observed a synchronous fluctuation in AdoCbl and the much larger hydroxycobalamin pool during the inactivation and recovery phase, suggesting that the loss and repletion of AdoCbl reflect changes in intracellular Cbl homoeostasis. Our data demonstrate that the nitrous oxide-induced changes in MS and CH3Cbl are associated with reversible changes in both MCM holoactivity and the AdoCbl level, suggesting co-ordinate distribution of Cbl cofactors during depletion and repletion. (+info)

Reversal of ethanol-induced hepatic steatosis and lipid peroxidation by taurine: a study in rats. (3/254)

Alcohol (ethanol) was administered chronically to female Sprague-Dawley rats in a nutritionally adequate, totally liquid diet for 28 days. This resulted in significant hepatic steatosis and lipid peroxidation. When taurine was administered for 2 days following alcohol withdrawal it was found to reduce alcohol-induced lipid peroxidation and completely reversed hepatic steatosis. The reversal of hepatic steatosis was demonstrated both biochemically and histologically. Two days following alcohol withdrawal, the apparent activity of the alcohol-inducible form of cytochrome P450 (CYP2E1) was unchanged although total cytochrome P450 content was increased. In addition, alcohol significantly inhibited hepatic methionine synthase activity and increased homocysteine excretion in urine. Although alcohol did not affect the urinary excretion of taurine (a non-invasive marker of liver damage), levels of serum and hepatic taurine were markedly raised in animals given taurine following their treatment with alcohol, compared to animals given taurine alone. There was evidence of slight bile duct injury in animals treated with alcohol and with alcohol followed by taurine, as indicated by raised serum alkaline phosphatase (ALP) and cholesterol. Aspartate aminotransferase (AST) was also slightly raised. The effects of taurine on reversing hepatic steatosis may be due to the enhanced secretion of hepatic triglycerides. It is suggested that increased bile flow as a result of taurine treatment may have contributed to the removal of lipid peroxides. These in-vivo findings demonstrate for the first time that hepatic steatosis and lipid peroxidation, occurring as a result of chronic alcohol consumption, can be reversed by administration of taurine to rats for 2 days. (+info)

A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium. (4/254)

No periplasmic binding protein has been demonstrated for the ATP-binding cassette (ABC)-type cobalamin transporter BtuCD. New mutations (btuF) are described that affect inner-membrane transport. The BtuF protein has a signal sequence and resembles the periplasmic binding proteins of several other ABC transporters. (+info)

Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. (5/254)

Methionine synthase reductase (MSR) deficiency is an autosomal recessive disorder of folate/cobalamin metabolism leading to hyperhomocysteinemia, hypo- methioninemia and megaloblastic anemia. Deficiency in MSR activity occurs as the result of a defect in the MSR enzyme, which is required for the reductive activation of methionine synthase (MS). MS itself is responsible for the folate/cobalamin-dependent conversion of homo- cysteine to methionine. We have recently cloned the cDNA corresponding to the MSR protein, a novel member of the ferredoxin-NADP(+)reductase (FNR) family of electron transferases. We have used RT-PCR, heteroduplex, single-strand conformation poly- morphism (SSCP) and DNA sequence analyses to reveal 11 mutations in eight patients from seven families belonging to the cblE complementation group of patients of cobalamin metabolism that is defective in the MSR protein. The mutations include splicing defects leading to large insertions or deletions, as well as a number of smaller deletions and point mutations. Apart from an intronic substitution found in two unrelated patients, the mutations appear singular among individuals. Of the eleven, three are nonsense mutations, allowing for the identification of two patients for whom little if any MSR protein should be produced. The remaining eight involve point mutations or in-frame disruptions of the coding sequence and are distributed throughout the coding region, including proposed FMN, FAD and NADPH binding sites. These data demonstrate a unique requirement for MSR in the reductive activation of MS. (+info)

A polymorphism of the methionine synthase gene: association with plasma folate, vitamin B12, homocyst(e)ine, and colorectal cancer risk. (6/254)

We previously reported (J. Chen et al., Cancer Res., 56: 4862-4864, 1996; J. Ma et al., Cancer Res., 57: 1098-1102, 1997) that a 5,10-methylenetetrahydrofolate reductase (MTHFR) polymorphism (677C-->T, ala-->val) was associated with lower risk of colorectal cancer. In this study, we examined the relationship of a polymorphism (2756A-->G, asp-->gly) in the gene (MTR) for methionine synthase, another important enzyme in the same folate/methionine/homocyst(e)ine metabolic pathway, with risk of colorectal cancer among 356 cases and 476 cancer-free controls. The frequency of the homozygous variant genotype (gly/gly) was slightly lower among cases (3%) than controls (5%). The odds ratio for the gly/gly genotype was 0.59 [95% confidence interval (CI), 0.27-1.27] compared with those with the homozygous wild type (asp/asp). There were no significant differences in plasma levels of folate, vitamin B12, and homocyst(e)ine (tHcy) among the MTR genotypes, in contrast to the MTHFR polymorphism. However, similar to the interaction observed for the MTHFR polymorphism among men who consumed less than 1 alcoholic drink/day, those with the gly/gly genotype had a lower risk of colorectal cancer with an odds ratio of 0.27 (95% CI, 0.09-0.81) compared with those with the asp/asp genotype. The possible association of the MTR polymorphism with lower risk of colorectal cancer especially among those with low alcohol consumption, in the same direction as for the MTHFR polymorphism, is intriguing. However, our study had limited statistical power because of the low frequency of the MTR variant genotype, which is reflected in the wide CIs. Hence, these findings need to be confirmed in larger populations. (+info)

Heterologous high level expression, purification, and enzymological properties of recombinant rat cobalamin-dependent methionine synthase. (7/254)

Rat methionine synthase was expressed chiefly as apoenzyme in recombinant baculovirus-infected insect cells (Yamada, K., Tobimatsu, T., and Toraya, T. (1998) Biosci. Biotech. Biochem. 62, 2155-2160). The apoenzyme produced was very unstable, and therefore, after complexation with methylcobalamin, the functional holoenzyme was purified to homogeneity. The specific activity and apparent K(m) values for substrates were in good agreement with those obtained with purified rat liver enzyme. The electronic spectrum of the purified recombinant enzyme resembled that of cob(II)alamin and changed to a methylcobalamin-like one upon incubation of the enzyme with titanium(III) and S-adenosylmethionine. The rate of oxidative inactivation of the enzyme in the absence of S-adenosylmethionine was slower with a stronger reducing agent like titanium(III). The nucleotide moiety, especially the phosphodiester group, was shown to play an important role in the binding of the coenzyme to apoprotein and thus for catalysis. Upon incubation with the apoenzyme in the absence of a reducing agent, cyano- and aquacobalamin were not effective or were effective only slightly in reconstituting holoenzyme. Ethyl- and propylcobalamin formed inactive complexes with apoenzyme, which were converted to holoenzyme by photolytic activation. Adenosylcobalamin was not able to form a complex with apoenzyme, which was convertible to holoenzyme by photoirradiation. (+info)

Characterization and functional expression of cDNAs encoding methionine-sensitive and -insensitive homocysteine S-methyltransferases from Arabidopsis. (8/254)

Plants synthesize S-methylmethionine (SMM) from S-adenosylmethionine (AdoMet), and methionine (Met) by a unique reaction and, like other organisms, use SMM as a methyl donor for Met synthesis from homocysteine (Hcy). These reactions comprise the SMM cycle. Two Arabidopsis cDNAs specifying enzymes that mediate the SMM --> Met reaction (SMM:Hcy S-methyltransferase, HMT) were identified by homology and authenticated by complementing an Escherichia coli yagD mutant and by detecting HMT activity in complemented cells. Gel blot analyses indicate that these enzymes, AtHMT-1 and -2, are encoded by single copy genes. The deduced polypeptides are similar in size (36 kDa), share a zinc-binding motif, lack obvious targeting sequences, and are 55% identical to each other. The recombinant enzymes exist as monomers. AtHMT-1 and -2 both utilize l-SMM or (S,S)-AdoMet as a methyl donor in vitro and have higher affinities for SMM. Both enzymes also use either methyl donor in vivo because both restore the ability to utilize AdoMet or SMM to a yeast HMT mutant. However, AtHMT-1 is strongly inhibited by Met, whereas AtHMT-2 is not, a difference that could be crucial to the control of flux through the HMT reaction and the SMM cycle. Plant HMT is known to transfer the pro-R methyl group of SMM. This enabled us to use recombinant AtHMT-1 to establish that the other enzyme of the SMM cycle, AdoMet:Met S-methyltransferase, introduces the pro-S methyl group. These opposing stereoselectivities suggest a way to measure in vivo flux through the SMM cycle. (+info)

Methyltransferase Arakawa's syndrome II Betaine-homocysteine S-methyltransferase GRCh38: Ensembl release 89: ENSG00000116984 - ... "Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, ... The cob-independent MetE consists of two TIM-barrel domains that bind homocysteine and N5-MeTHF individually. The two domains ... March 2003). "Homocysteine remethylation enzyme polymorphisms and increased risks for neural tube defects". Molecular Genetics ...

https://en.wikipedia.org/wiki/Methionine_synthase

Chronic homocysteine elevation increases s-adenosyl-L-homocysteine levels, consequently inhibiting methyltransferase activity ... Prenatal diagnosis of this condition is possible using [14C] methyltetrahydrofolate. Mutation analysis in native chorionic ... Homocysteine, a sulfur based amino acid is the main product of methionine demethylation. Elevated homocysteine is an ... A major product of methionine demethylation is homocysteine. Remethylation of homocysteine occurs via a cobalamin dependent ...

https://en.wikipedia.org/wiki/MTRR_(gene)

... may refer to: 5-methyltetrahydrofolate-homocysteine methyltransferase reductase, a human gene Memory Type Range Registers ...

https://en.wikipedia.org/wiki/MTRR

SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of ... Methanol, methyl tetrahydrofolate, mono-, di-, and trimethylamine, methanethiol, methyltetrahydromethanopterin, and ... These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM ... Examples include: Catechol-O-methyltransferase DNA methyltransferase Histone methyltransferase 5-Methyltetrahydrofolate- ...

https://en.wikipedia.org/wiki/Methyltransferase

Changes to chromosome 5 include an extra segment of the short (p) or long (q) arm of the chromosome in each cell (partial ... Chromosome 5 spans about 181 million base pairs (the building blocks of DNA) and represents almost 6% of the total DNA in cells ... Chromosome 5 is the 5th largest human chromosome, yet has one of the lowest gene densities. This is partially explained by ... Chromosome 5 is one of the 23 pairs of chromosomes in humans. People normally have two copies of this chromosome. ...

https://en.wikipedia.org/wiki/Chromosome_5

... is one of two active coenzymes used by vitamin B12-dependent enzymes and is the specific vitamin B12 form used by 5- ... methyltetrahydrofolate-homocysteine methyltransferase (MTR), also known as methionine synthase.[citation needed] ...

https://en.wikipedia.org/wiki/Methylcobalamin

82 (5): 941-950. doi:10.1007/s00253-009-1880-4. ISSN 1432-0614. PMID 19194700. S2CID 25880408. Bergey, D. H. (July 1919). " ... 145 (5): 1191-1199. doi:10.1099/13500872-145-5-1191. ISSN 1465-2080. PMID 10376835. Matsui, Tatsunobu; Yamada, Yukie; Mitsuya, ... 5-methyltetrahydrofolate-homocysteine methyltransferase, cadmium transporter and polynucleotide phosphorylase and are ...

https://en.wikipedia.org/wiki/Meiothermus

Amtrak code 5-Methyltetrahydrofolate-homocysteine methyltransferase Mavalli Tiffin Room, an Indian food company Former ...

https://en.wikipedia.org/wiki/MTR_(disambiguation)

Protein arginine methyltransferase 6 PSRC1: Proline/serine-rich coiled-coil protein 1 RAD54L: RAD54-like RAP1A (1p13) RBM15 ( ... 11 (5): 206. doi:10.1186/gb-2010-11-5-206. PMC 2898077. PMID 20441615. "Statistics & Downloads for chromosome 1". HUGO Gene ... 5-azacytidine type, common, fra(1)(q12) G0S2: encoding G0/G1 switch 2 GAS5 (1q25) GBA: glucosidase, beta; acid (includes ... TRE-CTC1-5: Transfer RNA-Glu (CTC) 1-5 TRP (1q31) UAP1: UDP-N-acetylhexosamine pyrophosphorylase USH2A: Usher syndrome 2A ( ...

https://en.wikipedia.org/wiki/Chromosome_1

Other cobalamin-requiring methyltransferase enzymes are also known in bacteria, such as Me-H4-MPT, coenzyme M methyltransferase ... van der Put NM, van Straaten HW, Trijbels FJ, Blom HJ (April 2001). "Folate, homocysteine and neural tube defects: an overview ... Methyltransferases Methyl (-CH3) group transfers between two molecules. These use the MeB12 (methylcobalamin) form of the ... Methionine synthase, coded by MTR gene, is a methyltransferase enzyme which uses the MeB12 and reaction type 2 to transfer a ...

https://en.wikipedia.org/wiki/Vitamin_B12

... that homocysteine can also be converted to methionine by the folate-independent enzyme betaine-homocysteine methyltransferase ( ... and recommended supplementation of methyltetrahydrofolate to potentially prevent and treat dementia (along with depression). A ... 677TT (but not 677CC/CT) individuals with lower plasma folate levels are at risk for elevated plasma homocysteine levels. In ... It does not result in thermolabile MTHFR and does not appear to affect homocysteine levels. It does, however, affect the ...

https://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase

"Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli" (Free full text). The ... Other names in common use include tetrahydropteroyltriglutamate methyltransferase, homocysteine methylase, methyltransferase, ... homocysteine methyltransferase, cobalamin-independent methionine synthase, methionine synthase (cobalamin-independent), and ... Homocysteine is coordinated to a zinc ion, as initially suggested by spectroscopy and mutagenesis . Pejchal R, Ludwig ML ( ...

https://en.wikipedia.org/wiki/5-Methyltetrahydropteroyltriglutamate—homocysteine_S-methyltransferase

... histamine N-methyltransferase MeSH D08.811.913.555.500.625 - homocysteine S-methyltransferase MeSH D08.811.913.555.500.645 - 5- ... methyltetrahydrofolate-homocysteine s-methyltransferase MeSH D08.811.913.555.500.650 - nicotinamide N-methyltransferase MeSH ... betaine-homocysteine S-methyltransferase MeSH D08.811.913.555.500.250 - catechol O-methyltransferase MeSH D08.811.913.555. ... histone-lysine n-methyltransferase MeSH D08.811.913.555.500.800.650 - o-6-methylguanine-DNA methyltransferase MeSH D08.811. ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

The formation of Me-CpG is catalyzed by the enzyme DNA methyltransferase. In mammals, DNA methylation is common in body cells, ... Methionine synthase regenerates methionine (Met) from homocysteine (Hcy). The overall reaction transforms 5- ... methyltetrahydrofolate (N5-MeTHF) into tetrahydrofolate (THF) while transferring a methyl group to Hcy to form Met. Methionine ... This process, catalyzed by enzymes such as caffeoyl-CoA O-methyltransferase, is a key reaction in the biosynthesis of lignols, ...

https://en.wikipedia.org/wiki/Methylation

S-adenosyl-L-homocysteine + sarcosine Thus, the substrates of this enzyme are S-adenosyl methionine and glycine, whereas its ... Glycine N-methyltransferase belongs to the family of methyltransferase enzymes. The systematic name of this enzyme class is S- ... Other names in common use include glycine methyltransferase, S-adenosyl-L-methionine:glycine methyltransferase, and GNMT. This ... In enzymology, a glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that catalyzes the chemical reaction S-adenosyl-L- ...

https://en.wikipedia.org/wiki/Glycine_N-methyltransferase

Homocysteine is an intermediate that is responsible for maintaining methylation reactions in critical metabolic processes. It ... Recent studies have shown that diabetic patients have decreased H3K9me3 and an increase in the Histone methyltransferase called ... This reaction is a critical step in the conversion of homocysteine to methionine. The resulting product is a methyl donor that ... After examining Type 2 diabetes patients, it was found that levels of homocysteine were exceptionally high when compared to ...

https://en.wikipedia.org/wiki/Epigenetics_of_diabetes_Type_2

... can be recycled into methionine. This process uses N5-methyl tetrahydrofolate as the methyl donor and cobalamin ( ... DNA methyltransferase as an intermediate acceptor in the process of DNA methylation). The adenosine is then hydrolyzed to yield ... Wikiversity has learning resources about Homocysteine Homocysteine MS Spectrum Homocysteine at Lab Tests Online Homocysteine: ... Homocysteine also acts as an allosteric antagonist at Dopamine D2 receptors. It has been proposed that both homocysteine and ...

https://en.wikipedia.org/wiki/Homocysteine

This is hydrolysed to homocysteine and adenosine by S-adenosylhomocysteine hydrolase EC 3.3.1.1 and the homocysteine recycled ... DNA methyltransferase SAM-I riboswitch SAM-II riboswitch SAM-III riboswitch SAM-IV riboswitch SAM-V riboswitch SAM-VI ... that use SAM as a substrate produce S-adenosyl homocysteine as a product. S-Adenosyl homocysteine is a strong negative ... Methyltransferases are also responsible for the addition of methyl groups to the 2′ hydroxyls of the first and second ...

https://en.wikipedia.org/wiki/S-Adenosyl_methionine

Additionally, a defect in homocysteine methyltransferase or a deficiency of vitamin B12 may lead to a so-called "methyl-trap" ... measured as methyltetrahydrofolate (in practice, "folate" refers to all derivatives of folic acid, but methylhydrofolate is the ... Plasma total homocysteine is only measured in special circumstances. A level above 15 μmol/L could be indicative of a folate ... High homocysteine levels in the blood can lead to vascular injuries by oxidative mechanisms which can contribute to cerebral ...

https://en.wikipedia.org/wiki/Folate_deficiency

... in a reaction catalyzed by homocysteine methyltransferase, to methionine. A defect in homocysteine methyltransferase or a ... methyltetrahydrofolate (5-MTHF), a direct target of methyl donors such as S-adenosyl methionine (SAMe), recycles the inactive ... Increased homocysteine levels suggest tissue folate deficiency, but homocysteine is also affected by vitamin B12 and vitamin B6 ... Conversion of homocysteine to methionine requires folate and vitamin B12. Elevated plasma homocysteine and low folate are ...

https://en.wikipedia.org/wiki/Folate

... histamine N-methyltransferase EC 2.1.1.9: thiol S-methyltransferase EC 2.1.1.10: homocysteine S-methyltransferase EC 2.1.1.11: ... betaine-homocysteine S-methyltransferase EC 2.1.1.6: catechol O-methyltransferase EC 2.1.1.7: nicotinate N-methyltransferase EC ... EC 2.1.1.1: nicotinamide N-methyltransferase EC 2.1.1.2: guanidinoacetate N-methyltransferase EC 2.1.1.3: thetin-homocysteine S ... phenol O-methyltransferase EC 2.1.1.26: iodophenol O-methyltransferase EC 2.1.1.27: tyramine N-methyltransferase EC 2.1.1.28: ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)

The accumulation of homocysteine leads to damage of the collagen and elastic fibers. The binding of homocysteine to lysine ... Glycine N -methyltransferase deficiency: a new patient with a novel mutation. J Inherit Metab Dis. 2003. 26(8):745-59. [QxMD ... Homocysteine is readily oxidized in plasma to form homocystine- and homocysteine-mixed disulfides. This oxidation has been ... Homocysteine has been found to induce neurological dysfunction via oxidative stress. The cytotoxicity of homocysteine has been ...

https://emedicine.staging.medscape.com/article/1115062-overview

Vitamin B12 and homocysteine levels and 6-year change in peripheral nerve function and neurological signs. J Gerontol A Biol ... TS = thymidylate synthase, DHFR = dihydrofolate reductase, SHMT = serine methyl-transferase. View Media Gallery ... Vitamin B12 and homocysteine levels and 6-year change in peripheral nerve function and neurological signs. J Gerontol A Biol ... Diaz-Arrastia R. Homocysteine and neurologic disease. Arch Neurol. 2000 Oct. 57(10):1422-7. [QxMD MEDLINE Link]. ...

https://www.staging.medscape.com/answers/1152670-77131/how-does-the-prevalence-of-vitamin-b-12-related-neurological-disorders-vary-among-males-and-females

Homocysteine-methyl tetrahydrofolate methyltransferase. *METH_HUMAN. *Methionine Synthase. *Tetrahydropteroylglutamate ... Some of the excess homocysteine is excreted in urine. Researchers have not determined how altered levels of homocysteine and ... Without functional methionine synthase, homocysteine cannot be converted to methionine. As a result, homocysteine builds up in ... Carmel R, Green R, Rosenblatt DS, Watkins D. Update on cobalamin, folate, and homocysteine. Hematology Am Soc Hematol Educ ...

https://medlineplus.gov/genetics/gene/mtr/

5-Methyltetrahydrofolate-homocysteine methyltransferase gene polymorphism (MTR) and risk of head and neck cancer. Brazilian ... 5): 445-50. Galbiatti A L S, Ruiz M T, Biselli-Chicote P M, Chicote-Biselli P M, Raposo L S, Maniglia J V, Pavarino-Bertelli E ... 5): 1188-93. Zhang Zhengdong, Shi Qiuling, Liu Zhensheng, Sturgis Erich M, Spitz Margaret R, Wei Qing ...

https://phgkb.cdc.gov/PHGKB/searchSummary.action?firstQuery=Carcinoma and MTR&Mysubmit=search

https://www.staging.medscape.com/answers/1152670-77122/what-is-the-structure-of-vitamin-b-12

https://www.medscape.com/answers/1152670-77122/what-is-the-structure-of-vitamin-b-12

Cbl G is due to a defect in methyltetrahydrofolate homocysteine methyltransferase located on chromosome arm 1q43. ... Cbl C is a combined deficiency of methylmalonyl CoA mutase and homocysteine:methyltetrahydrofolate methyltransferase. Patients ... Vitamin B12 and homocysteine levels and 6-year change in peripheral nerve function and neurological signs. J Gerontol A Biol ... Vitamin B12 and homocysteine levels and 6-year change in peripheral nerve function and neurological signs. J Gerontol A Biol ...

https://emedicine.medscape.com/article/1152670-clinical

Vitamin B12 metabolic defect with combined deficiency of methylmalonyl-coA mutase and homocysteine:methyltetrahydrofolate ... methyltransferase. *Vitamin B12 metabolic defect with combined deficiency of methylmalonyl-coA mutase and methionine synthase ... As a result, homocysteine builds up in the bloodstream and methionine is depleted. Some of the excess homocysteine is excreted ... MeCbl is also a cofactor, but for another enzyme that converts the amino acid homocysteine to another amino acid, methionine. ...

https://medlineplus.gov/genetics/condition/methylmalonic-acidemia-with-homocystinuria/

Site-specific methyltransferase (cytosine-specific) (substance) {1978009 , SNOMED-CT } Thetin-homocysteine methyltransferase ( ... Arylamine N-methyltransferase (substance) {46566007 , SNOMED-CT } Betaine-homocysteine methyltransferase (substance) {52442007 ... Histone-lysine methyltransferase (substance) {71437001 , SNOMED-CT } Homocysteine methyltransferase (substance) {8473001 , ... Fatty-acid methyltransferase (substance) {6172005 , SNOMED-CT } Glycine methyltransferase (substance) {63664001 , SNOMED-CT } ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=130055001

FAM82A is a hypothetical protein that lies immediately 5′ of CYP1B1. This variant may be an intronic polymorphism of FAM82A or ...

https://www.cdc.gov/genomics/population/genvar/genetic_variants_t1.htm

https://medlineplus.gov/genetics/gene/mtr/

Methyltransferase Arakawas syndrome II Betaine-homocysteine S-methyltransferase GRCh38: Ensembl release 89: ENSG00000116984 - ... "Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, ... The cob-independent MetE consists of two TIM-barrel domains that bind homocysteine and N5-MeTHF individually. The two domains ... March 2003). "Homocysteine remethylation enzyme polymorphisms and increased risks for neural tube defects". Molecular Genetics ...

https://en.wikipedia.org/wiki/Methionine_synthase

In addition, alcohol significantly inhibited hepatic methionine synthase activity and increased homocysteine excretion in urine ...

https://pubmed.ncbi.nlm.nih.gov/10456581/?dopt=Abstract

Synonyms: 5-aminolevulinate synthase, succinyl-CoA: glycine C-succinyl transferase, Alas-1, ALAS-N ...

https://www.mmrrc.org/catalog/sds.php?mmrrc_id=41626

... homocysteine methyltransferase. 34. SEQF2445,KE952623.1. ERH26101.1 jb [NA] [AA] 1185/394. 11928-13112. lipoprotein releasing ... RNA methyltransferase%2C TrmH family%2C group 1. 168. SEQF2445,KE952621.1. ERH26343.1 jb [NA] [AA] 483/160. 30404-30886. iron- ... methyltransferase small domain protein. 180. SEQF2445,KE952621.1. ERH26355.1 jb [NA] [AA] 918/305. 44960-44043. formate ... methyltransferase domain protein. 194. SEQF2445,KE952620.1. ERH26380.1 jb [NA] [AA] 1980/659. 44516-42537. exodeoxyribonuclease ...

https://homd.org/genome/explorer?gid=SEQF2445&anno=ncbi

Chang, C. C., Yang, K. H., Liu, Y. C. & Hsu, T. C., May 1 2012, In: Colloids and Surfaces B: Biointerfaces. 93, p. 169-173 5 p. ... Li, S. C., Huang, C. H. & Hung, K. L., Jun 2007, In: Human Genetics. 121, 5, p. 647 1 p.. Research output: Contribution to ... Hu, X. P., Wu, M. Y. & Liu, J. F., Oct 1997, In: Journal of the American College of Nutrition. 16, 5, p. 439-442 4 p.. Research ... Chang, H. P., Huang, S. Y. & Chen, Y. H., Apr 6 2005, In: Journal of Agricultural and Food Chemistry. 53, 7, p. 2530-2534 5 p. ...

https://tmu.pure.elsevier.com/en/organisations/school-of-nutrition-and-health-sciences-2/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&ordering=type&descending=true&page=16

Homocysteine-methyl tetrahydrofolate methyltransferase Current Synonym true false 3721747017 5-methyltetrahydrofolate- ... Substance with methyltransferase mechanism of action (substance) {130055001 , SNOMED-CT } Substance with transferase mechanism ... 5-Methyltetrahydrofolate-homocysteine methyltransferase Current Synonym true false 20876015 Methionine synthase Current Synonym ... 5-methyltetrahydrofolate-homocysteine methyltransferase (substance). Code System Preferred Concept Name. 5- ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=12117006

https://en.wikipedia.org/wiki/5-Methyltetrahydropteroyltriglutamate%E2%80%94homocysteine_S-methyltransferase

5 Untranslated Regions. S. R McIsaac, Gibney, P. A., Chandran, S. S., Benjamin, K. R., and Botstein, D., "Synthetic biology ... 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase. S. R McIsaac, Petti, A. A., Bussemaker, H. J., and Botstein, D., " ...

https://lsi.princeton.edu/research/publications?page=7&s=keyword&o=asc&f%5Bauthor%5D=89

https://phgkb.cdc.gov/PHGKB/searchSummary.action?firstQuery=Carcinoma+and+MTR&Mysubmit=search

Akagi, R., 1993, In: 美育文化. 43, 5, p. 50-57 8 p.. Research output: Contribution to journal › Article ... Kawata, T., 1992, In: ビタミン. 66, 8, p. 451-455 5 p.. Research output: Contribution to journal › Article ... 39-43 5 p.. Research output: Contribution to journal › Article › peer-review ...

https://okayama.pure.elsevier.com/en/organisations/faculty-of-education/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&ordering=publicationYearThenTitle&descending=true&page=63

Catechol-O-methyl transferase ‎]] #[[Chromosome 15q partial deletion ‎]] #[[Clavulanic acid ‎]] #[[Collaborative Hypertext of ... Homocysteine ‎]] #[[Homologous series ‎]] #[[ICD-10 Chapter K ‎]] #[[Cementum ‎]] #[[Chronic stable angina historical ... 5-Methoxy-diisopropyltryptamine ‎]] #[[ATC code M02 ‎]] #[[Accessory breast ‎]] #[[American College of Cardiology ‎]] #[[ ... 5-alpha reductase ‎]] #[[Adductor pollicis muscle ‎]] #[[Alcohol abuse ‎]] #[[Allylamine ‎]] #[[Analysis of covariance ‎]] #[[ ...

https://www.wikidoc.org/index.php?title=Static_popular_pages_list&action=edit

Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). This gene encodes the 5- ... methyltetrahydrofolate-homocysteine methyltransferase. This enzyme, also known as cobalamin-dependent methionine synthase, ... Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and ... Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and ...

https://pharos.nih.gov/targets/Q99707

Control cells were able to grow in deficient medium supplied with homocysteine, cobalamin and folate, while mutant cells were ... Control cells were able to grow in deficient medium supplied with homocysteine, cobalamin and folate, while mutant cells were ... Control cells were able to grow in deficient medium supplied with homocysteine, cobalamin and folate, while mutant cells were ... Control cells were able to grow in deficient medium supplied with homocysteine, cobalamin and folate, while mutant cells were ...

https://mayoclinic.pure.elsevier.com/en/publications/methionine-auxotrophy-in-inborn-errors-of-cobalamin-metabolism

TRM1 tRNA methyltransferase 1-like. 0.037. PLK1S1. polo-like kinase 1 substrate 1. 0.036. ...

http://imp.princeton.edu/predictions/process/human-context-global/3143/?gene=20319

... homocysteine methyltransferase; methylenetetrahydrofolate reductase; betaine, homocysteine methyltransferase; choline dehydro- ... Across three arms, 5 mg and 10 mg of ulipristal achieved outcomes at least as good, or better, than leuprolide for control of ... Finally Pray the prayer of faith with me, Father, I have a covenant of divine therapeutic with You (Isaiah 53 v 5). A: Tumor ... Perkembangan tajam penglihatan dari 20/200 (6/60) hinga 20/20 (6/6), yaitu pada saat lahir sampai usia three вЂ" 5 tahun. Se ...

https://nialmed.com/category/services-show/

Hua Tao Meng, Peter G. Shields, Jing Nie, Catalin Marian, Christine B. Ambrosone, Susan E. McCann, Mary Platek, Shiva S. Krishnan, Bin Xie, Stephen B. Edge, Janet Winston, Dominica Vito, Maurizio Trevisan, Jo L. Freudenheim ...

https://experts.unthsc.edu/en/publications/dna-promoter-methylation-in-breast-tumors-no-association-with-gen/fingerprints/

Click on a genes description to view its network relationships with genes known to be involved in "regulation of mitotic sister chromatid segregation" ...

http://imp.princeton.edu/predictions/process/rat-context-global/259/?gene=108004

5-methyltetrahydrofolate-homocysteine methyltransferase Previous and unofficial names. cblG , cobalamin-dependent methionine ...

https://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=1027

Levels of key enzymes of methionine-homocysteine metabolism in preeclampsia. Alejandra Pérez-Sepúlveda, Pedro P. España-Perrot ... Levels of key enzymes of methionine-homocysteine metabolism in preeclampsia. En: BioMed Research International. 2013 ; Vol. ... Levels of key enzymes of methionine-homocysteine metabolism in preeclampsia. BioMed Research International. 2013;2013. 731962. ... To evaluate the role of key enzymes in the methionine- homocysteine metabolism (MHM) in the physiopathology of preeclampsia (PE ...

https://investigadores.uandes.cl/es/publications/levels-of-key-enzymes-of-methionine-homocysteine-metabolism-in-pr-3

Lee, H. C., Ko, H. K., Huang, B. E. T. G., Chu, Y. H. & Huang, S. Y., 2014, In: Food and Function. 5, 5, p. 990-996 7 p.. ... High-dose ferric citrate supplementation attenuates omega-3 polyunsaturated fatty acid biosynthesis via downregulating delta 5 ... 5, p. 2662-2680 19 p.. Research output: Contribution to journal › Article › peer-review ... 117-121 5 p.. Research output: Contribution to journal › Article › peer-review ...

https://tmu.pure.elsevier.com/en/persons/shih-yi-huang/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&ordering=publicationYearThenTitle&descending=true

... methyltetrahydrofolate--homocysteine methyltransferase (EC 2.1.1.13)::Isocitrate dehydrogenase phosphatase /kinase (EC 3.1.3.-) ... methyltransferase (EC 2.1.1.35)::tmRNA (uracil(341)-C5)-methyltransferase::YciL protein::Hemophore HasA outer membrane receptor ... methyltransferase::tRNA (cmo5U34)-methyltransferase::Copper homeostasis protein CutF precursor::Hypothetical protein YaeJ with ... methyltransferase (EC 2.1.1.33)::Fructose-1,6-bisphosphatase, type I (EC 3.1.3.11)::UDP-N-acetylmuramate:L-alanyl-gamma-D- ...

https://www.bv-brc.org/docs/cli_tutorial/cli_clustering.html

... also called N5-methyltetrahydrofolate homocysteine methyltransferase or 5-methyltetrahydropteroyl triglutamate homocysteine ... homocysteine S-methyltransferase, sulfur amino acid metabolism, YMR175W -2.346610 INESSENTIAL SIP18 Salt-Induced Protein of 18 ... homocysteine S-methyltransferase, sulfur amino acid metabolism, YDR474C 1.094095 INESSENTIAL biological_process unknown, ... homocysteine S-methyltransferase, cytosol YKR069W 268.781606 INESSENTIAL MET1 siroheme synthase, methionine metabolism*, ...

https://genomics.lbl.gov/YeastFitnessData/websitefiles/47_minimal-media_sen.txt

... catalyzes methyl group transfer from methyltetrahydrofolate to homocysteine to create methionine using B12 as a cofactor ( ... Galinski EA, Pfeiffer H-P, TrÜPer HG (1985) 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid. Eur J Biochem 149(1):135- ... Ectoine, also known as tetrahydropyrimidine ectoine, and its derivative 5-hydroxyectoine, are widely used as compatible solutes ... Curr Opin Microbiol 10(5):499-503. doi:10.1016/j.mib.2007.08.004 ... Genome Res 18(5):821-829. doi:10.1101/gr.074492.107 Article CAS ...

https://amb-express.springeropen.com/articles/10.1186/s13568-017-0490-2

... gamma 5 subunit AF319526 Gstm2 glutathione S-transferase, mu 2 U96116 Hadh2 hydroxyacyl-Coenzyme A dehydrogenase type II D63663 ... meningioma expressed antigen 5 (hyaluronidase) AK020927 Rdh12 retinol dehydrogenase 12 AB053477 Abtb1 ankyrin repeat and BTB ( ... coiled-coil-helix-coiled-coil-helix domain containing 5 BC027546 Mrps21 mitochondrial ribosomal protein S21 AK028011 Ndufc1 ... 5-methyltetrahydrofolate-homocysteine methyltransferase AY277588 MGI:2668443 retinal short chain dehydrogenase reductase 2 ...

http://www.molvis.org/molvis/v12/a49/medvedovic-table10.html

... homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine ... methyltetrahydrofolate to homocysteine resulting in methionine formation ... homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine ... homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine ...

https://string-db.org/network/287.DR97_3424

A cobalamin-dependent N5-methyltetra-hydrofolate-homocysteine methyltransferase (methyl-transferase) was demonstrated in ... Properties of leukocytes enzymes resembled those of methyltransferases previously studied in bacteria and other animal cells. ... After 5-FU administration, levels of FdUMP reached a dose-dependent peak within 6 h in the ascites tumor and in bone marrow, ... The enzyme, 5-nucleotidase (5N) (E.C.-3.1.3.5) is present in lymphocytes isolated from the blood of normal subjects. This ...

https://www.jci.org/56/5

To evaluate the role of key enzymes in the methionine- homocysteine metabolism (MHM) in the physiopathology of preeclampsia (PE). (uandes.cl)
Properties of leukocytes enzymes resembled those of methyltransferases previously studied in bacteria and other animal cells. (jci.org)

Both the cobalamin-dependent and cobalamin-independent forms of the enzyme carry out the same overall chemical reaction, the transfer of a methyl group from 5-methyltetrahydrofolate (N5-MeTHF) to homocysteine, yielding tetrahydrofolate (THF) and methionine. (wikipedia.org)
The remethylation pathway comprises 2 intersecting biochemical pathways and results in the transfer of a methyl group (CH3) to homocysteine from methylcobalamin, which receives its methyl group from S-adenosylmethionine (SAM), from 5-methyltetrahydrofolate (an active form of folic acid), or from betaine (trimethylglycine). (medscape.com)
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. (nih.gov)

In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). (wikipedia.org)
5-Methyltetrahydrofolate-homocysteine methyltransferase gene polymorphism (MTR) and risk of head and neck cancer. (cdc.gov)
This gene encodes the 5-methyltetrahydrofolate-homocysteine methyltransferase. (nih.gov)
Two common mutations in the MTHFR gene (C677T and A1298C) may contribute to increased levels of homocysteine, a known risk factor for heart disease, atherosclerosis 2 and venous thrombosis. (jahealthadvocate.com)

When in the Cob(I) form, the enzyme-bound cofactor is now able to abstract a methyl group from activated 5-methyltetrahydrofolate (N5-MeTHF), yielding tetrahydrofolate (THF) and regenerating the methylcoalamin form of the enzyme. (wikipedia.org)
Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli" (Free full text). (wikipedia.org)

DL-homocysteine inhibits the production of tyrosinase, which is the major pigment enzyme. (medscape.com)
In enzymology, a 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) is an enzyme that catalyzes the chemical reaction 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine ⇌ {\displaystyle \rightleftharpoons } tetrahydropteroyltri-L-glutamate + L-methionine Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamate and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamate and L-methionine. (wikipedia.org)
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. (wikipedia.org)
The systematic name of this enzyme class is 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase. (wikipedia.org)
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Fatty Acid Transport Protein 5 (FATP5) in Tissue homogenates, cell lysates and other biological fluids. (lotusbiotechnologies.com)
This enzyme is vital for creating 5-methyltetrahydrofolate, an essential substance for converting the amino acid homocysteine into the amino acid methionine. (jahealthadvocate.com)

The cobalamin is then demethylated by zinc-activated thiolate homocysteine, generating methionine and reducing the cofactor to a Cob(I) state. (wikipedia.org)
The mechanism of the cobalamin-independent (MetE) form, by contrast, proceeds through a direct methyl transfer from the activated N5-MeTHF to zinc thiolate homocysteine. (wikipedia.org)
The domains, from N- to C-terminus, are denoted homocysteine binding (Hcy domain), N5-methylTHF binding (MTHF domain) Cobalamin-binding (Cob domain) and the S-adenosymethionine-binding or reactivation domain. (wikipedia.org)
Control cells were able to grow in deficient medium supplied with homocysteine, cobalamin and folate, while mutant cells were not, due to their inability to synthesize methionine from its immediate metabolic precursor, homocysteine. (elsevier.com)
Because vitamin B-12 is highly conserved through the enterohepatic circulation, cobalamin deficiency from malabsorption develops after 2-5 years and deficiency from dietary inadequacy in vegetarians develops after 10-20 years. (medscape.com)
Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate. (expasy.org)
A cobalamin-dependent N5-methyltetra-hydrofolate-homocysteine methyltransferase (methyl-transferase) was demonstrated in unfractioned extracts of human normal and leukemia leukocytes. (jci.org)
Protonation state of methyltetrahydrofolate in a binary complex with cobalamin-dependent methionine synthase. (wikipathways.org)

GapMind does not represent the formation of the methyl donors for methionine synthase, such as 5-methyltetrahydrofolate or methyl corrinoid proteins. (lbl.gov)

Without functional methionine synthase, homocysteine cannot be converted to methionine. (medlineplus.gov)

Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). (nih.gov)

In addition, alcohol significantly inhibited hepatic methionine synthase activity and increased homocysteine excretion in urine. (nih.gov)

The transsulfuration pathway of methionine/homocysteine degradation produces the amino acids cysteine and taurine. (medscape.com)
Cysteine (Cys) is a sulfur-containing amino acid, whereas taurine is a product of Cys oxidation, and homocysteine (Hcy) is a metabolite of methionine (Met), which also serves as a precursor of Cys sulfur. (basicmedicalkey.com)
Interest in taurine surged following the discovery in 1975 that cats fed diets containing little or no taurine suffered retinal degeneration accompanied by low retinal and plasma taurine concentrations ( 5 ). (basicmedicalkey.com)

Vitamin B6 helps maintain healthy homocysteine levels via conversion to cysteine, which serves as a building block for collagen, keratin, and glutathione. (mindbodygreen.com)
Comment: Transsulfuration is the conversion of homoserine to homocysteine, with the sulfur being obtained from cysteine. (lbl.gov)

The RNA expression of MTHFR and MTR is elevated in placentas of PE patients, highlighting a potential compensation mechanism of the methionine-homocysteine metabolism in the physiopathology of this disease. (uandes.cl)
B12 serves a complementary role with folate in the methionine cycle, as they are both essential cofactors for one-carbon metabolism, optimal homocysteine recycling to methionine, and methylation. (mindbodygreen.com)

Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. (medlineplus.gov)

This pathway is dependent on adequate intake of vitamin B-6 and the hepatic conversion of vitamin B-6 into its active form, pyridoxal-5'-phosphate (P5P). (medscape.com)
VITAMIN B6 Our vitamin B6 is in the bioactive pyridoxal 5'-phosphate form. (mindbodygreen.com)

indicates that the protein contains two domains (at least), one of which performs the role Glutamate 5-kinase and the other which performs the role RNA-binding C-terminal domain PUA . (bv-brc.org)
Description: A sandwich quantitative ELISA assay kit for detection of Human Fatty Acid Transport Protein 5 (FATP5) in samples from tissue homogenates or other biological fluids. (lotusbiotechnologies.com)

In its bioactive form, folic acid is clinically shown to support healthy homocysteine and SAM-e levels to drive optimal methylation in every cell. (mindbodygreen.com)
In fact, high-potency betaine has been clinically shown to support homocysteine reduction and methionine regeneration, ultimately driving methylation function and health. (mindbodygreen.com)

Homocystinuria represents a group of hereditary metabolic disorders characterized by an accumulation of homocysteine in the serum and an increased excretion of homocysteine in the urine. (medscape.com)

Methyltransferases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (childrensmercy.org)

Specifically, methionine synthase carries out a chemical reaction that converts the amino acid homocysteine to another amino acid called methionine. (medlineplus.gov)

Homocysteine is metabolized by means of 2 pathways: remethylation and transsulfuration. (medscape.com)

Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. (wikipathways.org)

Quatrefolic® methylfolate is the fully activated, glucosamine salt form of methylated folic acid (5-MTHF), for optimal absorption and utilization in the body. (mindbodygreen.com)

5,10-methylenetetrahydrofolate reductase [Ensembl]. (ntu.edu.sg)

Simplified picture showing homocysteine involvement in different metabolic pathways, as well as the role of vitamins B-6, B-12, and folate as a co-factors in this pathway. (medscape.com)

The active site lies between the tops of the two barrels, the N-terminal barrel binds 5-methyltetrahydropteroyltri-L-glutamic acid and the C-terminal barrel binds homocysteine. (wikipedia.org)

Table representing the top 5 knowledge attributes in the illumination graph. (nih.gov)
This graph shows the total number of publications written about "Methyltransferases" by people in this website by year, and whether "Methyltransferases" was a major or minor topic of these publications. (childrensmercy.org)

Researchers have not determined how altered levels of homocysteine and methionine lead to the health problems associated with homocystinuria. (medlineplus.gov)
When pyridoxine supplementation was initiated at age 18 years, the patient's plasma homocysteine levels decreased below the reference range. (medscape.com)
At age 50 years, the patient's plasma homocysteine levels still remained low. (medscape.com)
The best solution for elevated levels is getting plenty of natural 5-methyltetrahydrofolate (methylfolate for short). (jahealthadvocate.com)

[ 5 ] In 1926, Minot and Murphy fed PA patients a half-pound of calf liver daily, for which they received the Nobel Prize. (medscape.com)
Total body stores are 2-5 mg, of which half is stored in the liver. (medscape.com)

Checking for elevations of homocysteine and RBC folate in the blood is an indirect way to check for the problem. (jahealthadvocate.com)

Our riboflavin 5'-phosphate is the fully bioactive form of this essential water-soluble micronutrient. (mindbodygreen.com)

S-adenosyl methionine (SAM) and S-adenosyl homocysteine (SAH) were measured in plasma using high-performance liquid chromatography-tandem mass spectrometry (HPLC/MS/MS). The SNP association analysis was carried out using Fisher's exact test. (uandes.cl)

100% diagnostic certainty was reached when all 5 domains were abnormally scored. (frontiersin.org)

Purification and properties of 5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase" (Free full text). (wikipedia.org)

Anatomy7

Organisms3

Diseases10

Chemicals and Drugs87

Analytical, Diagnostic and Therapeutic Techniques and Equipment8

Phenomena and Processes29

Technology, Industry, Agriculture2

Information Science3

Health Care3

Folate and homocysteine metabolism in copper-deficient rats. (1/254)

Co-ordinate variations in methylmalonyl-CoA mutase and methionine synthase, and the cobalamin cofactors in human glioma cells during nitrous oxide exposure and the subsequent recovery phase. (2/254)

Reversal of ethanol-induced hepatic steatosis and lipid peroxidation by taurine: a study in rats. (3/254)

A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium. (4/254)

Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. (5/254)

A polymorphism of the methionine synthase gene: association with plasma folate, vitamin B12, homocyst(e)ine, and colorectal cancer risk. (6/254)

Heterologous high level expression, purification, and enzymological properties of recombinant rat cobalamin-dependent methionine synthase. (7/254)

Characterization and functional expression of cDNAs encoding methionine-sensitive and -insensitive homocysteine S-methyltransferases from Arabidopsis. (8/254)

Tetrahydrofolates

Folic Acid

5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase

Methyltransferases

Folate Receptors, GPI-Anchored

5,10-Methylenetetrahydrofolate Reductase (FADH2)

DNA (Cytosine-5-)-Methyltransferase

Vitamin B 12

Formyltetrahydrofolates

S-Adenosylmethionine

Methylenetetrahydrofolate Reductase (NADPH2)

Pteroylpolyglutamic Acids

Methylation

Hyperhomocysteinemia

Glycine N-Methyltransferase

S-Adenosylhomocysteine

Methionine

Homocysteine

Oxidoreductases Acting on CH-NH Group Donors

Protein Methyltransferases

Reduced Folate Carrier Protein

O(6)-Methylguanine-DNA Methyltransferase

Betaine-Homocysteine S-Methyltransferase

Anemia, Macrocytic

Vitamin B 12 Deficiency

Histone-Lysine N-Methyltransferase

tRNA Methyltransferases

Vitamin B Complex

Methotrexate

Protein-Arginine N-Methyltransferases

Folic Acid Deficiency

Hydroxocobalamin

Corrinoids

DNA-Cytosine Methylases

Leucovorin

Protein D-Aspartate-L-Isoaspartate Methyltransferase

DNA Modification Methylases

Leukemia L1210

Site-Specific DNA-Methyltransferase (Adenine-Specific)

Betaine

Folic Acid Antagonists

DNA Methylation

Cystathionine beta-Synthase

Pterins

Homocystine

Polyglutamic Acid

Dietary Supplements

Folate Receptor 1

Proton-Coupled Folate Transporter

Nitrous Oxide

Carrier Proteins

Pteridines

gamma-Glutamyl Hydrolase

Kinetics

Receptors, Cell Surface

Clostridium

Methylmalonyl-CoA Mutase

Vitamin B 6

Biological Availability

Biological Transport

Chromatography, High Pressure Liquid

Neural Tube Defects

Anemia, Pernicious

Biopterin

Cystathionine

Liver

Molecular Sequence Data

Erythrocytes

Phosphatidylethanolamine N-Methyltransferase

Histones

Genotype

Protein O-Methyltransferase

Guanidinoacetate N-Methyltransferase

Phosphatidyl-N-Methylethanolamine N-Methyltransferase

Homocysteine S-Methyltransferase

Homocystinuria

Acetyl Coenzyme A

Amino Acid Sequence

Mutation

Azacitidine