Phenylethanolamine N-Methyltransferase
Glycine N-Methyltransferase
Epinephrine
The active sympathomimetic hormone from the ADRENAL MEDULLA. It stimulates both the alpha- and beta- adrenergic systems, causes systemic VASOCONSTRICTION and gastrointestinal relaxation, stimulates the HEART, and dilates BRONCHI and cerebral vessels. It is used in ASTHMA and CARDIAC FAILURE and to delay absorption of local ANESTHETICS.
Adrenal Medulla
The inner portion of the adrenal gland. Derived from ECTODERM, adrenal medulla consists mainly of CHROMAFFIN CELLS that produces and stores a number of NEUROTRANSMITTERS, mainly adrenaline (EPINEPHRINE) and NOREPINEPHRINE. The activity of the adrenal medulla is regulated by the SYMPATHETIC NERVOUS SYSTEM.
Tetrahydroisoquinolines
Planarians
Stem Cells
Epidermis
The external, nonvascular layer of the skin. It is made up, from within outward, of five layers of EPITHELIUM: (1) basal layer (stratum basale epidermidis); (2) spinous layer (stratum spinosum epidermidis); (3) granular layer (stratum granulosum epidermidis); (4) clear layer (stratum lucidum epidermidis); and (5) horny layer (stratum corneum epidermidis).
Cell Differentiation
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.
Nucleic Acids
RNA Nucleotidyltransferases
Gene Library
Harmine
Alkaloid isolated from seeds of Peganum harmala L., Zygophyllaceae. It is identical to banisterine, or telepathine, from Banisteria caapi and is one of the active ingredients of hallucinogenic drinks made in the western Amazon region from related plants. It has no therapeutic use, but (as banisterine) was hailed as a cure for postencephalitic Parkinson disease in the 1920's.
Oligonucleotides
Catechol O-Methyltransferase
Monoamine Oxidase
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4.
Norepinephrine
Precursor of epinephrine that is secreted by the adrenal medulla and is a widespread central and autonomic neurotransmitter. Norepinephrine is the principal transmitter of most postganglionic sympathetic fibers and of the diffuse projection system in the brain arising from the locus ceruleus. It is also found in plants and is used pharmacologically as a sympathomimetic.
Transferases
Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.
Glutathione Transferase
Ornithine Carbamoyltransferase
Ornithine Carbamoyltransferase Deficiency Disease
An inherited urea cycle disorder associated with deficiency of the enzyme ORNITHINE CARBAMOYLTRANSFERASE, transmitted as an X-linked trait and featuring elevations of amino acids and ammonia in the serum. Clinical features, which are more prominent in males, include seizures, behavioral alterations, episodic vomiting, lethargy, and coma. (Menkes, Textbook of Child Neurology, 5th ed, pp49-50)
Ornithine Decarboxylase
Aspartate Carbamoyltransferase
Carbamyl Phosphate
Carboxyl and Carbamoyl Transferases
Irritable Bowel Syndrome
Short Bowel Syndrome
Colonic Diseases, Functional
Sick Building Syndrome
A group of symptoms that are two- to three-fold more common in those who work in large, energy-efficient buildings, associated with an increased frequency of headaches, lethargy, and dry skin. Clinical manifestations include hypersensitivity pneumonitis (ALVEOLITIS, EXTRINSIC ALLERGIC); allergic rhinitis (RHINITIS, ALLERGIC, PERENNIAL); ASTHMA; infections, skin eruptions, and mucous membrane irritation syndromes. Current usage tends to be less restrictive with regard to the type of building and delineation of complaints. (From Segen, Dictionary of Modern Medicine, 1992)
Isolation and characterization of the gene coding for the amidinotransferase involved in the biosynthesis of phaseolotoxin in Pseudomonas syringae pv. phaseolicola. (1/58)
Pseudomonas syringae pv. phaseolicola is the causal agent of the "halo blight" disease of beans. A key component in the development of the disease is a nonhost-specific toxin, Ndelta-(N'-sulphodiaminophosphinyl)-ornithyl-alanyl-homoarginine, known as phaseolotoxin. The homoarginine residue in this molecule has been suggested to be the product of L-arginine:lysine amidinotransferase activity, previously detected in extracts of P. syringae pv. phaseolicola grown under conditions of phaseolotoxin production. We report the isolation and characterization of an amidinotransferase gene (amtA) from P. syringae pv. phaseolicola coding for a polypeptide of 362 residues (41.36 kDa) and showing approximately 40% sequence similarity to L-arginine:inosamine-phosphate amidinotransferase from three species of Streptomyces spp. and 50.4% with an L-arginine:glycine amidinotransferase from human mitochondria. The cysteine, histidine, and aspartic acid residues involved in substrate binding are conserved. Furthermore, expression of the amtA and argK genes and phaseolotoxin production occurs at 18 degrees C but not at 28 degrees C. An amidinotransferase insertion mutant was obtained that lost the capacity to synthesize homoarginine and phaseolotoxin. These results show that the amtA gene isolated is responsible for the amidinotransferase activity detected previously and that phaseolotoxin production depends upon the activity of this gene. (+info)Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans. (2/58)
Arginine:glycine amidinotransferase (AGAT) catalyzes the first step of creatine synthesis, resulting in the formation of guanidinoacetate, which is a substrate for creatine formation. In two female siblings with mental retardation who had brain creatine deficiency that was reversible by means of oral creatine supplementation and had low urinary guanidinoacetate concentrations, AGAT deficiency was identified as a new genetic defect in creatine metabolism. A homozygous G-A transition at nucleotide position 9297, converting a tryptophan codon (TGG) to a stop codon (TAG) at residue 149 (T149X), resulted in undetectable cDNA, as investigated by reverse-transcription PCR, as well as in undetectable AGAT activity, as investigated radiochemically in cultivated skin fibroblasts and in virus-transformed lymphoblasts of the patients. The parents were heterozygous for the mutant allele, with intermediate residual AGAT activities. Recognition and treatment with oral creatine supplements may prevent neurological sequelae in affected patients. (+info)Methylation demand and homocysteine metabolism: effects of dietary provision of creatine and guanidinoacetate. (3/58)
S-adenosylmethionine, formed by the adenylation of methionine via S-adenosylmethionine synthase, is the methyl donor in virtually all known biological methylations. These methylation reactions produce a methylated substrate and S-adenosylhomocysteine, which is subsequently metabolized to homocysteine. The methylation of guanidinoacetate to form creatine consumes more methyl groups than all other methylation reactions combined. Therefore, we examined the effects of increased or decreased methyl demand by these physiological substrates on plasma homocysteine by feeding rats guanidinoacetate- or creatine-supplemented diets for 2 wk. Plasma homocysteine was significantly increased (~50%) in rats maintained on guanidinoacetate-supplemented diets, whereas rats maintained on creatine-supplemented diets exhibited a significantly lower (~25%) plasma homocysteine level. Plasma creatine and muscle total creatine were significantly increased in rats fed the creatine-supplemented or guanidinoacetate-supplemented diets. The activity of kidney L-arginine:glycine amidinotransferase, the enzyme catalyzing the synthesis of guanidinoacetate, was significantly decreased in both supplementation groups. To examine the role of the liver in mediating these changes in plasma homocysteine, isolated rat hepatocytes were incubated with methionine in the presence and absence of guanidinoacetate and creatine, and homocysteine export was measured. Homocysteine export was significantly increased in the presence of guanidinoacetate. Creatine, however, was without effect. These results suggest that homocysteine metabolism is sensitive to methylation demand imposed by physiological substrates. (+info)On the control of arginine metabolism in chicken kidney and liver. (4/58)
Arginases have been found to be located on the external side of the inner mitochondrial membrane of chicken kidney and liver. Transamidinase has been detected within the liver mitochondrial matrix space. Arginases and transamidinase act upon two different intracellular arginine pools. Penetration of arginine into the matrix space occurs only in respring mitochondria and in the presence of anions such as acetate and phosphate; D-arginine, L-ornithine, D-'ornithine and L-lysine penetrate with the same modalities. L-Histidine penetrates only kidney mitochondria. Because of transamidinase compartmentation, the rate of creatine synthesis is influenced by the rate of penetration of arginine into the mitochondria. (+info)Guanidinoacetate and creatine plus creatinine assessment in physiologic fluids: an effective diagnostic tool for the biochemical diagnosis of arginine:glycine amidinotransferase and guanidinoacetate methyltransferase deficiencies. (5/58)
BACKGROUND: Disorders of creatine metabolism arise from genetic alterations of arginine:glycine amidinotransferase (AGAT), guanidinoacetate methyltransferase (GAMT), and the creatine transporter. We developed a strategy for the detection of AGAT and GAMT defects by measurement of guanidinoacetate (GAA) and creatine plus creatinine (Cr+Crn) in biological fluids. METHODS: Three patients with AGAT deficiency from the same pedigree and their eight relatives, as well as a patient affected by a GAMT defect and his parents were analyzed by a new HPLC procedure in comparison with 90 controls. The method, which uses precolumn derivatization with benzoin, separation with a reversed-phase column, and fluorescence detection, has shown good precision and sensitivity and requires minimal sample handling. RESULTS: In the three AGAT patients, plasma GAA was 0.01-0.04 micro mol/L [mean (SD) for neurologically normal controls was 1.16 (0.59) micromol/L], Cr+Crn was 15-29 micro mol/L [reference limit in our laboratory, 79 (38) micromol/L]. Urinary GAA was 2.4-5.8 micro mol/L [reference, 311 (191) micromol/L], and Cr+Crn was 2.1-3.3 mmol/L [reference, 9.9 (4.1) mmol/L]. We found a smaller decrease in GAA and Cr+Crn in some carriers of an AGAT defect. In the patient with GAMT deficiency, plasma and urine GAA was increased (18.6 and 1783 micromol/L, respectively), and Cr+Crn was decreased in plasma (10.7 micromol/L) and urine (2.1 mmol/L). GAA was increased in the parents' plasmas and in the mother's urine. CONCLUSION: The assessment of GAA is a new tool for the detection of both GAMT and AGAT deficiencies. (+info)Fresh and cultured thyroid gland: survival and function after implantation. (6/58)
Isogeneic or allogeneic thyroid glands were implanted into thyroidectomized recipeint rats. These grafts, either fresh or cultured, were placed in hamstring muscle pocket or under the renal capsule. Survival and function of the grafts were evaluated by: restoration of normal levels of serum thyroxine, weight gain, kidney transamidinase (a thyroxine-induced enzyme), and histological appearance of re-excised implants. A isografts, fresh and cultured, functioned well as ectopic thyroid glands, though restoration of normal serum thyroxine levels was more rapid for the fresh implants. Fresh allografts functioned transiently but then failed due to rejection. No function was detected for cultured allografts, and rejection was seen histologically. The rat thyroid allograft therefore differs from the rat parathyroid allograft, which often can function for several months despite histological evidence of rejection. Maintenance in tissue culture prior to implantation does not appear to alter the longterm immunogenicity of either organ. (+info)Gatm, a creatine synthesis enzyme, is imprinted in mouse placenta. (7/58)
To increase our understanding of imprinting and epigenetic gene regulation, we undertook a search for new imprinted genes. We identified Gatm, a gene that encodes l-arginine:glycine amidinotransferase, which catalyzes the rate-limiting step in the synthesis of creatine. In mouse, Gatm is expressed during development and is imprinted in the placenta and yolk sac, but not in embryonic tissues. The Gatm gene maps to mouse chromosome 2 in a region not previously shown to contain imprinted genes. To determine whether Gatm is located in a cluster of imprinted genes, we investigated the expression pattern of genes located near Gatm: Duox1-2, Slc28a2, Slc30a4 and a transcript corresponding to LOC214616. We found no evidence that any of these genes is imprinted in placenta. We show that a CpG island associated with Gatm is unmethylated, as is a large CpG island associated with a neighboring gene. This genomic screen for novel imprinted genes has elucidated a new connection between imprinting and creatine metabolism during embryonic development in mammals. (+info)Studies on the catabolism of Ng-methylarginine, Ng, Ng-dimethylarginine and Ng, Ng-dimethylarginine in the rabbit. (8/58)
1. The routes of elimination of Ng-methylarginine, Ng, Ng-dimethylarginine and Ng, Ng-dimethylarginine were investigated in the rabbit. 2. Analyses showed low plasma concentrations of these amino acids (around 1 nmol/ml) and ratios similar to those found in tissue proteins. The concentrations of these amino acids in extracts of brain, kidney, liver and spleen were similar except that liver had a lower concentration of Ng-methylarginine and Ng, Ng-dimethylarginine. Cerebrospinal fluid contained traces of each amino acid. (+info)
GATM gene - Genetics Home Reference
glycine amidinotransferase
Creatine Metabolism and Safety Profiles after Six-Week Oral Guanidinoacetic Acid Administration in Healthy Humans
GATM - Glycine amidinotransferase, mitochondrial precursor - Gallus gallus (Chicken) - GATM gene & protein
anti-Gatm antibody | GeneTex
RCSB PDB - 3JDW: CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN...
PDB 1jdw function and biology ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBI
The metabolic burden of creatine synthesis | SpringerLink
Detox Blog Series Part 5 | Methylation Capacity - WholisticMatters
Glycine - what is and why is it becoming more and more popular?
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Treatment monitoring of brain creatine deficiency syndromes: a 1h and 31P MR spectroscopy study | IRIS Università di Pisa
Impaired cardiac contractile function in AGAT knockout mice devoid of creatine is rescued by homoarginine but not creatine. -...
Simultaneous determination of guanidinoacetate, creatine and creatinine in urine and plasma by un-derivatized liquid...
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Low-Dose Creatine Supplementation Lowers Plasma Guanidinoacetate, but Not Plasma Homocysteine, in a Double-Blind, Randomized,...
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THE URINARY EXCRETION OF CREATINE IN ARTHRITIS* | Annals of Internal Medicine | American College of Physicians
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Simultaneous determination of creatine and guanidinoacetate in plasma by liquid chromatography-tandem mass spectrometry (LC-MS...
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Streptidine 6-phosphate
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Scyllo-inosamine-4-phosphate amidinotransferase
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the amidinotransferases. The ...
List of MeSH codes (D08)
... amidinotransferases MeSH D08.811.913.555.275 - carboxyl and carbamoyl transferases MeSH D08.811.913.555.275.200 - aspartate ...
Amidinotransferases | REACH
"Amidinotransferases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Amidinotransferases" by people in this website by year, and ... Below are the most recent publications written about "Amidinotransferases" by people in Profiles. ... whether "Amidinotransferases" was a major or minor topic of these publications. To see the data from this visualization as text ...
Phenylethanolamine N-methyltransferase - wikidoc
KEGG BRITE: Enzymes - Pseudomonas putida H8234
KEGG BRITE: Enzymes - Sinocyclocheilus anshuiensis
Scyllo-inosamine-4-phosphate amidinotransferase - Wikipedia
Transferases | definition of transferases by Medical dictionary
Egr-5 is a post-mitotic regulator of planarian epidermal differentiation | eLife
ENZYME search by enzyme class
RCSB PDB - 5JDW: CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH GLYCINE
List of MeSH codes (D08) - Wikipedia
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OPUS at UTS: Evolutionary acquisition and loss of saxitoxin biosynthesis in dinoflagellates: the second 'core' gene, sxtG -...
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Althoff, M., Braunschweig, W., Gerhards, R., Kirschfink, F. J., Martyn, H. U., Rosskamp, P., Wallraff, W., Bock, B., Eisenmann, J., Fischer, H. M., Hartmann, H., Jocksch, A., Kolanoski, H., Mertens, V., Wedemeyer, R., Foster, B., Bernardi, E., Eisenberg, Y., Eskreys, A., Gather, K. & 71 others, Hultschig, H., Joos, P., Klima, B., Kowalski, H., Ladage, A., Löhr, B., Lüke, D., Mättig, P., Notz, D., Revel, D., Ronat, E., Schütte, W., Trines, D., Tymieniecka, T., Walczak, R., Wolf, G., Zeuner, W., Hilger, E., Kracht, T., Krasemann, H. L., Krüger, J., Lohrmann, E., Poelz, G., Pösnecker, K. U., Binnie, D. M., Dornan, P. J., Garbutt, D. A., Jenkins, C., Jones, W. G., Sedgbeer, J. K., Su, D., Thomas, J., Wan Abdullah, W. A. T., Barreiro, F., Ros, E., Bowler, M. G., Bull, P., Cashmore, R. J., Dauncey, P., Devenish, R., Heath, G., Mellor, D. J., Ratoff, P., Yelton, J. M., Lloyd, S. L., Forden, G. E., Hart, J. C., Hasell, D. K., Saxon, D. H., Brandt, S., Holder, M., Labarga, L., Neumann, B., Karshon, ...
DeCS
Effects of SLCO1B1 and GATM gene variants on rosuvastatin-induced myopathy are unrelated to high plasma exposure of...
A short review on creatine-creatine kinase system in relation to cancer and some experimental results on creatine as adjuvant...
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Functional modeling and phylogenetic distribution of putative cylindrospermopsin biosynthesis enzymes. - PubMed - NCBI
Catechol-O-methyl transferase
DeCS Ingl s+escopo
Ornithine transcarbamylase
A Maldiisotopic Approach to Discover Natural Products: Cryptomaldamide, a Hybrid Tripeptide from the Marine Cyanobacterium...
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Transferases1
- This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the amidinotransferases. (wikipedia.org)
MeSH1
- Amidinotransferases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (sickkids.ca)