Amidophosphoribosyltransferase: An enzyme, involved in the early steps of purine nucleotide biosynthesis, that catalyzes the formation of 5-phosphoribosylamine from glutamine and phosphoribosylpyrophosphate. EC 2.4.2.14.Phosphoribosyl Pyrophosphate: The key substance in the biosynthesis of histidine, tryptophan, and purine and pyrimidine nucleotides.Pentosyltransferases: Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.Purine Nucleotides: Purines attached to a RIBOSE and a phosphate that can polymerize to form DNA and RNA.Hypoxanthine Phosphoribosyltransferase: An enzyme that catalyzes the conversion of 5-phosphoribosyl-1-pyrophosphate and hypoxanthine, guanine, or 6-mercaptopurine to the corresponding 5'-mononucleotides and pyrophosphate. The enzyme is important in purine biosynthesis as well as central nervous system functions. Complete lack of enzyme activity is associated with the LESCH-NYHAN SYNDROME, while partial deficiency results in overproduction of uric acid. EC 2.4.2.8.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.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Hydroxymethyl and Formyl Transferases: Enzymes that catalyze the transfer of hydroxymethyl or formyl groups. EC 2.1.2.Methanococcales: An order of anaerobic methanogens in the kingdom EURYARCHAEOTA. They are pseudosarcina, coccoid or sheathed rod-shaped and catabolize methyl groups. The cell wall is composed of protein. The order includes one family, METHANOCOCCACEAE. (From Bergey's Manual of Systemic Bacteriology, 1989)Methanococcaceae: A family of anaerobic METHANOCOCCALES whose organisms are motile by means of flagella. These methanogens use carbon dioxide as an electron acceptor.Methanocaldococcus: A genus of obligate anaerobic METHANOCALDOCOCCACEAE whose organisms are non-motile despite possessing long thin flagella. These methanogens are found in deep-sea vent and other hydrothermal environments.Methanococcus: A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.Archaeal Proteins: Proteins found in any species of archaeon.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Genes, Archaeal: The functional genetic units of ARCHAEA.Ribose-Phosphate Pyrophosphokinase: An enzyme that catalyzes the formation of phosphoribosyl pyrophosphate from ATP and ribose-5-phosphate. EC 2.7.6.1.PentosephosphatesRibosemonophosphates: Ribose substituted in the 1-, 3-, or 5-position by a phosphoric acid moiety.Anthranilate Phosphoribosyltransferase: An enzyme that catalyzes the formation of N-5'-phosphoribosylanthranilic acid from anthranilate and phosphoribosylpyrophosphate, the first step in tryptophan synthesis in E. coli. It exists in a complex with ANTHRANILATE SYNTHASE in bacteria. EC 2.4.2.18.Hypoxanthines: Purine bases related to hypoxanthine, an intermediate product of uric acid synthesis and a breakdown product of adenine catabolism.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)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Ficain: A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.Sulfur: An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.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.Dual-Specificity Phosphatases: A sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein.MicroRNAs: Small double-stranded, non-protein coding RNAs, 21-25 nucleotides in length generated from single-stranded microRNA gene transcripts by the same RIBONUCLEASE III, Dicer, that produces small interfering RNAs (RNA, SMALL INTERFERING). They become part of the RNA-INDUCED SILENCING COMPLEX and repress the translation (TRANSLATION, GENETIC) of target RNA by binding to homologous 3'UTR region as an imperfect match. The small temporal RNAs (stRNAs), let-7 and lin-4, from C. elegans, are the first 2 miRNAs discovered, and are from a class of miRNAs involved in developmental timing.Streptomyces griseus: An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.3' Untranslated Regions: The sequence at the 3' end of messenger RNA that does not code for product. This region contains transcription and translation regulating sequences.Protein Tyrosine Phosphatases: An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.Insectivora: An order of insect eating MAMMALS including MOLES; SHREWS; HEDGEHOGS and tenrecs.Cyclin-Dependent Kinases: Protein kinases that control cell cycle progression in all eukaryotes and require physical association with CYCLINS to achieve full enzymatic activity. Cyclin-dependent kinases are regulated by phosphorylation and dephosphorylation events.Phosphoribosylaminoimidazolecarboxamide Formyltransferase: An enzyme that catalyzes the conversion of aminoimidazole-4-carboxamide ribonucleotide to 5-formyl-aminoimidazole-4-carboxamide ribonucleotide in the purine de novo synthesis pathway. It requires the cofactor N(10)-FORMYLTETRAHYDROFOLATE as the formyl donor.Expressed Sequence Tags: Partial cDNA (DNA, COMPLEMENTARY) sequences that are unique to the cDNAs from which they were derived.RNA-Binding Proteins: Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.RNA Splicing: The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.Authorship: The profession of writing. Also the identity of the writer as the creator of a literary production.Nocardia asteroides: A species of bacterium of the family NOCARDIACEAE, producing pulmonary infections in man.Nocardia: A genus of gram-positive, aerobic bacteria whose species are widely distributed and are abundant in soil. Some strains are pathogenic opportunists for humans and animals.Nocardia Infections: Infections with bacteria of the genus NOCARDIA.Paratuberculosis: A chronic GASTROENTERITIS in RUMINANTS caused by MYCOBACTERIUM AVIUM SUBSPECIES PARATUBERCULOSIS.Biometric Identification: A method of differentiating individuals based on the analysis of qualitative or quantitative biological traits or patterns. This process which has applications in forensics and identity theft prevention includes DNA profiles or DNA fingerprints, hand fingerprints, automated facial recognition, iris scan, hand geometry, retinal scan, vascular patterns, automated voice pattern recognition, and ultrasound of fingers.Mycobacterium avium subsp. paratuberculosis: A subspecies of gram-positive, aerobic bacteria. It is the etiologic agent of Johne's disease (PARATUBERCULOSIS), a chronic GASTROENTERITIS in RUMINANTS.Radio Frequency Identification Device: Machine readable patient or equipment identification device using radio frequency from 125 kHz to 5.8 Ghz.Neptune: The eighth planet in order from the sun. It is one of the five outer planets of the solar system. Its two natural satellites are Nereid and Triton.Solar System: The group of celestial bodies, including the EARTH, orbiting around and gravitationally bound by the sun. It includes eight planets, one minor planet, and 34 natural satellites, more than 1,000 observed comets, and thousands of lesser bodies known as MINOR PLANETS (asteroids) and METEOROIDS. (From Academic American Encyclopedia, 1983)Meteoroids: Any solid objects moving in interplanetary space that are smaller than a planet or asteroid but larger than a molecule. Meteorites are any meteoroid that has fallen to a planetary surface. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Accounts Payable and Receivable: Short-term debt obligations and assets occurring in the regular course of operational transactions.Health Insurance Portability and Accountability Act: Public Law 104-91 enacted in 1996, was designed to improve the efficiency and effectiveness of the healthcare system, protect health insurance coverage for workers and their families, and to protect individual personal health information.Dens in Dente: Anomaly of the tooth, found chiefly in upper lateral incisors. It is characterized by invagination of the enamel at the incisal edge.Societies, Medical: Societies whose membership is limited to physicians.

Mutational analysis of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase propeptide processing. (1/86)

Glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis is a member of an N-terminal nucleophile hydrolase enzyme superfamily, several of which undergo autocatalytic propeptide processing to generate the mature active enzyme. A series of mutations was analyzed to determine whether amino acid residues required for catalysis are also used for propeptide processing. Propeptide cleavage was strongly inhibited by replacement of the cysteine nucleophile and two residues of an oxyanion hole that are required for glutaminase function. However, significant propeptide processing was retained in a deletion mutant with multiple defects in catalysis that was devoid of enzyme activity. Intermolecular processing of noncleaved mutant enzyme subunits by active wild-type enzyme subunits was not detected in hetero-oligomers obtained from a coexpression experiment. While direct in vitro evidence for autocatalytic propeptide cleavage was not obtained, the results indicate that some but not all of the amino acid residues that have a role in catalysis are also needed for propeptide processing.  (+info)

Methotrexate inhibits the first committed step of purine biosynthesis in mitogen-stimulated human T-lymphocytes: a metabolic basis for efficacy in rheumatoid arthritis? (2/86)

The immunosuppressive and anti-inflammatory effects of low-dose methotrexate (MTX) have been related directly to inhibition of folate-dependent enzymes by polyglutamated derivatives, or indirectly to adenosine release and/or apoptosis and clonal deletion of activated peripheral blood lymphocytes in S-phase. In this study of phytohaemagglutinin-stimulated primary human T-lymphocytes we show that MTX (20 nM to 20 microM) was cytostatic not cytotoxic, halting proliferation at G(1). This stasis of blastogenesis was associated with an inhibition of purine ribonucleotide synthesis but a stimulation of pyrimidine biosynthesis, the normal mitogen-induced expansion of ATP and GTP pools over 72 h being restricted to concentrations of unstimulated T-cells, whereas the increment in UTP pools exceeded that of controls. Decreased incorporation of H(14)CO(3) or [(14)C]glycine into purine ribonucleotides, with no radiolabel accumulation in any de novo synthetic intermediate but enhanced H(14)CO(3) incorporation into UTP, supported these MTX-related effects. Exaggerated [(14)C]hypoxanthine salvage (which normalized the purine and UTP pools) confirmed the increased availability of 5-phosphoribosyl-1-pyrophosphate (PP-ribose-P) as the molecular mechanism underlying these disparate changes. These results provide the first substantive evidence that the immunosuppressive effects of low-dose MTX in primary blasting human T-lymphocytes relate not to the inhibition of the two folate-dependent enzymes of purine biosynthesis but to inhibition of the first enzyme, amidophosphoribosyltransferase, thereby elevating PP-ribose-P and stimulating UTP synthesis. Varying cell types or incubation conditions employed by other workers, especially malignant/activated cells with high basal metabolic rates, might mask the effects noted in primary human T-lymphocytes. The findings imply the involvement of low-dose MTX in the inhibition of T-lymphocyte proliferation and proliferation-dependent processes in rheumatoid arthritis.  (+info)

Purine metabolism in murine virus-induced erythroleukemic cells during differentiation in vitro. (3/86)

Purine metabolism was studied in murine virus-induced erythroleukemia cells stimulated to differentiate in vitro in the presence of dimethylsulfoxide. The activities of the enzymes that catalyze the synthesis of the first intermediate of the de novo purine pathway, phosphoribosyl-1-amine, were decreased while the enzymes that catalyze the conversion of purine bases to purine ribonucleotides remained unchanged at the time the cells acquired the specialized function of hemoglobin synthesis. In addition, cytidine deaminase (cytidine aminohydrolase, EC 3.5.4.5) activity increased with erythropoietic maturation, as it does during murine erythropoiesis in vivo. Stimulation of cellular proliferation of stationary erythroleukemic cells resulted in a marked increase in the activities of purine biosynthetic enzymes. These data provide a convincing example of repression and derepression of the PRA synthesizing enzymes in mammalian cells in vitro, and further evidence that the regulatory mechanisms operative in the normal development of erythrocytes can be activated by exposure of erythroleukemic cells to dimethylsulfoxide.  (+info)

Interdomain signaling in glutamine phosphoribosylpyrophosphate amidotransferase. (4/86)

The glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase-catalyzed synthesis of phosphoribosylamine from PRPP and glutamine is the sum of two half-reactions at separated catalytic sites in different domains. Binding of PRPP to a C-terminal phosphoribosyltransferase domain is required to activate the reaction at the N-terminal glutaminase domain. Interdomain signaling was monitored by intrinsic tryptophan fluorescence and by measurements of glutamine binding and glutamine site catalysis. Enzymes were engineered to contain a single tryptophan fluorescence reporter in key positions in the glutaminase domain. Trp(83) in the glutamine loop (residues 73-84) and Trp(482) in the C-terminal helix (residues 471-492) reported fluorescence changes in the glutaminase domain upon binding of PRPP and glutamine. The fluorescence changes were perturbed by Ile(335) and Tyr(74) mutations that disrupt interdomain signaling. Fluoresence titrations of PRPP and glutamine binding indicated that signaling defects increased the K(d) for glutamine but had little or no effect on PRPP binding. It was concluded that the contact between Ile(335) in the phosphoribosyltransferase domain and Tyr(74) in the glutamine site is a primary molecular interaction for interdomain signaling. Analysis of enzymes with mutations in the glutaminase domain C-terminal helix and a 404-420 peptide point to additional signaling interactions that activate the glutamine site when PRPP binds.  (+info)

Lesions in the nuo operon, encoding NADH dehydrogenase complex I, prevent PurF-independent thiamine synthesis and reduce flux through the oxidative pentose phosphate pathway in Salmonella enterica serovar typhimurium. (5/86)

In Salmonella enterica serovar Typhimurium, PurF-independent thiamine synthesis (or alternative pyrimidine biosynthesis) allows strains, under some growth conditions, to synthesize thiamine in the absence of the first step in the purine biosynthetic pathway. Mutations have been isolated in a number of loci that prevent this synthesis and thus result in an Apb(-) phenotype. Here we identify a new class of mutations that prevent PurF-independent thiamine synthesis and show that they are defective in the nuo genes, which encode the major, energy-generating NADH dehydrogenase of the cell. Data presented here indicated that a nuo mutant has reduced flux through the oxidative pentose phosphate pathway that may contribute to, but is not sufficient to cause, the observed thiamine requirement. We suggest that reduction of the oxidative pentose phosphate pathway capacity in a nuo mutant is an attempt to restore the ratio between reduced and oxidized pyridine nucleotide pools.  (+info)

A purine auxotroph deficient in phosphoribosylpyrophosphate amidotransferase and phosphoribosylpyrophosphate aminotransferase activities with normal activity of ribose-5-phosphate aminotransferase. (6/86)

Three enzyme reactions have been reported to catalyze the synthesis of phosphoribosylamine in eukaryotic cells. These activities are glutamine phosphoribosylpyrophosphate (P-Rib-P-P) amidotransferase [amidophosphoribosyl-transferase; 5-phosphoribosylamine: pyrophosphate phosphoribosyltransferase (glutamate-amidating) EC 2.4.2.14], ammonia P-Rib-P-P aminotransferase, and ammonia ribose-5-phosphate aminotransferase. A purine auxotroph derived from a cell line of Chinese hamster fibroblasts was shown to be deficient in catalytic activities of glutamine P-Rib-P-P amidotransferase and ammonia P-Rib-P-P aminotransferase. Extracts from this cell line had normal ammonia ribose-5-phosphate aminotransferase activity. The defect in purine biosynthesis in the mutant cell line was localized to the synthesis of phosphoribosylamine. These results indicate that glutamine P-Rib-P-P amidotransferase or ammonia P-Rib-P-P aminotransferase or both are important for phosphoribosylamine synthesis, but that ammonia ribose-5-phosphate aminotransferase activity probably does not play a significant role in this eukaryotic cell line. The simultaneous disappearance of both P-Rib-P-P-dependent activities suggests these two enzyme activities are closely related structurally or genetically.  (+info)

Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain signaling and intermediate channeling. (7/86)

Glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase catalyzes the first reaction of de novo purine nucleotide synthesis in two steps at two sites. Glutamine is hydrolyzed to glutamate plus NH(3) at an N-terminal glutaminase site, and NH(3) is transferred through a 20-A hydrophobic channel to a distal PRPP site for synthesis of phosphoribosylamine. Binding of PRPP is required to activate the glutaminase site (termed interdomain signaling) to prevent the wasteful hydrolysis of glutamine in the absence of phosphoribosylamine synthesis. Mutations were constructed to analyze the function of the NH(3) channel. In the wild type enzyme, NH(3) derived from glutamine hydrolysis was transferred to the PRPP site, and little or none was released. Replacement of Leu-415 at the PRPP end of the channel with an alanine resulted in a leaky channel and release of NH(3) to the solvent. Mutations in five amino acids that line the channel and two other residues required for the reorganization of phosphoribosyltransferase domain "flexible loop" that leads to formation of the channel perturbed channel function as well as interdomain signaling. The data emphasize the role of the NH(3) channel in coupling interdomain signaling and NH(3) transfer.  (+info)

Temperature-dependent function of the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel and coupling with glycinamide ribonucleotide synthetase in a hyperthermophile. (8/86)

Genes encoding glutamine phosphoribosylpyrophosphate amidotransferase (GPAT) and glycinamide ribonucleotide synthetase (GARS) from Aquifex aeolicus were expressed in Escherichia coli, and the enzymes were purified to near homogeneity. Both enzymes were maximally active at a temperature of at least 90 degrees C, with half-lives of 65 min for GPAT and 60 h for GARS at 80 degrees C. GPAT activity is known to depend upon channeling of NH(3) from a site in an N-terminal glutaminase domain to a distal phosphoribosylpyrophosphate site in a C-terminal domain where synthesis of phosphoribosylamine (PRA) takes place. The efficiency of channeling of NH(3) for synthesis of PRA was found to increase from 34% at 37 degrees C to a maximum of 84% at 80 degrees C. The mechanism for transfer of PRA to GARS is not established, but diffusion between enzymes as a free intermediate appears unlikely based on a calculated PRA half-life of approximately 0.6 s at 90 degrees C. Evidence was obtained for coupling between GPAT and GARS for PRA transfer. The coupling was temperature dependent, exhibiting a transition between 37 and 50 degrees C, and remained relatively constant up to 90 degrees C. The calculated PRA chemical half-life, however, decreased by a factor of 20 over this temperature range. These results provide evidence that coupling involves direct PRA transfer through GPAT-GARS interaction rather than free diffusion.  (+info)

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The protein encoded by this gene is a member of the purine/pyrimidine phosphoribosyltransferase family. It is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosythetic pathway. This gene and PAICS/AIRC gene, a bifunctional enzyme catalyzing steps six and seven of this pathway, are located in close proximity on chromosome 4, and divergently transcribed from an intergenic region. [provided by RefSeq, Mar 2011 ...
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List of all the English words with 30 letters containing letter B. amidophosphoribosyltransferase, dimethylacetylenedicarboxylate, methylenedioxybenzylpiperazine
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Tay, B S.; Lilley, R M.; Murray, A W.; and Atkinson, M R., "Inhibition of phosphoribosyl pyrophosphate amidotransferase from ehrlich ascites-tumour cells by thiopurine nucleotides." (1969). Subject Strain Bibliography 1969. 1170 ...
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Background: Cell proliferation occurs not only in normal but also in cancer cells. Most of cell proliferation inhibition can be done by inhibiting the DNA synthesis, notably by intervening the formation of purine or pyrimidine. In purine de novo synthesis, it was assumed that biotin plays a role as a coenzyme in carboxylation reaction, one of the pivotal steps in the purine de novo pathways. The aim of this study was to see the avidin potency to bind biotin and inhibit mitosis.. Methods: Peripheral blood mononuclear cell (PBMC) was cultured in RPMI-1640 medium and stimulated by phytohemagglutinin (PHA) in the presence or absence of interleukin-2 (IL-2), with or without avidin. The effect of avidin addition was observed at 24, 48, and 72 hours for cell proliferation, viability, and cell cycle. Statistical analysis was done by one-way ANOVA.. Results: Avidin inhibited cell proliferation and viability in culture under stimulation by PHA with and without IL-2. Cell cycle analysis showed that avidin ...
The protein encoded by this gene is a member of the purine/pyrimidine phosphoribosyltransferase family. It is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosythetic pathway. This gene and PAICS/AIRC gene, a bifunctional enzyme catalyzing steps six and seven of this pathway, are located in close proximity on chromosome 4, and divergently transcribed from an intergenic region ...
Rate limiting enzymes Glycolysis- Phosphofructokinase 1f Gluconeogenesis- Fructose 1,6 bisphosphatase Glycogen synthesis- Glycogen synthase Glycogenolysis-Glycogen Phosphorylase Fatty acid synthesis- AcetylCoA Carboxylase Fatty acid beta oxidation-Carnitine acyl transferase 1 Lipolysis- hormone sensitive lipase Purine metabolism- PRPP Amidotransferase Pyrimidine metabolism- Aspartate transacetylase Ketone body synthesis-HMG CoA synthase Cholesterol synthesis- HMG CoA resuctase Bile acid synthesis- 7 Alpha hydroxylase Uric acid synthesis- xanthine oxidase Catecholamine synthesis- Tyrosine hydroxylase Urea cycle- Carbamoyl Phosphate synthase 1 Pentose phosphate pathway- Glucose-6-Phosphate dehydrogenase Krebs- Isocitrate dehydrogenase Adrenal hormones- Desmolase Porphyrin/Haem synthesis- ALA synthase Postaglandin synthesis- PG ...
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Based on the results of these studies we propose that accelerated purine nucleotide synthesis and uric acid overproduction in our patient resulted from PRS superactivity due to a point mutation in PRPS1, a T-for-A substitution at nucleotide 578 in the PRPS1 coding region. This mutation has 2 distinct functional effects on the activity of the PRS1 isoform thus encoded. First, as is the case in most of the point mutations encountered to date in affected male patients (6), the mutant PRS1 in our patient appears to be more labile than its normal counterpart, resulting in reduced concentrations and activities of the mutant isoform in the patients cells and accounting for the subnormal maximum PRS activities measured in her cell extracts at maximally activating Pi concentrations. Second, the mutation in the patients PRS1 imparts altered allosteric regulatory properties on the activity of the isoform. These altered properties include increased responsiveness of enzyme activity to activation by Pi ...
An intricate system of interrelated control mechanisms regulate biochemical reaction sequences. Metabolic pathways are controlled not only by specific activity and inherent kinetic properties of...
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1P19: Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase.
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This chapter discusses the de novo pathway of pyrimidine nucleotide biosynthesis. Animals do not have a dietary requirement for pyrimidines, and many microorgan
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TY - JOUR. T1 - Differential effects of inhibitors of purine metabolism on two trichomonad species. AU - Wang, Ching C.. AU - Verham, Ron. AU - Hui-wen, Cheng. AU - rice, Audie. AU - Wang, Alice L.. PY - 1984/4/15. Y1 - 1984/4/15. N2 - Tritrichomonas foetus and Trichomonas vaginalis are both incapable of de novo purine nucleotide synthesis. Previous studies indicated that T. foetus relies mainly on the salvage of hypoxanthine and subsequent conversion of IMP to AMP and GMP, whereas T. vaginalis depends on direct conversions of exogenous adenosine to AMP and guanosine to GMP without much interconversion between the two nucleotides. These two different types of purine salvage suggest the possibility of differential sensitivities between the two species of trichomonad flagellates toward different purine antimetabolites. Mycophenolic acid, hadacidin, 8-azaguanine, and formycin B inhibited the growth of T. foetus but had no effect on T. vaginalis. Mycophenolic acid acted by blocking conversion of IMP ...
Schistosoma mansoni do not have de novo purine pathways and rely on purine salvage for their purine supply. It has been demonstrated that, unlike humans, the S. mansoni is able to produce adenine directly from adenosine, although the enzyme responsible for this activity was unknown. In the present work we show that S. mansoni 5´-deoxy-5´-methylthioadenosine phosphorylase (MTAP, E.C. 2.4.2.28) is capable of use adenosine as a substrate to the production of adenine. Through kinetics assays, we show that the Schistosoma mansoni MTAP (SmMTAP), unlike the mammalian MTAP, uses adenosine substrate with the same efficiency as MTA phosphorolysis, which suggests that this enzyme is part of the purine pathway salvage in S ...
Ammonia transfer from the glutamine site to the fructose-6P site of bacterial glucosamine-6-phosphate synthase was studied by molecular dynamics simulations. The studies suggest a key role for Trp74, in the sealing of the hydrophobic channel connecting the two binding sites, as well as for the two Ala602 and Val605 residues, which form a narrow passage whose opening/closing constitutes an essential event in ammonia transfer. Kinetic analyses of the corresponding protein mutants confirmed our predictions. The efficiency of ammonia transfer which was close to zero in the W74A mutant was partially restored by increasing the size of the corresponding side-chain; the simulations performed on the W74A mutant suggested the formation of a hole in the channel. In the case of A602L and V605L mutants, the efficiency of ammonia transfer decreased to 50% of the value of the native protein. None of the mutants were, however, able to use exogenous ammonia as a substrate.
Camille Prats husband, Anthony Linsangan 32, passed away at 8:45 a.m., September 23, because of cancer.. Camilles husband died of nasopharyngeal (throat) cancer. It affected his nasopharynx, the uppermost part of the pharynx.. Camille 26, is now a young widow.. She was a former child star and one of the main casts of Munting Heredera, got married to Linsangan in a civil wedding in Los Angeles, California on January 5, 2008, and a church wedding in Makati City on March 4, 2008.. Her husband left Prats a 3-year old son, Nathaniel Caesar.. ...
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How is De Novo Purine Synthesis abbreviated? DNPS stands for De Novo Purine Synthesis. DNPS is defined as De Novo Purine Synthesis somewhat frequently.
A short-root rice mutant was isolated from an ethyl methane sulfonate-mutagenized library. From map-based cloning strategy, a point mutation, resulting in an amino acid change from proline to leucine, was identified in the fourth exon of a glutamyl-tRNA (Gln) amidotransferase B subunit family protein (OsGatB, LOC_Os11g34210). This gene is an ortholog of Arabidopsis GatB and yeast PET112. GatB is a subunit of tRNA-dependent amidotransferase (AdT), an essential enzyme involved in Gln-tRNAGln synthesis in mitochondria. Although previous studies have described that cessation in mitochondrial translation is lethal at very early developmental stages in plants, this point mutation resulted in a non-lethal phenotype of smaller root meristem and shorter root cell length. In the root, OsGatB was predominantly expressed in the root tip and played an important role in cell division and elongation there. OsGatB was localized in the mitochondria, and mitochondrial structure and function were all affected in Osgatb
TY - JOUR. T1 - Short-term metabolic fate of 13N-labeled glutamate, alanine, and glutamine(amide) in rat liver. AU - Cooper, A. J.L.. AU - Nieves, E.. AU - Rosenspire, K. C.. AU - Filc-DeRicco, S.. AU - Gelbard, A. S.. AU - Brusilow, S. W.. PY - 1988/12/1. Y1 - 1988/12/1. N2 - Tracer quantities (in 0.2 ml) of 13N-labele glutamate, alanine, or glutamine(amide) were administered rapidly (≤ 2 s) via the portal vein of anesthetized adult male rats. Liver content of tracer at 5 s was 57 ± 6 (n = 6), 24 ± 1 (n = 3), and 69 ± 7 (n = 3) % of the injected dose, respectively. Portal-hepatic vein differences for the corresponding amino acids were 17 ± 6, 26 ± 8, and 19 ± 9% (n = 4), respectively, suggesting some export of glutamate and glutamine, but not of alanine, to the hepatic vein. Following L-[13N]glutamate administration, label rapidly appeared in liver alanine and aspartate (within seconds). The data emphasize the rapidity of nitrogen exchange via linked transaminases. By 30 s following ...
2BPQ: The Crystal Structure of Trpd, a Metabolic Enzyme Essential for Lung Colonization by Mycobacterium Tuberculosis, in Complex with its Substrate Phosphoribosylpyrophosphate
An enzyme that catalyzes the formation of 2 molecules of glutamate from Glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13 ...
Mario Prats Computer Science Engineer T B marioprats [AT] gmail.com twitter youtube - pratsmario, IRSLab Linkedin Short bio Mario Prats was born on
This is a list of all employees at the Department of Biomedical Sciences. The list is sorted in alphabetical order in accordance to the employees first name.
Molecular association of cancer cell metastasis with signaling pathways has been explicated so as to aid in the development of new prognostic models for better cancer therapies. However, those metastatic signaling pathways are barely explored to take account of the functions of enzymes involved in cellular metabolism. Particularly, the metabolic enzymes in de novo purine biosynthesis have been overlooked for their potential roles in cancer cell metastasis even though they have been successfully validated anti-cancer drug targets. Meanwhile, several lines of recent discoveries on de novo purine biosynthesis suggest that the spatiotemporal assembly of purine biosynthetic enzymes, the purinosome, is under controls of signaling pathways in cancer cells. The results of the inquiry reveal an unanticipated mechanism of action of 3-phosphoinositide-dependent protein kinase 1 (PDK1) signaling pathways in regulation of purine biosynthesis in an Akt-independent manner. Considering the biological action of ...
The effect of a temperature rise from 28 to 37 degrees C on the biosynthesis of 5-inosine acid (IMP) by the mutant Brevibacterium ammoniagenes 225-5 was studied. The inhibitory effect of increased temperature on the IMP biosynthesis was dependent on the adenine concentration. The study of IMP synthesis on the media with different adenine concentrations showed that adenine controlled not only the synthesis of purines de novo but also, to a larger extent, so-called salvage IMP synthesis from hypoxanthine. The effect of increased temperature was identical to that of excessive adenine. Temperature rise as well as increase in adenine concentration intensified metabolic processes (increased the level of glucose consumption and the rate of nucleic acid synthesis) and restored in part cell permeability. This was indicated by the release of protein and ribose-5-phosphate into the culture fluid, and by the change in cell morphology. An optimal adenine concentration may be altered either way in response ...
et al. Involvement of exogenous purines and purine nucleotides in nucleic acid biosynthesis in plague microorganism // Voprosy meditsinskoi khimii. - 1968. - V. 14. -N 1. - P. 48-53 ...
TY - JOUR. T1 - Bioanalysis of 6-diazo-5-oxo-l-norleucine in plasma and brain by ultra-performance liquid chromatography mass spectrometry. AU - Alt, Jesse. AU - Potter, Michelle C.. AU - Rojas, Camilo. AU - Slusher, Barbara. PY - 2015/4/1. Y1 - 2015/4/1. N2 - Glutamine is an abundant amino acid that plays pivotal roles in cell growth, cell metabolism, and neurotransmission. Dysregulation of glutamine-using pathways has been associated with pathological conditions such as cancer and neurodegenerative diseases. 6-Diazo-5-oxo-l-norleucine (DON) is a reactive glutamine analog that inhibits enzymes affecting glutamine metabolism such as glutaminase, 2-N-amidotransferase, l-asparaginase, and several enzymes involved in pyrimidine and purine de novo synthesis. As a result, DON is actively used in preclinical models of cancer and neurodegenerative disease. Moreover, there have been several clinical trials using DON to treat a variety of cancers. Considerations of dose and exposure are especially ...
The purinosome is a putative multi-enzyme complex that carries out de novo purine biosynthesis within the cell. It is postulated to include all six of the human enzymes identified as direct participants in this ten-step biosynthetic pathway converting phosphoribosyl pyrophosphate to inosine monophosphate: The enzymes of the multi-step de novo purine biosynthesis pathway have been postulated to form a multi-enzyme complex to facilitate substrate channeling between each enzyme of the pathway. Slight variations of the pathway exists between phyla; however, there are 13 enzymes that can be considered part of this biosynthetic pathway. Several individual enzymatic functions have consolidated onto single bifunctional or trifunctional polypeptide chains in higher organisms, suggesting stable physical interactions exist between enzymes. The functional consolidation of steps 2,3, and 5 of the pathway into a single enzyme in higher organisms such as humans suggests physical local proximity of the enzyme ...
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Organise in kick upstairs the C. H. Best that you prat ahead a voice communication. What do you project to sound out? If youre incertain of a fact, do your inquiry before adding it to your delivery. Invest your thoughts push down on report. Practise your delivery a telephone number of times until you make it memorized. The Thomas More time you make to be prepared, the more than convinced you leave be patch speaking ...
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family (333 aa ...
It is generated from Phosphoribosyl pyrophosphate (PRPP). Amidophosphoribosyltransferase Phosphoribosyl pyrophosphate. ...
amidophosphoribosyltransferase MEROPS: clan PB, family C44 *^ Subtilisin MEROPS: clan SB, family S8 ...
Increased levels of these ribotides may cause feedback inhibition of amidophosphoribosyl transferase, the first and rate- ...
... write AmidoPhosphoRibosylTransferase instead of amidophosphoribosyltransferase. This usage was not widely adopted. Camelcase is ...
... the enzyme amidophosphoribosyltransferase acts upon PRPP to create phosphoribosylamine. Increased levels of PRPP is ...
... catalyzed by amidophosphoribosyltransferase, which is activated by PRPP and inhibited by AMP, GMP and IMP. PRPP + L-Glutamine ... researchers have suggested that the compound is channeled from amidophosphoribosyltransferase to GAR synthetase in vivo. PRA + ...
... amidophosphoribosyltransferase EC 2.4.2.15: guanosine phosphorylase EC 2.4.2.16: urate-ribonucleotide phosphorylase EC 2.4.2.17 ...
... amidophosphoribosyltransferase MeSH D08.811.913.400.725.160 --- anthranilate phosphoribosyltransferase MeSH D08.811.913.400. ...
Amidophosphoribosyl transferase at the US National Library of Medicine Medical Subject Headings (MeSH) Human PPAT genome ... Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an ... researchers have suggested that the compound is channeled from Amidophosphoribosyltransferase to GAR synthetase in vivo. Click ... "Molecular cloning of human amidophosphoribosyltransferase". Biochemical and Biophysical Research Communications. 190 (1): 192- ...
OST is a component of the translocon in the endoplasmic reticulum (ER) membrane. A lipid-linked core-oligosaccharide is assembled at the membrane of the endoplasmic reticulum and transferred to selected asparagine residues of nascent polypeptide chains by the oligosaccharyl transferase complex.[3] The active site of OST is located about 4 nm from the lumenal face of the ER membrane.[4] It usually acts during translation as the nascent protein is entering the ER, but this cotranslational glycosylation is nevertheless called a posttranslational modification. A few examples have been found of OST activity after translation is complete.[5][6] Current opinion is that post-translational activity may occur if the protein is poorly folded or folds slowly.[6] ...
... is regulated by both allosteric control and by phosphorylation.. Hormones such as epinephrine, insulin and glucagon regulate glycogen phosphorylase using second messenger amplification systems that are linked to G proteins. Glucagon activates adenylate cyclase through a seven transmembrane receptor coupled to Gs which, in turn, activates adenylate cyclase to increase intracellular concentrations of cAMP. cAMP binds to and releases an active form of protein kinase A (PKA). Next, PKA phosphorylates phosphorylase kinase, which, in turn, phosphorylates glycogen phosphorylase b, transforming it into the active glycogen phosphorylase a. This phosphorylation is added onto the glycogen phosphorylase b serine 14. In the liver, glucagon activates another G-protein-linked receptor that triggers a different cascade, resulting in the activation of Phospholipase C (PLC). PLC indirectly causes the release of calcium from the hepatocytes' endoplasmic reticulum into the cytosol. The ...
Amidophosphoribosyltransferase. *Phosphoribosylglycinamide formyltransferase. *AIR synthetase (FGAM cyclase). * ...
Amidophosphoribosyltransferase. *Phosphoribosylglycinamide formyltransferase. *AIR synthetase (FGAM cyclase). * ...
... acts by the following mechanism: First, the B subunit ring of the cholera toxin binds to GM1 gangliosides on the surface of target cells. The B subunit can also bind to cells lacking GM1. The toxin then most likely binds to other types of glycans, such as Lewis Y and Lewis X, attached to proteins instead of lipids.[7][8][9] Once bound, the entire toxin complex is endocytosed by the cell and the cholera toxin A1 (CTA1) chain is released by the reduction of a disulfide bridge. The endosome is moved to the Golgi apparatus, where the A1 protein is recognized by the endoplasmic reticulum chaperone, protein disulfide isomerase. The A1 chain is then unfolded and delivered to the membrane, where Ero1 triggers the release of the A1 protein by oxidation of protein disulfide isomerase complex.[10] As the A1 protein moves from the ER into the cytoplasm by the Sec61 channel, it refolds and avoids deactivation as a result of ubiquitination. CTA1 is then free to bind with a human partner protein ...
Amidophosphoribosyltransferase. *Phosphoribosylglycinamide formyltransferase. *AIR synthetase (FGAM cyclase). * ...
... is a glucosyltransferase enzyme involved in the generation of beta-glucan in fungi. It serves as a pharmacological target for antifungal drugs such as caspofungin, anidulafungin, and micafungin, deemed 1,3-Beta-glucan synthase inhibitors. The biosynthesis of disaccharides, oligosaccharides, and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates (EC 2.4.1.-.), and related proteins into distinct sequence-based families has been described.[1] This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site . The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of ...
Amidophosphoribosyltransferase precursor (Homo sapiens) PC. C26, C56. Gamma-glutamyl hydrolase (Rattus norvegicus) ...
Amidophosphoribosyltransferase, N-terminal (IPR035584). Short name: PurF_N Domain relationships *Glutamine amidotransferase ... also known as amidophosphoribosyltransferase. The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the ...
Amidophosphoribosyl transferase at the US National Library of Medicine Medical Subject Headings (MeSH) Human PPAT genome ... Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an ... researchers have suggested that the compound is channeled from Amidophosphoribosyltransferase to GAR synthetase in vivo. Click ... "Molecular cloning of human amidophosphoribosyltransferase". Biochemical and Biophysical Research Communications. 190 (1): 192- ...
Recombinant Protein and Amidophosphoribosyltransferase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Amidophosphoribosyltransferase 1 Recombinant. Amidophosphoribosyltransferase 1 Antibody ASE1 ELISA Kit. ASE1 Recombinant. ASE1 ... Amidophosphoribosyltransferase 2 Recombinant. Amidophosphoribosyltransferase 2 Antibody ASE2 ELISA Kit. ASE2 Recombinant. ASE2 ... Amidophosphoribosyltransferase 3 Recombinant. Amidophosphoribosyltransferase 3 Antibody ASE3 ELISA Kit. ASE3 Recombinant. ASE3 ...
The protein encoded by this gene is a member of the purine/pyrimidine phosphoribosyltransferase family. It is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosythetic pathway. This gene and PAICS/AIRC gene, a bifunctional enzyme catalyzing steps six and seven of this pathway, are located in close proximity on chromosome 4, and divergently transcribed from an intergenic region. [provided by RefSeq, Mar 2011 ...
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Purchase Recombinant Pseudomonas aeruginosa Amidophosphoribosyltransferase(purF). It is produced in Yeast. High purity. Good ... Recommended name: Amidophosphoribosyltransferase Short name= ATase EC= 2.4.2.14 Alternative name(s): Glutamine ... Recombinant Pseudomonas aeruginosa Amidophosphoribosyltransferase(purF). Recombinant Pseudomonas aeruginosa ...
amidophosphoribosyltransferase. And here is another: phosphoribulosyl. forminoaminoimidazolcarboxamidoribotide.. Do you find ... So the two examples above would read: AmidoPhosphoRibosylTransferase and. PhosphoRibulosyl ... amidophosphoribosyltransferase. And here is another: phosphoribulosyl forminoaminoimidazolcarboxamidoriboti ...
Amidophosphoribosyltransferase (purF). *Phosphoribosylamine--glycine ligase (purD). This subpathway is part of the pathway IMP ...
Amidophosphoribosyltransferase (purF). *Phosphoribosylamine--glycine ligase (purD). This subpathway is part of the pathway IMP ...
Molecular cloning of human amidophosphoribosyltransferase. (PMID: 8380692) Iwahana H … Itakura M (Biochemical and biophysical ...
Amidophosphoribosyltransferase [Precursor]. *ATase. *Glutamine phosphoribosylpyrophosphatate amidotransferase. *Glutamine ...
amidophosphoribosyltransferase MEROPS: clan PB, family C44 *^ Subtilisin MEROPS: clan SB, family S8 ...
... amidophosphoribosyltransferase [EC:2.4.2.14] K00764 purF; amidophosphoribosyltransferase [EC:2.4.2.14] K00820 glmS; glutamine ... 107737308 amidophosphoribosyltransferase-like 107749915 glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2-like ...
It is generated from Phosphoribosyl pyrophosphate (PRPP). Amidophosphoribosyltransferase Phosphoribosyl pyrophosphate. ...
Inhibition of Murine Amido Phosphoribosyltransferase by Folate Derivatives Sarah L. Schoettle, Richard I. Christopherson ...
Accepted name: amidophosphoribosyltransferase Reaction: 5-phospho-β-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + ... EC 2.4.2.14 amidophosphoribosyltransferase EC 2.4.2.15 guanosine phosphorylase EC 2.4.2.16 urate-ribonucleotide phosphorylase ...
UAmidophosphoribosyltransferase. Not Available. Bacillus subtilis (strain 168). UProtein-glutamine gamma-glutamyltransferase E ...
Details2. Amidophosphoribosyltransferase. Kind. Protein. Organism. Humans. Pharmacological action. Unknown. Actions. Product of ...
Protein Aliases: Amidophosphoribosyltransferase; ATase; glutamine phosphoribosylpyrophosphatate amidotransferase; Glutamine ...
amidophosphoribosyltransferase precursor. Comment. Comment: REVIEWED REFSEQ: This record has been curated by NCBI staff. The ... amidophosphoribosyltransferase. Comment. Comment: REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference ... amidophosphoribosyltransferase isoform X1. Comment. Comment: MODEL REFSEQ: This record is predicted by automated computational ... amidophosphoribosyltransferase. glutamine PRPP amidotransferase. glutamine phosphoribosylpyrophosphatate amidotransferase. ...
... 14 amidophosphoribosyltransferase EC 2.4.2.15 guanosine phosphorylase EC 2.4.2.16 urate-ribonucleotide phosphorylase ...
Deficiency of amidophosphoribosyltransferase. *Deficiency of amine oxidase. *Deficiency of aminoacyl-histidine dipeptidase ...
BRENDA - The Comprehensive Enzyme Information System
In de novo generation of purines, the enzyme amidophosphoribosyltransferase acts upon PRPP to create phosphoribosylamine. Six ...
  • SUMMARY: Mutants of Saccharomyces cerevisiae deficient in adenine phosphoribosyltransferase (A-PRT, EC 2.4.2.7) have been isolated following selection for resistance to 8-azaadenine in a prototrophic strain carrying the ade4-su allele of the gene coding for amidophosphoribosyltransferase(EC 2.4.2.14). (microbiologyresearch.org)
  • Due to the chemical lability of PRA, which has a half-life of 38 seconds at PH 7.5 and 37 °C, researchers have suggested that the compound is channeled from Amidophosphoribosyltransferase to GAR synthetase in vivo. (wikipedia.org)
  • You need info about Chicken Amidophosphoribosyltransferase (PPAT) ELISA Kit or any other Gentaur produtct? (gentaurshop.com)
  • Increased amidophosphoribosyltransferase and decreased xanthine oxidase activity in human and rat renal cell carcinoma. (saladgaffe.tk)
  • This differential expression pattern may be related to the oxygen sensitivity of amidophosphoribosyltransferase. (elsevier.com)