Aminomethyltransferase: A one-carbon group transferase that transfers lipoamide-linked methylamine groups to tetrahydrofolate (TETRAHYDROFOLATES) to form methylenetetrahydrofolate and AMMONIA. It is one of four components of the glycine decarboxylase complex.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Glycine Decarboxylase Complex H-Protein: A LIPOIC ACID-containing protein that plays the pivotal role in the transfer of methylamine groups and reducing equivalents between the three enzymatic components of the glycine decarboxylase complex.Glycine Dehydrogenase (Decarboxylating): A PYRIDOXAL PHOSPHATE dependent enzyme that catalyzes the decarboxylation of GLYCINE with the transfer of an aminomethyl group to the LIPOIC ACID moiety of the GLYCINE DECARBOXYLASE COMPLEX H-PROTEIN. Defects in P-protein are the cause of non-ketotic hyperglycinemia. It is one of four subunits of the glycine decarboxylase complex.Glycine Decarboxylase Complex: A enzyme complex that catalyzes the oxidative DECARBOXYLATION and DEAMINATION of GLYCINE into CARBON DIOXIDE; AMMONIA; NADH; and N5N10-methylenetetrahydrofolate. It is composed of four different component protein components referred to as H, P, L, and T.Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.Amino Acid Oxidoreductases: A class of enzymes that catalyze oxidation-reduction reactions of amino acids.Hydroxymethyl and Formyl Transferases: Enzymes that catalyze the transfer of hydroxymethyl or formyl groups. EC 2.1.2.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Health Records, Personal: Longitudinal patient-maintained records of individual health history and tools that allow individual control of access.Triose-Phosphate Isomerase: An enzyme that catalyzes reversibly the conversion of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. A deficiency in humans causes nonspherocytic hemolytic disease (ANEMIA, HEMOLYTIC, CONGENITAL NONSPHEROCYTIC). EC 5.3.1.1.Metabolic Networks and Pathways: Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.Molecular Sequence Annotation: The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.Gene Ontology: Sets of structured vocabularies used for describing and categorizing genes, and gene products by their molecular function, involvement in biological processes, and cellular location. These vocabularies and their associations to genes and gene products (Gene Ontology annotations) are generated and curated by the Gene Ontology Consortium.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Transcriptome: The pattern of GENE EXPRESSION at the level of genetic transcription in a specific organism or under specific circumstances in specific cells.Hyperglycinemia, Nonketotic: An autosomal recessive metabolic disorder caused by deficiencies in the mitochondrial GLYCINE cleavage system.Cytophaga: A genus of gram-negative gliding bacteria found in SOIL; HUMUS; and FRESHWATER and marine habitats.Tetrahydrofolates: Compounds based on 5,6,7,8-tetrahydrofolate.Metabolome: The dynamic collection of metabolites which represent a cell's or organism's net metabolic response to current conditions.Metabolomics: The systematic identification and quantitation of all the metabolic products of a cell, tissue, organ, or organism under varying conditions. The METABOLOME of a cell or organism is a dynamic collection of metabolites which represent its net response to current conditions.Canada: The largest country in North America, comprising 10 provinces and three territories. Its capital is Ottawa.Folic Acid: 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.British Columbia: A province of Canada on the Pacific coast. Its capital is Victoria. The name given in 1858 derives from the Columbia River which was named by the American captain Robert Gray for his ship Columbia which in turn was named for Columbus. (From Webster's New Geographical Dictionary, 1988, p178 & Room, Brewer's Dictionary of Names, 1992, p81-2)Genomics: The systematic study of the complete DNA sequences (GENOME) of organisms.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Proto-Oncogene Proteins c-myc: Cellular DNA-binding proteins encoded by the c-myc genes. They are normally involved in nucleic acid metabolism and in mediating the cellular response to growth factors. Elevated and deregulated (constitutive) expression of c-myc proteins can cause tumorigenesis.MEDLINE: The premier bibliographic database of the NATIONAL LIBRARY OF MEDICINE. MEDLINE® (MEDLARS Online) is the primary subset of PUBMED and can be searched on NLM's Web site in PubMed or the NLM Gateway. MEDLINE references are indexed with MEDICAL SUBJECT HEADINGS (MeSH).Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Mitochondrial Proteins: Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.Alternative Splicing: A process whereby multiple RNA transcripts are generated from a single gene. Alternative splicing involves the splicing together of other possible sets of EXONS during the processing of some, but not all, transcripts of the gene. Thus a particular exon may be connected to any one of several alternative exons to form a mature RNA. The alternative forms of mature MESSENGER RNA produce PROTEIN ISOFORMS in which one part of the isoforms is common while the other parts are different.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Software: Sequential operating programs and data which instruct the functioning of a digital computer.One-Carbon Group Transferases: A subclass of transferases that transfer chemical groups containing a single carbon. These include the METHYLTRANSFERASES, the HYDROXYMETHYL AND FORMYL TRANSFERASES, the CARBOXYL AND CARBAMOYL TRANSFERASES, and the AMIDINOTRANSFERASES. EC 2.1.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Barth Syndrome: Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.Tripterygium: A plant genus of the family CELASTRACEAE that is a source of triterpenoids and diterpene epoxides such as triptolide.Medication Adherence: Voluntary cooperation of the patient in taking drugs or medicine as prescribed. This includes timing, dosage, and frequency.
Control of expression of one-carbon metabolism genes of Saccharomyces cerevisiae is mediated by a tetrahydrofolate-responsive protein binding to a glycine regulatory region including a core 5'-CTTCTT-3' motif. (1/33)
Expression of yeast genes involved in one-carbon metabolism is controlled by glycine, by L-methionine, and by nitrogen sources. Here we report a novel control element containing a core CTTCTT motif mediating the glycine response, demonstrating that a protein binds this element, that binding is modulated by tetrahydrofolate, and that folate is required for the in vivo glycine response. In an heterologous CYC1 promoter the region needed for the glycine response of GCV2 (encoding the P-subunit of glycine decarboxylase) mediated repression that was relieved by glycine. It was also responsible for L-methionine control but not nitrogen repression. GCV1 and GCV3 have an homologous region in their promoters. The GCV1 region conferred a glycine response on an heterologous promoter acting as a repressor or activator depending on promoter context. A protein was identified that bound to the glycine regulatory regions of GCV1 and GCV2 only if the CTTCTT motif was intact. This protein protected a 17-base pair CATCN7CTTCTT region of GCV2 that is conserved between GCV1 and GCV2. Protein binding was increased by tetrahydrofolate, and use of a fol1 deletion mutant indicated the involvement of a folate in the in vivo glycine response. Tetrahydrofolate or a derivative may act as a ligand for the transcription factor controlling expression of one-carbon metabolism genes. (+info)Role for the leucine-responsive regulatory protein (Lrp) as a structural protein in regulating the Escherichia coli gcvTHP operon. (2/33)
The Escherichia coli glycine-cleavage enzyme system (gcvTHP and lpd gene products) provides C1 units for cellular methylation reactions. Both the GcvA and leucine-responsive regulatory (Lrp) proteins are required for regulation of the gcv operon. One model proposed for gcv regulation is that Lrp plays a structural role, bending the DNA to allow GcvA to function as either an activator or a repressor in response to environmental signals. This hypothesis was tested by replacing all but the upstream 22 bp of the Lrp-binding region in a gcvT::lacZ fusion with the I1A site from phage lambda. Integration host factor (IHF) binds the I1A site and bends the DNA about 140 degrees. Shifting the I1A site by increments of 1 base around the DNA helix resulted in IHF-dependent activation and repression of gcvT::lacZ expression that were face-of-the-helix dependent. Activation was also dependent on the GcvA protein, and repression was dependent on both the GcvA and GcvR proteins, demonstrating that the roles for these proteins were not altered. The results are consistent with Lrp playing primarily a structural role in gcv regulation, although they do not completely rule out the possibility that Lrp also interacts with another gcv-regulatory protein or with RNA polymerase. (+info)Identification of the folate binding sites on the Escherichia coli T-protein of the glycine cleavage system. (3/33)
T-protein is a component of the glycine cleavage system and catalyzes the tetrahydrofolate-dependent reaction. To determine the folate-binding site on the enzyme, 14C-labeled methylenetetrahydropteroyltetraglutamate (5,10-CH2-H4PteGlu4) was enzymatically synthesized from methylenetetrahydrofolate (5, 10-CH2-H4folate) and [U-14C]glutamic acid and subjected to cross-linking with the recombinant Escherichia coli T-protein using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, a zero-length cross-linker between amino and carboxyl groups. The cross-linked product was digested with lysylendopeptidase, and the resulting peptides were separated by reversed-phase high performance liquid chromatography. Amino acid sequencing of the labeled peptides revealed that three lysine residues at positions 78, 81, and 352 were involved in the cross-linking with polyglutamate moiety of 5, 10-CH2-H4PteGlu4. The comparable experiment with 5,10-CH2-H4folate revealed that Lys-81 and Lys-352 were also involved in cross-linking with the monoglutamate form. Mutants with single or multiple replacement(s) of these lysine residues to glutamic acid were constructed by site-directed mutagenesis and subjected to kinetic analysis. The single mutation of Lys-352 caused similar increase (2-fold) in Km values for both folate substrates, but that of Lys-81 affected greatly the Km value for 5,10-CH2-H4PteGlu4 rather than for 5,10-CH2-H4folate. It is postulated that Lys-352 may serve as the primary binding site to alpha-carboxyl group of the first glutamate residue nearest the p-aminobenzoic acid ring of 5,10-CH2-H4folate and 5,10-CH2-H4PteGlu4, whereas Lys-81 may play a key role to hold the second glutamate residue through binding to alpha-carboxyl group of the second glutamate residue. (+info)The amino-terminal region of the Escherichia coli T-protein of the glycine cleavage system is essential for proper association with H-protein. (4/33)
T-protein is a component of the glycine cleavage system and catalyzes the tetrahydrofolate-dependent reaction. Our previous work on Escherichia coli T-protein (ET) showed that the lack of the N-terminal 16 residues caused a loss of catalytic activity [Okamura-Ikeda, K., Ohmura, Y., Fujiwara, K. and Motokawa, Y. (1993) Eur. J. Biochem. 216, 539-548]. To define the role of the N-terminal region of ET, a series of deletion mutants were constructed by site-directed mutagenesis and expressed in E. coli. Deletions of the N-terminal 4, 7 and 11 residues led to reduction in the activity to 42, 9 and 4%, respectively, relative to the wild-type enzyme (wtET). The mutant with 7-residue deletion (ETDelta7) was purified and analyzed. ETDelta7 exhibited a marked increase in Km (25-fold) for E. coli H-protein (EH) accompanied by a 10-fold decrease in kcat compared with wtET, indicating the importance of the N-terminal region in the interaction with EH. The role of this region in the ET-EH interaction was investigated by cross-linking of wtET-EH or ETDelta7-EH complex with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, a zero-length cross-linker, in the presence of folate substrates. The resulting tripartite cross-linked products were cleaved with lysylendopeptidase and V8 protease. After purification by reversed-phase HPLC, the cross-linked peptides were subjected to Edman sequencing. An intramolecular cross-linking between Asp34 and Lys216 of wtET which was not observed in wtET alone and an intermolecular cross-linking between Lys288 of wtET and Asp-43 of EH were identified. In contrast, no such cross-linking was detected from the cross-linked product of ETDelta7. These results suggest that EH, when it interacts with ET, causes a change in conformation of ET and that the N-terminal region of ET is essential for the conformational change leading to the proper interaction with EH. (+info)Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae. (5/33)
One-carbon metabolism in yeast is an essential process that relies on at least one of three one-carbon donor molecules: serine, glycine, or formate. By a combination of genetics and biochemistry we have shown how cells regulate the balance of one-carbon flow between the donors by regulating cytoplasmic serine hydroxymethyltransferase activity in a side reaction occurring in the presence of excess glycine. This control governs the level of 5,10-methylene tetrahydrofolate (5,10-CH(2)-H(4)folate) in the cytoplasm, which has a direct role in signaling transcriptional control of the expression of key genes, particularly those encoding the unique components of the glycine decarboxylase complex (GCV1, GCV2, and GCV3). Based on these and other observations, we propose a model for how cells balance the need to supplement their one-carbon pools when charged folates are limiting or when glycine is in excess. We also propose that under normal conditions, cytoplasmic 5,10-CH(2)-H(4)folate is mainly directed to generating methyl groups via methionine, whereas one-carbon units generated from glycine in mitochondria are more directed to purine biosynthesis. When glycine is in excess, 5, 10-CH(2)-H(4)folate is decreased, and the regulation loop shifts the balance of generation of one-carbon units into the mitochondrion. (+info)Nitrite reductase gene enrichment improves assimilation of NO(2) in Arabidopsis. (6/33)
Transgenic plants of Arabidopsis bearing the spinach (Spinacia oleracea) nitrite reductase (NiR, EC 1.7.7.1) gene that catalyzes the six-electron reduction of nitrite to ammonium in the second step of the nitrate assimilation pathway were produced by use of the cauliflower mosaic virus 35S promoter and nopaline synthase terminator. Integration of the gene was confirmed by a genomic polymerase chain reaction (PCR) and Southern-blot analysis; its expression by a reverse transcriptase-PCR and two-dimensional polyacrylamide gel electrophoresis western-blot analysis; total (spinach + Arabidopsis) NiR mRNA content by a competitive reverse transcriptase-PCR; localization of NiR activity (NiRA) in the chloroplast by fractionation analysis; and NO(2) assimilation by analysis of the reduced nitrogen derived from NO(2) (NO(2)-RN). Twelve independent transgenic plant lines were characterized in depth. Three positive correlations were found for NiR gene expression; between the total NiR mRNA and total NiR protein contents (r = 0.74), between the total NiR protein and NiRA (r = 0.71), and between NiRA and NO(2)-RN (r = 0.65). Of these twelve lines, four had significantly higher NiRA than the wild-type control (P < 0.01), and three had significantly higher NO(2)-RN (P < 0.01). Each of the latter three had one to two copies of spinach NiR cDNA per haploid genome. The NiR flux control coefficient for NO(2) assimilation was estimated to be about 0.4. A similar value was obtained for an NiR antisense tobacco (Nicotiana tabacum cv Xanthi XHFD8). The flux control coefficients of nitrate reductase and glutamine synthetase were much smaller than this value. Together, these findings indicate that NiR is a controlling enzyme in NO(2) assimilation by plants. (+info)Effects of breed, parity, and folic Acid supplement on the expression of folate metabolism genes in endometrial and embryonic tissues from sows in early pregnancy. (7/33)
Folic acid and glycine are factors of great importance in early gestation. In sows, folic acid supplement can increase litter size through a decrease in embryonic mortality, while glycine, the most abundant amino acid in the sow oviduct, uterine, and allantoic fluids, is reported to act as an organic osmoregulator. In this study, we report the characterization of cytoplasmic serine hydroxymethyltransferase (cSHMT), T-protein, and vT-protein (variant T-protein) mRNA expression levels in endometrial and embryonic tissues in gestating sows on Day 25 of gestation according to the breed, parity, and folic acid + glycine supplementation. Expression levels of cSHMT, T-protein, and vT-protein mRNA in endometrial and embryonic tissues were performed using semiquantitative reverse transcription-polymerase chain reaction. We also report, for the first time, an alternative splicing event in the porcine T-protein gene. Results showed that a T-protein splice variant, vT-protein, is present in all the tested sow populations. Further characterizations revealed that this T-protein splice variant contains a coding intron that can adopt a secondary structure. Results demonstrated that cSHMT mRNA expression levels were significantly higher in sows receiving the folic acid + glycine supplementation, independently of the breed or parity and in both endometrial and embryonic tissues. Upon receiving the same treatment, the vT-protein and T-protein mRNA expression levels were significantly reduced in the endometrial tissue of Yorkshire-Landrace sows only. These results indicate that modulation of specific gene expression levels in endometrial and embryonic tissues of sows in early gestation could be one of the mechanism involved with the role of folic acid on improving swine reproduction traits. (+info)Probing the H-protein-induced conformational change and the function of the N-terminal region of Escherichia coli T-protein of the glycine cleavage system by limited proteolysis. (8/33)
T-protein, a component of the glycine cleavage system, catalyzes a tetrahydrofolate-dependent reaction. Previously, we reported a conformational change of Escherichia coli T-protein upon interacting with E. coli H-protein (EH), showing an important role for the N-terminal region of the T-protein in the interaction. To further investigate the T-protein catalysis, the wild type (ET) and mutants were subjected to limited proteolysis. ET was favorably cleaved at Lys(81), Lys(154), Lys(288), and Lys(360) by lysylendopeptidase and the cleavages at Lys(81) and Lys(288) were strongly prevented by EH. Although ET was highly resistant to trypsinolysis, the mutant with an N-terminal 7-residue deletion (ETDelta7) was quite susceptible and instantly cleaved at Arg(16) accompanied by the rapid degradation of the resulting C-terminal fragment, indicating that the cleavage at Arg(16) is the trigger for the C-terminal fragmentation. EH showed no protection from the N-terminal cleavage, although substantial protection from the C-terminal fragmentation was observed. The replacement of Leu(6) of ET with alanine resulted in a similar sensitivity to trypsin as ETDelta7. These results suggest that the N-terminal region of ET functions as a molecular "hasp" to hold ET in the compact form required for the proper association with EH. Leu(6) seems to play a central role in the hasp function. Interestingly, Lys(360) of ET was susceptible to proteolysis even after the stabilization of the entire molecule of ET by EH, indicating its location at the surface of the ET-EH complex. Together with the buried position of Lys(81) in the complex and previous results on folate binding sites, these results suggest the formation of a folate-binding cavity via the interaction of ET with EH. The polyglutamyl tail of the folate substrate may be inserted into the bosom of the cavity leaving the pteridine ring near the entrance of the cavity in the context of the catalytic reaction. (+info)Glycine cleavage T-protein, Aminomethyltransferase folate-binding domain. crystal structure of a component of glycine cleavage ...
... a tetrahydrofolate-requiring aminomethyltransferase enzyme), and L protein (a lipoamide dehydrogenase). The H protein shuttles ...
... may refer to: Alpha-Methyltryptamine (αMT), a synthetic psychedelic of the tryptamine family Aminomethyltransferase, gene ...
... aminomethyltransferase EC 2.1.2.11: 3-methyl-2-oxobutanoate hydroxymethyltransferase EC 2.1.2.12: now EC 2.1.1.74 EC 2.1.2.13: ...
... aminomethyltransferase MeSH D08.811.600.391.150 --- dihydrolipoamide dehydrogenase MeSH D08.811.600.391.175 --- glycine ... aminomethyltransferase MeSH D08.811.913.555.400.300 --- glutamate formimidoyltransferase MeSH D08.811.913.555.400.500 --- ...
... aminomethyltransferase MeSH D05.500.562.452.150 --- dihydrolipoamide dehydrogenase MeSH D05.500.562.452.175 --- glycine ...
... is an enzyme that catabolizes the creation of methylenetetrahydrofolate. It is part of the glycine ...
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazole-carb oxamide N-formyltransferase. Other names in common use include: ...
m6A and m4C methyltransferases are found primarily in prokaryotes (although recent evidence has suggested that m6A is abundant in eukaryotes[1]). m5C methyltransfereases are found in some lower eukaryotes, in most higher plants, and in animals beginning with the echinoderms. The m6A methyltransferases (N-6 adenine-specific DNA methylase) (A-Mtase) are enzymes that specifically methylate the amino group at the C-6 position of adenines in DNA. They are found in the three existing types of bacterial restriction-modification systems (in type I system the A-Mtase is the product of the hsdM gene, and in type III it is the product of the mod gene). These enzymes are responsible for the methylation of specific DNA sequences in order to prevent the host from digesting its own genome via its restriction enzymes. These methylases have the same sequence specificity as their corresponding restriction enzymes. These enzymes contain a conserved motif Asp/Asn-Pro-Pro-Tyr/Phe in their N-terminal section, this ...
Measurement of TPMT activity is encouraged prior to commencing the treatment of patients with thiopurine drugs such as azathioprine, 6-mercaptopurine and 6-thioguanine. Patients with low activity (10% prevalence) or especially absent activity (prevalence 0.3%) are at a heightened risk of drug-induced bone marrow toxicity due to accumulation of the unmetabolised drug. Reuther et al. found that about 5% of all thiopurine therapies will fail due to toxicity. This intolerant group could be anticipated by routine measurement of TPMT activity. There appears to be a great deal of variation in TPMT mutation, with ethnic differences in mutation types accounting for variable responses to 6MP.[9][12] Genetic variants of TPMT have also been associated with cisplatin-induced ototoxicity in children.[13] TPMT is now listed as a pharmacogenomic biomarker for adverse drug reactions to cisplatin by the FDA.[14] ...
Glycine cleavage T-protein, Aminomethyltransferase folate-binding domain. crystal structure of a component of glycine cleavage ...
AMT: aminomethyltransferase. *ANK1: ankyrin 1. *ANK2: ankyrin 2. *ANKH: ANKH inorganic pyrophosphate transport regulator ...
Aminomethyltransferase is an enzyme that catabolizes the creation of methylenetetrahydrofolate. It is part of the glycine ...
Rabbit polyclonal Aminomethyltransferase antibody validated for WB, ELISA and tested in Human. Immunogen corresponding to ... Anti-Aminomethyltransferase antibody (ab76387) at 1 µg/ml + Human fetal lung lysate at 10 µg. Secondary. HRP-conjugated anti- ... corresponding to amino acids 2-51 of Human Aminomethyltransferase ...
Recombinant Protein and Aminomethyltransferase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Aminomethyltransferase. Aminomethyltransferase ELISA Kit. Aminomethyltransferase Recombinant. Aminomethyltransferase Antibody. ... Also known as Aminomethyltransferase (Glycine cleavage system T protein).. The glycine cleavage system catalyzes the ... Below are the list of possible Aminomethyltransferase products. If you cannot find the target and/or product is not available ...
Anti-Aminomethyltransferase Mouse Monoclonal Antibody [clone: 6F4]. Anti-Aminomethyltransferase Mouse Monoclonal Antibody [ ... The Aminomethyltransferase Antibody (6F4) from Novus Biologicals is a mouse monoclonal antibody to Aminomethyltransferase. This ... The Aminomethyltransferase Antibody (6F4) has been validated for the following applications: Western Blot, Immunohistochemistry ... Antigen: Aminomethyltransferase. Clonality: Monoclonal. Clone: 6F4. Conjugation: Unconjugated. Epitope: Host: Mouse. Isotype: ...
Canine Aminomethyltransferase(AMT)ELISA Kit \ 201-15-0069 for more molecular products just contact us ... Index / Sunred / Canine Aminomethyltransferase(AMT)ELISA Kit / Product Detail : 201-15-0069 Canine Aminomethyltransferase(AMT) ... Canine Aminomethyltransferase(AMT)ELISA Kit is an ELISA kit which is manufactured by highest quality antibodies and plates to ... We have also other products like : Canine Aminomethyltransferase(AMT)ELISA Kit. Related products : Canine ...
View all domain architectures containing the Aminomethyltransferase beta-barrel domain domain in Metallosphaera sedula ... Aminomethyltransferase beta-barrel domain superfamily assignments to Metallosphaera sedula DSM 5348. Click on the pictures ... Home > Genomes > Metallosphaera sedula DSM 5348 > Aminomethyltransferase beta-barrel domain > View all domain architectures ...
AMT: aminomethyltransferase. *ANK1: ankyrin 1. *ANK2: ankyrin 2. *ANKH: ANKH inorganic pyrophosphate transport regulator ...
Background De novo assembly of RNA-seq data allows the study of transcriptome in absence of a reference genome either if data is obtained from a single organism or from a mixed sample as in...
The AMT gene provides instructions for making an enzyme called aminomethyltransferase. Learn about this gene and related health ... The AMT gene provides instructions for making an enzyme called aminomethyltransferase. This protein is one of four enzymes that ... AMT gene mutations alter the structure and function of aminomethyltransferase. When an altered version of this enzyme is ... Most of these genetic changes alter single amino acids in aminomethyltransferase. Other mutations delete genetic material from ...
Aminomethyltransferase, folate-binding domain. IPR006222PF01571. 285-361. Glycine cleavage T-protein, C-terminal barrel domain ... Aminomethyltransferase. Pectobacterium carotovorum subsp carotovorum (strain PC1) ...
Similar to Aminomethyltransferase. 44.3. 8.53. 7. 19. 48. gi,115477148. Serine-glyoxylate aminotransaminase. 44.4. 8.19. 4. 18 ...
Aminomethyltransferase. Formyl-THF deformylase. Methenyl-THF cyclohydrolase. Formimino-THF cyclodeaminase. 5-Formyl-THF cyclo- ...
aminomethyltransferase activity Catalysis of the reaction: protein-S-aminomethyldihydrolipoyllysine + tetrahydrofolate = ...
Aminomethyltransferase, folate-binding domain (IPR006222) Pfam signature: PF01571 Bromovirus movement protein (IPR002538) Pfam ...
gcvT; aminomethyltransferase [KO:K00605] [EC:2.1.2.10]. TREPR_3835 dihydrolipoyl dehydrogenase [KO:K00382] [EC:1.8.1.4] ...
aminomethyltransferase [KO:K00605] [EC:2.1.2.10]. Daro_2857 dihydrolipoamide dehydrogenase [KO:K00382] [EC:1.8.1.4] ...
Gene Ontology (GO) annotations related to this gene include enzyme binding and aminomethyltransferase activity. An important ...
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Aminomethyltransferase. NM_001013814. Gene Info. Apoe. Apolipoprotein E. NM_009696. Gene Info. ...
Aminomethyltransferase activity. Specific Function. The glycine cleavage system catalyzes the degradation of glycine. The H ...
Urea carboxylase-related aminomethyltransferase. 11.1. ND. I35_7285. BCAS0271. Urea carboxylase-related aminomethyltransferase ...
Aminomethyltransferase, mitochondrial. P48728 AMT. 3p21.2-p21.1. Enzyme. Not Available. HMDBP00790. Dihydrofolate reductase. ...
- The glycine cleavage system T protein (GcvT) is also known as aminomethyltransferase (EC 2.1.2.10). (jcvi.org)
- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. (creative-enzymes.com)
- This superfamily represents a beta-barrel domain found at the C-terminal of the glycine cleavage T-protein (aminomethyltransferase) [ PMID: 15609340 ] and in tRNA-modifying protein YgfZ. (ebi.ac.uk)
- Also known as Aminomethyltransferase (Glycine cleavage system T protein). (mybiosource.com)
- this protein), T protein (a tetrahydrofolate-requiring aminomethyltransferase enzyme), and L protein (a lipoamide dehydrogenase). (wikipedia.org)
- However, in contrast to dimethylglycine oxidase and T-protein, the YgfZ family lacks amino acid conservation at the folate site, which implies that YgfZ is not an aminomethyltransferase but is likely a folate-dependent regulatory protein involved in one-carbon metabolism. (rcsb.org)
- The crystal structures of aminomethyltransferase (T-protein), YgfZ and TrmE all reveal similar THF-binding folds despite little similarity in sequence or function. (biochemsoctrans.org)
- Data indicate no mutation was found in glycine cleavage system protein-H (show GCSH Proteins ) ( GCSH (show GCSH Proteins )) and suggest that mutations in both glycine decarboxylase (GLDC ) and aminomethyltransferase (AMT (show AMT Proteins )) are the main cause of glycine encephalopathy in Malaysian population. (antibodies-online.com)
- The Aminomethyltransferase Antibody (6F4) from Novus Biologicals is a mouse monoclonal antibody to Aminomethyltransferase. (vwr.com)
- The Aminomethyltransferase Antibody (6F4) has been validated for the following applications: Western Blot, Immunohistochemistry. (vwr.com)
- Canine Aminomethyltransferase(AMT)ELISA Kit is an ELISA kit which is manufactured by highest quality antibodies and plates to provide you with excellent and reproducible results in your work. (antibody-antibodies.com)
- Other mutations delete genetic material from the AMT gene or disrupt how genetic information from the gene is spliced together to make a blueprint for producing aminomethyltransferase. (medlineplus.gov)
- AMT gene mutations alter the structure and function of aminomethyltransferase. (medlineplus.gov)
- Most of these genetic changes alter single amino acids in aminomethyltransferase. (medlineplus.gov)
- Crystal Structure of the Probable Aminomethyltransferase from Bacillus subtilis. (burnham.org)
- Below are the list of possible Aminomethyltransferase products. (mybiosource.com)