AMP Deaminase: An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.Nucleotide Deaminases: Catalyze the hydrolysis of nucleotides with the elimination of ammonia.Adenosine Deaminase: An enzyme that catalyzes the hydrolysis of ADENOSINE to INOSINE with the elimination of AMMONIA.Inosine Monophosphate: Inosine 5'-Monophosphate. A purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety.Adenosine Deaminase Inhibitors: Drugs that inhibit ADENOSINE DEAMINASE activity.Cytidine Deaminase: An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.Coformycin: A ribonucleoside antibiotic synergist and adenosine deaminase inhibitor isolated from Nocardia interforma and Streptomyces kaniharaensis. It is proposed as an antineoplastic synergist and immunosuppressant.Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.Cytosine Deaminase: An enzyme which catalyzes the deamination of CYTOSINE resulting in the formation of URACIL. It can also act on 5-methylcytosine to form THYMIDINE.DCMP Deaminase: An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12.Nucleoside Deaminases: Catalyze the hydrolysis of nucleosides with the elimination of ammonia.Cyclic AMP: An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.Guanine Deaminase: An enzyme that catalyzes the deamination of guanine to form xanthine. EC 3.5.4.3.Adenine NucleotidesRibonucleosides: Nucleosides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)Kinetics: The rate dynamics in chemical or physical systems.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Phosphates: Inorganic salts of phosphoric acid.Inosine: A purine nucleoside that has hypoxanthine linked by the N9 nitrogen to the C1 carbon of ribose. It is an intermediate in the degradation of purines and purine nucleosides to uric acid and in pathways of purine salvage. It also occurs in the anticodon of certain transfer RNA molecules. (Dorland, 28th ed)5'-Nucleotidase: A glycoprotein enzyme present in various organs and in many cells. The enzyme catalyzes the hydrolysis of a 5'-ribonucleotide to a ribonucleoside and orthophosphate in the presence of water. It is cation-dependent and exists in a membrane-bound and soluble form. EC 3.1.3.5.Adenosine: A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter.Muscles: Contractile tissue that produces movement in animals.Hydroxymethylbilane Synthase: An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8Purine Nucleotides: Purines attached to a RIBOSE and a phosphate that can polymerize to form DNA and RNA.Hypoxanthine: A purine and a reaction intermediate in the metabolism of adenosine and in the formation of nucleic acids by the salvage pathway.Extracorporeal Circulation: Diversion of blood flow through a circuit located outside the body but continuous with the bodily circulation.Oxygen: An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.Coronary Artery Bypass: Surgical therapy of ischemic coronary artery disease achieved by grafting a section of saphenous vein, internal mammary artery, or other substitute between the aorta and the obstructed coronary artery distal to the obstructive lesion.Anoxia: Relatively complete absence of oxygen in one or more tissues.Methanosarcinaceae: A family of anaerobic METHANOSARCINALES whose cells are mesophilic or thermophilic and appear as irregular spheroid bodies or sheathed rods. These methanogens are found in any anaerobic environment including aquatic sediments, anaerobic sewage digesters and gastrointestinal tracts. There are four genera: METHANOSARCINA, Methanolobus, Methanothrix, and Methanococcoides.Glucose Clamp Technique: Maintenance of a constant blood glucose level by perfusion or infusion with glucose or insulin. It is used for the study of metabolic rates (e.g., in glucose, lipid, amino acid metabolism) at constant glucose concentration.Insulin: A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).Insulin Resistance: Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS.Haplotypes: The genetic constitution of individuals with respect to one member of a pair of allelic genes, or sets of genes that are closely linked and tend to be inherited together such as those of the MAJOR HISTOCOMPATIBILITY COMPLEX.Receptor, Insulin: A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE.Blood Glucose: Glucose in blood.Diethyl Pyrocarbonate: Preservative for wines, soft drinks, and fruit juices and a gentle esterifying agent.Histidine: An essential amino acid that is required for the production of HISTAMINE.Hydrogen-Ion Concentration: 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)Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Tetrahydrofolate Dehydrogenase: 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.Tetrahydrofolates: Compounds based on 5,6,7,8-tetrahydrofolate.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Folic Acid Antagonists: 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)Trimetrexate: A nonclassical folic acid inhibitor through its inhibition of the enzyme dihydrofolate reductase. It is being tested for efficacy as an antineoplastic agent and as an antiparasitic agent against PNEUMOCYSTIS PNEUMONIA in AIDS patients. Myelosuppression is its dose-limiting toxic effect.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.Methotrexate: 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.IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.Nucleic Acids: High molecular weight polymers containing a mixture of purine and pyrimidine nucleotides chained together by ribose or deoxyribose linkages.Purines: A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include ADENINE and GUANINE, constituents of nucleic acids, as well as many alkaloids such as CAFFEINE and THEOPHYLLINE. Uric acid is the metabolic end product of purine metabolism.Mescaline: Hallucinogenic alkaloid isolated from the flowering heads (peyote) of Lophophora (formerly Anhalonium) williamsii, a Mexican cactus used in Indian religious rites and as an experimental psychotomimetic. Among its cellular effects are agonist actions at some types of serotonin receptors. It has no accepted therapeutic uses although it is legal for religious use by members of the Native American Church.Glutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.

Regulation of AMP deaminase from chicken erythrocytes. A kinetic study of the allosteric interactions. (1/194)

The allosteric properties of AMP deaminase [EC 3.5.4.6] from chicken erythrocytes have been qualitatively and quantitatively accounted for by the concerted transition theory of Monod et al., on the assumption that this enzyme has different numbers of binding sites for each ligand. Theoretical curves yield a satisfactory fit for all experimental saturation functions with respect to activation by alkali metals and inhibition by Pi, assuming that the numbers of binding sites for AMP, alkali metals, and Pi are 4, 2, and 4, respectively. The enzyme was inhibited by concentrations of ATP and GTP below 0.1 and 0.25 mM, respectively, whereas activation of the enzyme was observed at ATP and GTP concentrations above 0.4 and 1.5 mM, respectively. These unusual kinetics with respect to ATP and GTP could be also accounted for by assuming 2 inhibitory and 4 activating sites for each ligand.  (+info)

Regulation of chicken erythrocyte AMP deaminase by phytic acid. (2/194)

AMP deaminase [EC 3.5.6.4] purified from chicken erythrocytes was inhibited by phytic acid (inositol hexaphosphate), which is the principal organic phosphate in chicken red cells. Kinetic analysis has indicated that this inhibition is of an allosteric type. The estimated Ki value was within the normal range of phytic acid concentration, suggesting that this compound acts as a physiological effector. Divalent cations such as Ca2+ and Mg2+ were shown to affect AMP deaminase by potentiating inhibition by lower concentrations of phytic acid, and by relieving the inhibition at higher concentrations of phytic acid. These results suggests that Ca2+ and Mg2+ can modify the inhibition of AMP deaminase by phytic acid in chicken red cells.  (+info)

Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure. (3/194)

BACKGROUND: This study was undertaken to identify gene(s) that may be associated with improved clinical outcome in patients with congestive heart failure (CHF). The adenosine monophosphate deaminase locus (AMPD1) was selected for study. We hypothesized that inheritance of the mutant AMPD1 allele is associated with increased probability of survival without cardiac transplantation in patients with CHF. METHODS AND RESULTS: AMPD1 genotype was determined in 132 patients with advanced CHF and 91 control reference subjects by use of a polymerase chain reaction-based, allele-specific oligonucleotide detection assay. In patients with CHF, those heterozygous (n=20) or homozygous (n=1) for the mutant AMPD1 allele (AMPD1 +/- or -/-, respectively) experienced a significantly longer duration of heart failure symptoms before referral for transplantation evaluation than CHF patients homozygous for the wild-type allele (AMPD1 +/+; n=111; 7.6+/-6.5 versus 3.2+/-3.6 years; P<0.001). The OR of surviving without cardiac transplantation >/=5 years after initial hospitalization for CHF symptoms was 8.6 times greater (95% CI: 3.05, 23.87) in those patients carrying >/=1 mutant AMPD1 allele than in those carrying 2 wild-type AMPD1 +/+ alleles. CONCLUSIONS: After the onset of CHF symptoms, the mutant AMPD1 allele is associated with prolonged probability of survival without cardiac transplantation. The mechanism by which the presence of the mutant AMPD1 allele may modify the clinical phenotype of heart failure remains to be determined.  (+info)

AMP deaminase in piglet cardiac myocytes: effect on nucleotide metabolism during ischemia. (4/194)

The purpose of this study was to examine in situ regulation of AMP deaminase in newborn piglet cardiac myocytes and to determine its role in nucleotide metabolism during ischemia. When a rapid deenergization paradigm was used to assay AMP deaminase, enzyme activity depended on the hormonal and metabolic status of cells just before deenergization. Inosine 5'-monophosphate (IMP) formation was increased 150% in deenergized myocytes pretreated with phorbol 12-myristate 13-acetate (PMA; EC50 = 4.7 x 10(-8) M). This effect was 90% blocked with the protein kinase C (PKC) inhibitor staurosporine. In addition, the beta-adrenergic agonist isoproterenol stimulated AMP deaminase activity (EC50 = 1.5 x 10(-8) M), and IMP formation was directly correlated to intracellular cAMP levels (r2 = 0.9). Furthermore, adenosine increased IMP formation, whereas nonrespiring, glycolyzing piglet myocytes had reduced AMP deaminase activity. Pretreatment of perfused piglet hearts with adenosine, but not PMA, before exposure to global ischemia resulted in enhanced conversion of AMP to IMP during the ischemic period. Similar results were obtained in piglet myocytes preincubated with adenosine or PMA before exposure to simulated ischemia. These results may be relevant to the preconditioning phenomenon.  (+info)

5'-Nucleotidase as a marker of both general and local inflammation in rheumatoid arthritis patients. (5/194)

OBJECTIVES: To evaluate measurements of serum and synovial fluid 5'-nucleotidase (5'N) activity as a marker of general and local inflammation in arthritis, and to resolve a contradiction in the literature as to whether or not the activity of 5'N in the synovial fluids of rheumatoid arthritis (RA) patients is raised in comparison with that in the synovial fluids of other arthritis patients. METHODS: Assays for 5'N were carried out in the presence of inhibitors of other phosphatases, AMP deaminase and of 5'N itself. RESULTS: The 5'N activity in the synovial fluid of RA patients was both significantly higher (mean 1.7-fold) and had a greater variance than that in the synovial fluids of other arthritis patients, and the contradiction in the literature was resolved. There was a strong correlation between the 5'N activity in the sera of RA patients and their erythrocyte sedimentation rate. There was no significant correlation between the 5'N in the serum and synovial fluid for the RA patients, in marked contrast to the strong correlation between the two 5'N activities shown by the osteoarthritis patients. The 5'N activity was greater in the synovial fluid than in the serum for virtually all the patients, showing that it was being made locally. CONCLUSIONS: The 5'N activity in the serum (which came mostly from the liver) could be used as a marker of general inflammation, whereas the 5'N in the synovial fluid was mostly produced locally, and could be used as a marker of joint inflammation, particularly for the RA patients.  (+info)

Regulation of AMP deaminase by phosphoinositides. (6/194)

AMP deaminase (AMPD) converts AMP to IMP and is a diverse and highly regulated enzyme that is a key component of the adenylate catabolic pathway. In this report, we identify the high affinity interaction between AMPD and phosphoinositides as a mechanism for regulation of this enzyme. We demonstrate that endogenous rat brain AMPD and the human AMPD3 recombinant enzymes specifically bind inositide-based affinity probes and to mixed lipid micelles that contain phosphatidylinositol 4,5-bisphosphate. Moreover, we show that phosphoinositides specifically inhibit AMPD catalytic activity. Phosphatidylinositol 4,5-bisphosphate is the most potent inhibitor, effecting pure noncompetitive inhibition of the wild type human AMPD3 recombinant enzyme with a K(i) of 110 nM. AMPD activity can be released from membrane fractions by in vitro treatment with neomycin, a phosphoinositide-binding drug. In addition, in vivo modulation of phosphoinositide levels leads to a change in the soluble and membrane-associated pools of AMPD activity. The predicted human AMPD3 sequence contains pleckstrin homology domains and (R/K)X(n)(R/K)XKK sequences, both of which are characterized phosphoinositide-binding motifs. The interaction between AMPD and phosphoinositides may mediate membrane localization of the enzyme and function to modulate catalytic activity in vivo.  (+info)

Energy metabolism and lipid peroxidation of human erythrocytes as a function of increased oxidative stress. (7/194)

To study the influence of oxidative stress on energy metabolism and lipid peroxidation in erythrocytes, cells were incubated with increasing concentrations (0.5-10 mM) of hydrogen peroxide for 1 h at 37 degrees C and the main substances of energy metabolism (ATP, AMP, GTP and IMP) and one index of lipid peroxidation (malondialdehyde) were determined by HPLC on cell extracts. Using the same incubation conditions, the activity of AMP-deaminase was also determined. Under nonhaemolysing conditions (at up to 4 mM H2O2), oxidative stress produced, starting from 1 mM H2O2, progressive ATP depletion and a net decrease in the intracellular sum of adenine nucleotides (ATP + ADP + AMP), which were not paralleled by AMP formation. Concomitantly, the IMP level increased by up to 20-fold with respect to the value determined in control erythrocytes, when cells were challenged with the highest nonhaemolysing H2O2 concentration (4 mM). Efflux of inosine, hypoxanthine, xanthine and uric acid towards the extracellular medium was observed. The metabolic imbalance of erythrocytes following oxidative stress was due to a dramatic and unexpected activation of AMP-deaminase (a twofold increase of activity with respect to controls) that was already evident at the lowest dose of H2O2 used; this enzymatic activity increased with increasing H2O2 in the medium, and reached its maximum at 4 mM H2O2-treated erythrocytes (10-fold higher activity than controls). Generation of malondialdehyde was strictly related to the dose of H2O2, being detectable at the lowest H2O2 concentration and increasing without appreciable haemolysis up to 4 mM H2O2. Besides demonstrating a close relationship between lipid peroxidation and haemolysis, these data suggest that glycolytic enzymes are moderately affected by oxygen radical action and strongly indicate, in the change of AMP-deaminase activity, a highly sensitive enzymatic site responsible for a profound modification of erythrocyte energy metabolism during oxidative stress.  (+info)

IMP and AMP deaminase in reperfusion injury down-regulates neutrophil recruitment. (8/194)

We examined gene regulation in murine lungs after hind-limb vessel occlusion and reperfusion. A rapid increase of transcript for the AMP deaminase 3 gene (AMPD3) and its enzymatic activity (EC) generating inosine monophosphate (IMP) were identified with transcripts located in bronchial and alveolar epithelium. AMP deaminase inhibitor decreased IMP levels and significantly enhanced neutrophil recruitment within lung tissue during reperfusion. In addition, IMP inhibited cytokine-initiated neutrophil infiltration in vivo and selectively attenuated neutrophil rolling by 90% in microvessels. We prepared labeled IMP and demonstrated that IMP specifically binds to neutrophils. IMP also stimulated binding of gamma-[(35)S]thio-GTP, suggesting that IMP is a potent regulator of neutrophils. Taken together, these results elucidate a previously unrecognized mechanism that protects tissues from the potentially deleterious consequences of aberrant neutrophil accumulation. Moreover, they are relevant for new therapeutic approaches to regulate neutrophil responses in inflammation and vascular disease.  (+info)

AMPD2; adenosine monophosphate deaminase 2; adenosine monophosphate deaminase 2 (isoform L); AMP deaminase 2; AMPD isoform L; adenosine monophosphate deaminase 2 isoform L; AMP deaminase isoform L; AMPD 2; AMPD2_HUMAN; AMPD ...
Adenosine monophosphate deaminase deficiency type 1, also called myoadenylate deaminase deficiency (MADD), is a recessive genetic metabolic disorder that affects approximately 1-2% of populations of European descent. It appears to be considerably rarer in Asian populations. The genetic form is caused by a defect in the gene for AMP deaminase though there is also an acquired form of AMP deficiency. Although many people with a defective AMPD gene are asymptomatic, others may have symptoms such as exercise intolerance, muscle pain, and muscle cramping. Fatigue MADD lowers aerobic power output, so increased anaerobic power is needed to perform the same amount of work.[citation needed] Without myoadenlyate deaminase, heavy activity causes adenosine to be released into the cell or perfused into the surrounding tissues. Fatigue and sedation after heavy exertion can be caused by excess adenosine in the cells which signals muscle fiber to feel fatigued. In the brain, excess adenosine decreases alertness ...
Reaction of rabbit skeletal-muscle AMP deaminase with a low molar excess of diethyl pyrocarbonate results in conversion of the enzyme into a species with one or two carbethoxylated histidine residues per subunit that retains sensitivity to ATP at pH 7.1 but, unlike the native enzyme, it is not sensitive to regulation by ATP at pH 6.5. This effect mimics that exerted on the enzyme by limited proteolysis with trypsin, which removes the 95-residue N-terminal region from the 80 kDa enzyme subunit. These observations suggest involvement of some histidine residues localized in the region HHEMQAHILH (residues 51-60) in the regulatory mechanism which stabilizes the binding of ATP to its inhibitory site at acidic pH. Carbethoxylation of two histidine residues per subunit abolishes the inhibition by ATP of the proteolysed enzyme at pH 7.1, suggesting the obligatory participation of a second class of histidine residues, localized in the 70 kDa subunit core, in the mechanism of the pH-dependent inhibition ...
A major finding in the current study was the ability of the muscle to maintain TCA cycle intermediate (TCAi) concentrations and cellular energy charge during exercise in spite of AMPD activity being less than 1 % of control values. This finding demonstrates the utility of using an inborn error of metabolism to unravel a fundamental question in muscle physiology, namely, that the PNC is not required for TCA cycle anaplerosis. From a clinical perspective, the main finding in this study is that patients with less than 1 % residual AMPD activity were not markedly different from subjects with normal AMPD activity in their tolerance for progressive cycle ergometry exercise.. One conceivable consequence of AMPD deficiency would be an impairment of the PNC with a resultant attenuation of TCAi anaplerosis (Sabina et al. 1980; Flanagan et al. 1986). It has previously been demonstrated that the total muscle TCAi content increased severalfold during the initial minutes of moderate to intense contraction, ...
Studies on the effect of genetic polymorphisms known to affect AMP deaminase (AMPD) activity on progress of heart disease are conflicting: some highlights benefit of decreased AMPD activity in heart failure and ischemic heart disease while the other failed to confirm it. Detailed studies to identify clinical scenario that benefits from decreased AMPD activity are thus needed. We evaluated cardiac effects of decreased AMPD activity during acute oxygen deprivation in clinical and experimental settings. Patients undergoing coronary artery bypass grafting with use of extracorporeal circulation (n=184) were clinically analyzed and genotyped for C34T mutation of AMPD1 that we previously found to decrease cardiac AMPD activity. The effect of new inhibitor of AMPD: 3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol (AMPDI) was tested in apoA/LDLr knockout mouse exposed for 5 min to 5% oxygen in breathing air. The activity of AMP regulated protein ...
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Creatine Phosphokinase Increased & Inability to Supinate Forearm & Joint Hypermobility Symptom Checker: Possible causes include Myoadenylate Deaminase Deficiency. Check the full list of possible causes and conditions now! Talk to our Chatbot to narrow down your search.
Complete information for AMPD3 gene (Protein Coding), Adenosine Monophosphate Deaminase 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for AMPD1 gene (Protein Coding), Adenosine Monophosphate Deaminase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Tracy, Saoirse and Gómez, José Fernández and Sturrock, Craig and Wilson, Zoe A. and Ferguson, Alison (2017) Non-destructive determination of floral staging in cereals using X-ray micro computed tomography (µCT). Plant Methods, 13 (9). ISSN 1746-4811 Ferguson, Alison and Pearce, Simon and Band, Leah R. and Yang, Caiyun and Ferjentsikova, Ivana and King, John and Yuan, Zheng and Zhang, Dabing and Wilson, Zoe A. (2016) Biphasic regulation of the transcription factor ABORTED MICROSPORES (AMS) is essential for tapetum and pollen development in Arabidopsis. New Phytologist, 213 . pp. 778-790. ISSN 1469-8137 Chew, Bee Lynn and Fisk, Ian D. and Fray, Rupert and Tucker, Gregory A. and Bodi, Zsuzsanna and Ferguson, Alison and Xiao, Wei and Seymour, Graham B. (2016) The effect of adenosine monophosphate deaminase overexpression on the accumulation of umami-related metabolites in tomatoes. Plant Cell Reports, 36 (1). pp. 81-87. ISSN 1432-203X Pearce, Simon and Ferguson, Alison and King, John and Wilson, ...
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Learn more about Ribose at Medical City Dallas Uses Principal Proposed Uses None Other Proposed Uses AMPD (Congenital Myoadenylate Deaminase...
Learn more about Ribose at Sky Ridge Medical Center Uses Principal Proposed Uses None Other Proposed Uses AMPD (Congenital Myoadenylate Deaminase...
Given that aldolase B is Commonly current in kidney and intestinal mucosa and in liver, Cox et al. (1982) ended up ready to detect heterozygotes by intestinal biopsy. In a Jewish relatives, they shown that evident dominant inheritance was the result of a homozygote-heterozygote mating. Diagnosis In aldolase B-deficient tissues, cytoplasmic accumulation of fructose-1-phosphate causes sequestration of inorganic phosphate with ensuing activation of AMP deaminase that catalyzes the irreversible deamination of AMP to IMP (inosine monophosphate), a precursor of uric acid. During the cytoplasm, AMP, ADP, and ATP are managed inside a point out approaching equilibrium. Depletion of tissue ATP takes place by means of large degradation to uric acid and impairment of regeneration by oxidative phosphorylation while in the mitochondria on account of inorganic phosphate depletion ...
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The reconstituted glycolytic system described previously (Scopes, 1973) was used to simulate post-mortem glycolytic metabolism in muscle. The effects of the following factors have been investigated: ATPase (adenosine triphosphatase) amount, AMP deaminase amount, percentage of the phosphorylase in the a form and the effect of diluting the glycolytic enzyme complex as a whole. It was confirmed that the rate of metabolism was solely dependent on the amount of ATPase present and that various concentrations of the glycolytic enzymes had no effect over a wide range encompassing the variation found in anatomically different muscles. The extent of metabolism, represented by the value of the ultimate pH, depended markedly on the amount of phosphorylase in the a form; as little as 1% of the a form resulted in a considerably lower pH than in its absence. To a lesser extent the amount of AMP deaminase also affected the ultimate pH, but this was probably only significant for comparisons of genetically ...
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AMP deaminase 3 is an enzyme that in humans is encoded by the AMPD3 gene. This gene encodes a member of the AMP deaminase gene ... 1987). "Deficiency of AMP deaminase in erythrocytes". Hum. Genet. 75 (1): 15-8. doi:10.1007/BF00273831. PMID 3804327. Yamada Y ... Yamada Y, Goto H, Wakamatsu N, Ogasawara N (2001). "A rare case of complete human erythrocyte AMP deaminase deficiency due to ... Yamada Y, Goto H, Ogasawara N (1994). "A point mutation responsible for human erythrocyte AMP deaminase deficiency". Hum. Mol. ...
1998). "Control of AMP deaminase 1 binding to myosin heavy chain". Am. J. Physiol. 275 (3 Pt 1): C870-81. PMID 9730972. Weiss A ...
IMP→AMP:. *Adenylosuccinate synthase. *Adenylosuccinate lyase. *reverse *AMP deaminase. IMP→GMP:. *IMP dehydrogenase ...
XMP is then converted into GMP by using the hydrolysis of 1 ATP and the conversion of glutamine to glutamate.[1] AMP and GMP ... Guanine is then deaminated via guanine deaminase to form xanthine which is then converted to uric acid. Oxygen is the final ... While IMP can be directly converted to AMP, synthesis of GMP (guanosine monophosphate) requires an intermediate step, in which ... The nucleoside, adenosine, is then deaminated and hydrolyzed to form hypoxanthine via adenosine deaminase and nucleosidase ...
The nucleosides cytidine and deoxycytidine can be salvaged along the uracil pathway by cytidine deaminase, which converts them ... AMP Folate biosynthesis[edit]. Tetrahydrofolic acid and its derivatives are produced by salvage pathways from GTP.[1] ...
... encoding enzyme AMP deaminase 3 API5: encoding protein Apoptosis inhibitor 5 APLNR: Apelin receptor (APJ receptor) APOA4: ...
... synthase converts IMP to adenylosuccinate adenylosuccinate lyase converts adenylosuccinate into AMP AMP deaminase converts AMP ... then adenosine deaminase creates inosine Alternatively, AMP deaminase creates inosinic acid, then a nucleotidase creates ... GMP and AMP in high concentration binds the enzyme to exerts inhibition while PRPP is in large amount binds to the enzyme which ... which is activated by PRPP and inhibited by AMP, GMP and IMP. PRPP + L-Glutamine + H2O → PRA + L-Glutamate + PPi In the second ...
... nucleotide deaminases MeSH D08.811.277.151.653.060 --- amp deaminase MeSH D08.811.277.151.653.200 --- dcmp deaminase MeSH ... nucleoside deaminases MeSH D08.811.277.151.486.075 --- adenosine deaminase MeSH D08.811.277.151.486.250 --- cytidine deaminase ... cyclic amp-dependent protein kinases MeSH D08.811.913.696.620.682.700.150.125.500 --- beta-adrenergic-receptor kinase MeSH ... guanine deaminase MeSH D08.811.277.151.418 --- methenyltetrahydrofolate cyclohydrolase MeSH D08.811.277.151.486 --- ...
AMP deaminase (AMPD1) Cytodine deaminase of mononucelotides (CDA) Adenosine Deaminase acting on tRNA (ADAT) Adenosine Deaminase ... Guanine Deaminase (GDA) Adenosine monophosphate deaminase deficiency type 1 Gallinari, P. (1996). "Cloning and Expression of ... Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver, ... APOBEC1 APOBEC3A-H, APOBEC3G - affects HIV Activation-induced (cytidine) deaminase (AICDA) ...
... encoding enzyme AMP deaminase 2 ARID1A (1p36) ATXN7L2: Ataxin 7-like 2 AZIN2: encoding enzyme Antizyme inhibitor 2 (AzI2) also ...
... catalysed by the enzyme AMP deaminase: AMP + H2O → IMP + NH4+ The second stage is the formation of adenylosuccinate from IMP ... This reaction helps to dispose AMP produced after following reaction. ATP → ADP + Pi (Utilisation of ATP for Muscle contraction ... The first stage is the deamination of the purine nucleotide Adenosine monophosphate (AMP) to form inosine monophosphate (IMP), ... AMP + Fumarate A recent study conducted by Sridharan et al. (AJP Cell Physiology, 2008, 295:C29-C37) showed that activation of ...
... optimized for mobile web browsing AMP deaminase, a human enzyme encoded by the AMPD1 gene Adenosine monophosphate, a nucleotide ... Amp or AMP may refer to: Ampere, a unit of electric current, often shortened to Amp Amplifier, a device that increases the ... 1997 compilation Amp (comics), a Marvel Comics fictional mutant Amp (TV series), music video show on MTV The Amp, a British ... finance company AMP Incorporated, U.S. electronic connector company AMP Limited, Australian financial services company Amp ...
AMPD2: encoding enzyme AMP deaminase 2. *ARID1A (1p36). *ATXN7L2: Ataxin 7-like 2 ...
... 1 is an enzyme that in humans is encoded by the AMPD1 gene. Adenosine monophosphate deaminase is an enzyme that ... by directly inhibiting AMP deaminase, thereby increasing cellular AMP. It has been shown that in environments with high ... "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1-11. doi:10.1074/jbc.M110.121806 ... 1998). "Control of AMP deaminase 1 binding to myosin heavy chain". Am. J. Physiol. 275 (3 Pt 1): C870-81. PMID 9730972. Sims B ...
... is an enzyme that in humans is encoded by the AMPD2 gene. GRCh38: Ensembl release 89: ENSG00000116337 - Ensembl ... Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL (1992). "Molecular cloning of AMP deaminase isoform L. Sequence and ... Van den Bergh F, Sabina RL (1996). "Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative ... "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". J ...
The genetic form is caused by a defect in the gene for AMP deaminase though there is also an acquired form of AMP deficiency. ... AMP is normally converted into IMP by myoadenylate deaminase-so myoadenylate deaminase deficiency reduces energy that would be ... AMP deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia ... Fischer, H.; Esbjornsson, M.; Sabina, R. L.; Stromberg, A.; Peyrard-Janvid, M.; Norman, B. (2007). "AMP deaminase deficiency is ...
In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction 5'-AMP + H2O ... Other names in common use include adenylate deaminase, adenine nucleotide deaminase, and adenosine (phosphate) deaminase. Su JC ... Yates MG (1969). "A non-specific adenine nucleotide deaminase from desulfovibrio desulfuricans". Biochim. Biophys. Acta. 171 (2 ... displaystyle \rightleftharpoons } 5'-IMP + NH3 Thus, the two substrates of this enzyme are 5'-AMP and H2O, whereas its two ...
Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase. *GTP cyclohydrolase ...
Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase. *GTP cyclohydrolase ...
AMP can be converted into IMP by the enzyme myoadenylate deaminase, freeing an ammonia group. In a catabolic pathway, adenosine ... AMP Or AMP may be produced by the hydrolysis of one high energy phosphate bond of ADP: ADP + H2O → AMP + Pi AMP can also be ... AMP is used as a monomer in the synthesis of RNA. AMP does not have the high energy pyrophosphate bond associated with ADP and ... AMP can be regenerated to ATP as follows: AMP + ATP → 2 ADP (adenylate kinase in the opposite direction) ADP + Pi → ATP (this ...
... adenine deaminase EC 3.5.4.3: guanine deaminase EC 3.5.4.4: adenosine deaminase EC 3.5.4.5: cytidine deaminase EC 3.5.4.6: AMP ... pterin deaminase EC 3.5.4.12: dCMP deaminase EC 3.5.4.13: dCTP deaminase EC 3.5.4.14: deoxycytidine deaminase EC 3.5.4.15: ... adenosine-phosphate deaminase EC 3.5.4.18: ATP deaminase EC 3.5.4.19: phosphoribosyl-AMP cyclohydrolase EC 3.5.4.20: ... dCTP deaminase (dUMP-forming) EC 3.5.4.31: S-methyl-5'-thioadenosine deaminase EC 3.5.4.32: 8-oxoguanine deaminase EC 3.5.5.1: ...
... deaminase deficiency is a known cause of immunodeficiency. The adenosine analog NITD008 has been reported to directly ... Adenosine used as a second messenger can be the result of de novo purine biosynthesis via adenosine monophosphate (AMP), though ... When adenosine enters the circulation, it is broken down by adenosine deaminase, which is present in red cells and the vessel ...
... amp resistance - amplification - amplicon - anchor sequence - animal model - anneal - anti-sense strand - antibiotic resistance ... adenosine deaminase deficiency - adenovirus - agarose gel electrophoresis - agarose gel - Alagille syndrome - alkaline lysis - ...
Phillips, A.T.; Wood, W.A. (1964). "Basis for AMP activation of "Biodegradative" threonine dehydrase from". Biochemical and ... "Subunit structure of biodegradative threonine deaminase". The Journal of Biological Chemistry. 252 (7): 2206-8. PMID 321452. ...
Gupta RS: Adenosine-AMP exchange activity is an integral part of the mammalian adenosine kinase. Biochem Mol Biol Int 1996, 39 ... Arch JR, Newsholme EA: Activities and some properties of 5'-nucleotidase, adenosine kinase and adenosine deaminase in tissues ... The AdK from mammalian sources, in addition to carrying out ATP-dependent phosphorylation of Ado, also catalyzes an Ado-AMP ... Explanation of exchange reaction between adenosine and AMP. J Biol Chem 1994, 269: 17820-17825. Henderson JF, Mikoshiba A, Chu ...
aminoacyl-AMP + tRNA → aminoacyl-tRNA + AMP. Certain organisms can have one or more aminoacyl tRNA synthetases missing. This ... and adenosine deaminases in Eukarya), which increase the decoding capacity of a given tRNA.[31] As an example, tRNAAla encodes ...
Reaction of rabbit skeletal-muscle AMP deaminase with a low molar excess of diethyl pyrocarbonate results in conversion of the ... Regulation of skeletal-muscle AMP deaminase: involvement of histidine residues in the pH-dependent inhibition of the rabbit ... Regulation of skeletal-muscle AMP deaminase: involvement of histidine residues in the pH-dependent inhibition of the rabbit ... Regulation of skeletal-muscle AMP deaminase: involvement of histidine residues in the pH-dependent inhibition of the rabbit ...
Hisatome, I., Morisake, T., Kamma, H., Sugama, T., Morisaki, H., Ohtahara, A. & Holmes, E. W. (1998). Control of AMP deaminase ... Sinkeler S. P., Binkhorst, R. A., Joosten, E. M., Wevers, R. A., Coerwinkei, M. M. & Oei, T. L. (1987). AMP deaminase ... Morisaki, T., Gross, M., Morisaki, H., Pongratz, D., Zollner, N. & Holmes, E. W. (1992). Molecular basis of AMP deaminase ... Norman, B., Mahnke-Zizelman, D. K., Vallis, A. & Sabina, R. L. (1998). Genetic and other determinants of AMP deaminase activity ...
AMP deaminase 2; AMPD isoform L; adenosine monophosphate deaminase 2 isoform L; AMP deaminase isoform L; AMPD 2; AMPD2_HUMAN; ... Adenosine monophosphate deaminase-2 (EC 3.5.4.6) catalyzes the deamination of AMP to IMP and plays an important role in the ... AMPD2; adenosine monophosphate deaminase 2; adenosine monophosphate deaminase 2 (isoform L); ...
Expression patterns of AMP-deaminase isozymes in human hepatocellular carcinoma (HCC).. Mol. Cell. Biochem. null null 2008 ... AMP-deaminase (AMPD) is a large, well-conserved eukaryotic protein that catalyzes the hydrolytic deamination of adensosine ... In mammalian liver, the reaction catalysed by AMP-deaminase constitutes a rate-limiting step in adenine nucleotide catabolism [ ... monophosphate (AMP) to inosine monophosphate (IMP), and so plays an important role in purine metabolism. ...
AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene. Adenosine monophosphate deaminase is an enzyme that ... by directly inhibiting AMP deaminase, thereby increasing cellular AMP. It has been shown that in environments with high ... "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1-11. doi:10.1074/jbc.M110.121806 ... 1998). "Control of AMP deaminase 1 binding to myosin heavy chain". Am. J. Physiol. 275 (3 Pt 1): C870-81. PMID 9730972. Sims B ...
AMP deaminase 2 is an enzyme that in humans is encoded by the AMPD2 gene. GRCh38: Ensembl release 89: ENSG00000116337 - Ensembl ... Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL (1992). "Molecular cloning of AMP deaminase isoform L. Sequence and ... Van den Bergh F, Sabina RL (1996). "Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative ... "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5-exons". J ...
Abstract 19495: Cardioprotective Effect of AMP Deaminase Inhibition in Oxygen Deprivation. Ryszard T Smolenski, Tomasz ... Studies on the effect of genetic polymorphisms known to affect AMP deaminase (AMPD) activity on progress of heart disease are ... Abstract 19495: Cardioprotective Effect of AMP Deaminase Inhibition in Oxygen Deprivation. Ryszard T Smolenski, Tomasz ... Abstract 19495: Cardioprotective Effect of AMP Deaminase Inhibition in Oxygen Deprivation. Ryszard T Smolenski, Tomasz ...
By converting AMP to inosine monophosphate, AMPD1 plays a major role in regulating cellular AMP levels; AMP activates AMP ... codes for the muscle-specific form of the AMP deaminase enzyme (myoadenylate deaminase), which catalyzes the deamination of AMP ... We tested the candidate gene AMP deaminase 1 (AMPD1) for association with insulin-related traits because it codes for an enzyme ... Morisaki T, Gross M, Morisaki H, Pongratz D, Zollner N, Holmes EW: Molecular basis of AMP deaminase deficiency in skeletal ...
... metabolism through AMP deaminase (AMPD2) (summer) and activation of AMP-activated protein kinase (AMPK) (winter). Liver samples ... These data illuminate the opposing forces of metabolism of AMP by AMPD2 and its availability to activate AMPK as a switch that ... We hypothesized that this switch might be determined by AMP and the dominance of opposing effects: ...
THE EFFECT OF AMP DEAMINASE 3 DEFICIENCY ON POST-MYOCARDIAL INFARCT FUNCTIONAL AND HISTOLOGICAL OUTCOMES IN MICE. ECU Author/ ... The purpose of this study was to use a mouse model to understand the effects of AMP deaminase 3 (AMPD3) deficiency on cardiac ... Abstract: PURPOSE: Humans deficient in the metabolic enzyme AMP deaminase 3 have improved survival and clinical outcomes in ... Furthermore , this study examined how AMP deaminase 3 deficiency impacted infarct size as well as molecular remodeling post- ...
MalaCards integrated aliases for Erythrocyte Amp Deaminase Deficiency:. Name: Erythrocyte Amp Deaminase Deficiency 57 75 29 6 ... An important gene associated with Erythrocyte Amp Deaminase Deficiency is AMPD3 (Adenosine Monophosphate Deaminase 3). OMIM : ... MalaCards based summary : Erythrocyte Amp Deaminase Deficiency, is also known as adenosine monophosphate deaminase deficiency ... ClinVar genetic disease variations for Erythrocyte Amp Deaminase Deficiency:. 6 (show top 50) (show all 114) #. Gene. Variation ...
AMP Deaminase (AMPD: AMP [right arrow]IMP + NH3) isoform 1 is the dominant isoform in skeletal muscle, yet AMPD3 is robustly ... AMP Deaminase 3 knockout mice and loss of mitochondrial proteins and enzyme activity during denervation atrophy. ... July 2018). AMP Deaminase 3 knockout mice and loss of mitochondrial proteins and enzyme activity during denervation atrophy ( ... AMP Deaminase 3 knockout mice and loss of mitochondrial proteins and enzyme activity during denervation atrophy. Masters ...
IMP→AMP:. *Adenylosuccinate synthase. *Adenylosuccinate lyase. *reverse *AMP deaminase. IMP→GMP:. *IMP dehydrogenase ...
XMP is then converted into GMP by using the hydrolysis of 1 ATP and the conversion of glutamine to glutamate.[1] AMP and GMP ... Guanine is then deaminated via guanine deaminase to form xanthine which is then converted to uric acid. Oxygen is the final ... While IMP can be directly converted to AMP, synthesis of GMP (guanosine monophosphate) requires an intermediate step, in which ... The nucleoside, adenosine, is then deaminated and hydrolyzed to form hypoxanthine via adenosine deaminase and nucleosidase ...
... deaminase. Learn about this gene and related health conditions. ... AMP deaminase converts AMP to IMP, and as the cycle continues, ... Adenosine monophosphate deaminase deficiency. At least nine mutations in the AMPD1 gene have been found to cause AMP deaminase ... The lack of AMP deaminase as a source of energy production can result in fatigue and muscle weakness or pain in some people ... The AMPD1 gene provides instructions for producing an enzyme called adenosine monophosphate (AMP) deaminase. This enzyme is ...
AMP deaminase 1 gene polymorphism and heart disease-a genetic association that highlights new treatment.. Smolenski RT1, ... Several studies identified that polymorphism of AMP deaminase 1 gene (AMPD1), in particular the common C34T variant of this ... We suggest therefore that pharmacological inhibition of AMP deaminase before transient ischemic event such as during ischemic ... increased production of adenosine and de-inhibition of AMP regulated protein kinase. Thus, genetic, clinical and biochemical ...
AMP deaminase deficiency does not cause any symptoms. Explore symptoms, inheritance, genetics of this condition. ... deaminase deficiency is a condition that can affect the muscles used for movement (skeletal muscles). In many affected ... AMP deaminase deficiency is caused by mutations in the AMPD1 gene, which provides instructions for producing an enzyme called ... The lack of AMP deaminase activity can result in fatigue, muscle weakness or pain, or other muscle problems in some people with ...
ADA, adenosine deaminase; cAMP, cyclic AMP; ERK, extracellular signal-regulated kinase; MAPK, mitogen-activated protein kinase ... AMP or S-adenosylhomocysteine (SAH). Many cell types perform all the biological processes displayed in the figure, but some ...
Adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.UniRule annotation. Manual assertion according to rules ... IPR001365 A/AMP_deaminase_dom. IPR028892 ADE. IPR006330 Ado/ade_deaminase. IPR032466 Metal_Hydrolase. ... IPR001365 A/AMP_deaminase_dom. IPR028892 ADE. IPR006330 Ado/ade_deaminase. IPR032466 Metal_Hydrolase. ... sp,Q20YN2,ADE_RHOPB Adenine deaminase OS=Rhodopseudomonas palustris (strain BisB18) OX=316056 GN=RPC_4230 PE=3 SV=1 ...
A nucleotidase creates adenosine, then adenosine deaminase creates inosine. *Alternatively, AMP deaminase creates inosinic acid ... AMP[edit]. *adenylosuccinate synthase converts IMP to adenylosuccinate. *adenylosuccinate lyase converts adenylosuccinate into ... So IMP, GMP and AMP are inhibitors while PRPP is an activator. Between the formation of 5-phosphoribosyl, aminoimidazole and ... 1. Severe Immunodeficiency by loss of adenosine deaminase. 2. Hyperuricemia and Lesch-Nyhan syndrome by the loss of ...
IPR001365 A/AMP_deaminase_dom. IPR028893 A_deaminase. IPR006330 Ado/ade_deaminase. IPR032466 Metal_Hydrolase. ... IPR001365 A/AMP_deaminase_dom. IPR028893 A_deaminase. IPR006330 Ado/ade_deaminase. IPR032466 Metal_Hydrolase. ... Adenosine and AMP deaminases family. Adenosine deaminase subfamily.UniRule annotation. Manual assertion according to rulesi ... sp,A5U7Y8,ADD_MYCTA Adenosine deaminase OS=Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) OX=419947 GN=add PE=3 SV=1 ...
Muscle AMP deaminase was deficient (5 resp. 17%). Only one previous report (Neustein et al. 1979) on X-linked mitochondrial ...
Adenosine/AMP deaminase domain (IPR001365) Pfam signature: PF00962 Cellulosome anchoring protein, cohesin domain (IPR002102) ... Porphobilinogen deaminase, N-terminal (IPR022417) Pfam signature: PF01379 Sugar isomerase (SIS) (IPR001347) Pfam signature: ... AMP-dependent synthetase/ligase (IPR000873) Pfam signature: PF00501 Phycobilisome, alpha/beta subunit (IPR012128) Pfam ... Cytidine and deoxycytidylate deaminase domain (IPR002125) Pfam signature: PF00383 Molybdopterin oxidoreductase (IPR006656) Pfam ...
Counteracting roles of AMP deaminase and AMP kinase in the development of fatty liver. PLoS ONE 2012;7:e48801pmid:23152807. ... Metformin activates AMP kinase through inhibition of AMP deaminase. J Biol Chem 2011;286:1-11pmid:21059655. ... Intracellular phosphate (PO4) levels decrease, stimulating the activity of AMP deaminase 2 (AMPD2). AMPD2 converts AMP to ... The decrease in intracellular phosphate stimulates AMP deaminase (AMPD), which catalyzes the degradation of AMP to inosine ...
AMP deaminase deficiency. H02309 Adenosine deaminase deficiency. Drug. D00155 Pentostatin (JAN/USAN/INN). ... AMPD2; adenosine monophosphate deaminase 2 [KO:K01490] [EC:3.5.4.6]. 272 AMPD3; adenosine monophosphate deaminase 3 [KO:K01490 ...
  • Fischer H, Esbjörnsson M, Sabina RL, Strömberg A, Peyrard-Janvid M, Norman B. AMP deaminase deficiency is associated with lower sprint cycling performance in healthy subjects. (medlineplus.gov)
  • The crude preparation used in the assay for cyclic-AMP was fractionated by several methods and cyclic-AMP binding studies were carried out on the different fractions. (warwick.ac.uk)
  • PURPOSE: Humans deficient in the metabolic enzyme AMP deaminase 3 have improved survival and clinical outcomes in cases of revascularization , myocardial infarction , and/or heart failure. (uncg.edu)
  • Muscle AMP deaminase was deficient (5 resp. (nih.gov)
  • Deletion of AMP deaminase (AMD1) attempts to rectify this by elevating intracellular ADP concentrations. (princeton.edu)
  • Although ATP and ADP concentrations in amd1Δtps1Δ following glucose upshift are more stable, the resulting increase in AMP concentrations may directly interfere with proper glycolytic regulation, resulting in less efficient glycolytic flux and energy production. (princeton.edu)
  • 2. A study was made of adenylate cyclase in red blood cells and of the cyclic-AMP binding proteins of the bovine adrenal cortex. (warwick.ac.uk)
  • changes in Ca2+ via calmodulin, increasing cyclic AMP and that change in AMP+ADP:ATP triggered by exercise, low glucose, hypoxia and severely toxic doses of metformin. (blogspot.com)
  • The first committed step is the reaction of PRPP, glutamine and water to 5'-phosphoribosylamine (PRA), glutamate , and pyrophosphate - catalyzed by amidophosphoribosyltransferase , which is activated by PRPP and inhibited by AMP , GMP and IMP . (rug.nl)