Amidophosphoribosyltransferase: An enzyme, involved in the early steps of purine nucleotide biosynthesis, that catalyzes the formation of 5-phosphoribosylamine from glutamine and phosphoribosylpyrophosphate. EC 188.8.131.52.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 184.108.40.206.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.
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 220.127.116.11) 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 18.104.22.168], 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)
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- ...
It is generated from Phosphoribosyl pyrophosphate (PRPP). Amidophosphoribosyltransferase Phosphoribosyl pyrophosphate. ...
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 + ...
List of EC numbers (EC 2)
... amidophosphoribosyltransferase EC 22.214.171.124: guanosine phosphorylase EC 126.96.36.199: urate-ribonucleotide phosphorylase EC 188.8.131.52 ...
List of MeSH codes (D08)
... amidophosphoribosyltransferase MeSH D08.811.913.400.725.160 --- anthranilate phosphoribosyltransferase MeSH D08.811.913.400. ...
... family C59 amidophosphoribosyltransferase MEROPS: clan PB, family C44 Subtilisin MEROPS: clan SB, family S8 Prolyl ...
RCSB PDB - 1AO0: GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE FROM B. SUBTILIS COMPLEXED WITH ADP...
1AO0: Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.
RCSB PDB - 1ECG: DON INACTIVATED ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE...
1ECG: Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site.
amidophosphoribosyltransferase activity, animal organ regeneration, cellular response to drug, cellular response to insulin stimulus, G1/S transition of mitotic cell cycle, glutamine catabolic process, kidney development, lactation, maternal process involved in female pregnancy, protein homotetramerization
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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 ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
List of all the English words with 30 letters containing letter B. amidophosphoribosyltransferase, dimethylacetylenedicarboxylate, methylenedioxybenzylpiperazine
"Inhibition of phosphoribosyl pyrophosphate amidotransferase from ehrli" by B S. Tay, R M. Lilley et al.
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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DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC,...
The nucleotide sequence is described of a region of the Escherichia coli chromosome extending from oriC to phoS that also includes the loci gid, unc and glmS. Taken with known sequences for asnA and phoS this completes the sequence of a segment of about 17 kilobases or 0.4 min of the E. coli genome. Sequences that are probably transcriptional promoters for unc and phoS can be detected and the identity of the unc promoter has been confirmed by experiments in vitro with RNA polymerase. Upstream of the promoter sequence is an extensive region that appears to be non-coding. Conserved sequences are found that may serve to concentrate RNA polymerase in the vicinity of the unc promoter. Hairpin loop structures resembling known rho-independent transcription termination signals are evident following the unc operon and glmS. The glmS gene encoding the amidotransferase, glucosamine synthetase, has been identified by homology with glutamine 5-phosphoribosylpyrophosphate amidotransferase. ...
Avidin inhibits PHA-induced human peripheral blood mononuclear cell proliferation | Medical Journal of Indonesia
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 ...
Digestión anaerobia de la fracción sólida de purines de cerdo, separada mediante el proceso ECOpurín
CitacióMartínez-Almela, J. [et al.]. Digestión anaerobia de la fracción sólida de purines de cerdo, separada mediante el proceso ECOpurín. "Anaporc", 2001, vol. 1, núm. 1, p. 41-51 ...
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Phosphoribosylpyrophosphate synthetase overactivity as a cause of uric acid overproduction in a young woman - García-Pavía -...
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 ...
Observations of Altered Intracellular Phosphoribosylpyrophosphate (PP-Ribose-P) in Human Disease | SpringerLink
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...
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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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. 184.108.40.206) 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 channeling in bacterial glucosamine-6-phosphate synthase (Glms): molecular dynamics simulations and kinetic studies of...
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.
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Frontiers | OsGatB, the Subunit of tRNA-Dependent Amidotransferase, Is Required for Primary Root Development in Rice | Plant...
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
An enzyme that catalyzes the formation of 2 molecules of glutamate from Glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 220.127.116.11 ...
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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 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 ...
ADE12 - Adenylosuccinate synthetase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - ADE12 gene &...
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.
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Mycobacteria tuberculosis (Mtb), the causative agent of tuberculosis, is responsible for more death in the world today than any other bacteria. As part of the Tuberculosis Structural Genomics Consortium (TBSGC), our research group previously determined the structure of anthranilate phosphoribosyl transferase (AnPRT) from Mtb. AnPRT is the second enzyme in the tryptophan biosynthetic pathway and was identified as a potential drug target through gene knockout experiments, which resulted in a strain of Mtb that was essentially avirulent even in immunodeficient mice. AnPRT catalyses a reaction between anthranilate and phosphoribosylpyrophosphate (PRPP), and the crystal structure of Mtb-AnPRT was originally determined with and without PRPP (PDB ID: 1ZVW and 2BPQ, respectively). In silico docking was used to predict the binding motif of anthranilate, the second substrate, surprisingly predicted two sites despite a 1:1 reaction ratio with PRPP. Previously, 165 compounds were screened for inhibitory ...
This volume is designed to fill a void in the broad spectrum of disciplines in which uric acid has attracted the attention of scientists and to present in detail the recent progress in many of these disciplines. There are 27 different authors, leading to considerable variation in quality and some overlapping of discussions, but both are kept to a minimum. Included are detailed chapters on the chemistry and synthesis of uric acid, the regulation of purine nucleotide biosynthesis de novo and by way of salvage enzymes. Discussions of purine nucleotide interconversions and their degradation and inter-relationships of pyrimidine metabolism are ...
This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli , IfnA in P. aeriginosa  and PseA in C. jejuni . Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when ...
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1. As per usual, the media got it all wrong. For example, Kenneth Chang in the New York Times began his discussion of the article with the headline: "Study Suggests Math Teachers Scrap Balls and Slices," followed by a non sequitor having to do with trains leaving stations 400 miles apart and the reader is asked to determine the time the trains pass each other. Why might Chang have introduced this irrelevancy? 2. The supporting online material for this study may be found here and is well worth reading. In it, you will find details about the generic and the three concrete examples for explaining the commutative mathematical group of order three. Which of the four do you find the easiest to understand? Take the learning phase of your choice and see how well you do. Then, take the "Test of Transfer Domain" on page 26 and see how well you do on this phase. 3. If you have looked at the supporting material you will note that the questions are multiple choice, some questions of which have only two ...
Helium-filled balloons floated through the air to mark the dedication of the new women`s center for obstetrical and gynecological services at Humana Hospital South Broward.``This is a signal that
Amidophosphoribosyltransferase, N-terminal (IPR035584) | InterPro | EMBL-EBI
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 ...http://www.ebi.ac.uk/interpro/entry/IPR035584
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 ...https://pharos.nih.gov/idg/targets/Q06203
WikiGenes - PPAT - phosphoribosyl pyrophosphate amidotransferase
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.https://www.wikigenes.org/e/gene/e/5471.html
Words in 30 letters with B
amidophosphoribosyltransferase An enzyme that converts phosphoribosylpyrophosphate into 5-phosphoribosylamine.. → Definition ... and anagrams of amidophosphoribosyltransferase. → Other senses and detailed information on the Wiktionnary ...https://lotsofwords.com/b/30-letters
Amidophosphoribosyltransferase - Wikipedia
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- ...https://en.wikipedia.org/wiki/Amidophosphoribosyltransferase
Amidophosphoribosyltransferase elisa and antibody
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 ...https://www.mybiosource.com/proteins-family/amidophosphoribosyltransferase
Recombinant Pseudomonas aeruginosa Amidophosphoribosyltransferase(purF) - Cusabio
Purchase Recombinant Pseudomonas aeruginosa Amidophosphoribosyltransferase(purF). It is produced in Yeast. High purity. Good ... Recommended name: Amidophosphoribosyltransferase Short name= ATase EC= 18.104.22.168 Alternative name(s): Glutamine ... Recombinant Pseudomonas aeruginosa Amidophosphoribosyltransferase(purF). Recombinant Pseudomonas aeruginosa ...https://www.cusabio.com/Recombinant-Protein/Recombinant-Pseudomonas-aeruginosa-AmidophosphoribosyltransferasepurF-765356.html
Feedback | New Scientist
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 ...https://www.newscientist.com/article/mg15821399-900-feedback/
purD - Phosphoribosylamine--glycine ligase - Methanococcus maripaludis (strain S2 / LL) - purD gene & protein
Amidophosphoribosyltransferase (purF). *Phosphoribosylamine--glycine ligase (purD). This subpathway is part of the pathway IMP ...http://www.uniprot.org/uniprot/Q6M079
purD - Phosphoribosylamine--glycine ligase - Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 /...
Amidophosphoribosyltransferase (purF). *Phosphoribosylamine--glycine ligase (purD). This subpathway is part of the pathway IMP ...http://www.uniprot.org/uniprot/Q58347
PPAT Gene - GeneCards | PUR1 Protein | PUR1 Antibody
Molecular cloning of human amidophosphoribosyltransferase. (PMID: 8380692) Iwahana H … Itakura M (Biochemical and biophysical ...https://www.genecards.org/cgi-bin/carddisp.pl?id_type=entrezgene&id=5471
Recombinant Human Phosphoribosyl pyrophosphate amidotransferase protein (ab159164)
Amidophosphoribosyltransferase [Precursor]. *ATase. *Glutamine phosphoribosylpyrophosphatate amidotransferase. *Glutamine ...http://www.abcam.com/recombinant-human-phosphoribosyl-pyrophosphate-amidotransferase-protein-ab159164.html
KEGG BRITE: KEGG Orthology (KO) - Cricetulus griseus (Chinese hamster)
... amidophosphoribosyltransferase [EC:22.214.171.124] ...http://www.genome.jp/kegg-bin/get_htext?cge00001+100774486
KEGG BRITE: KEGG Orthology (KO) - Mycobacterium tuberculosis Haarlem
TBHG_00798 amidophosphoribosyltransferase PurF K00278 nadB; L-aspartate oxidase [EC:126.96.36.199] K01424 E188.8.131.52; L-asparaginase [ ...http://www.genome.jp/kegg-bin/get_htext?mtul00001+TBHG_00332
Accepted name: amidophosphoribosyltransferase Reaction: 5-phospho-β-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + ... EC 184.108.40.206 amidophosphoribosyltransferase EC 220.127.116.11 guanosine phosphorylase EC 18.104.22.168 urate-ribonucleotide phosphorylase ...https://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/0402.html
Guanosine-5'-Monophosphate - DrugBank
UAmidophosphoribosyltransferase. Not Available. Bacillus subtilis (strain 168). UProtein-glutamine gamma-glutamyltransferase E ...https://www.drugbank.ca/drugs/DB01972
L-Glutamine - DrugBank
Details2. Amidophosphoribosyltransferase. Kind. Protein. Organism. Humans. Pharmacological action. Unknown. Actions. Product of ...https://www.drugbank.ca/drugs/DB00130
PPAT Antibody (PA5-83310)
Protein Aliases: Amidophosphoribosyltransferase; ATase; glutamine phosphoribosylpyrophosphatate amidotransferase; Glutamine ...https://www.thermofisher.com/antibody/product/PPAT-Antibody-Polyclonal/PA5-83310
... 14 amidophosphoribosyltransferase EC 22.214.171.124 guanosine phosphorylase EC 126.96.36.199 urate-ribonucleotide phosphorylase ...https://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/4/2/
Purine and Pyrimidine Metabolism in Man VIII | SpringerLink
Inhibition of Murine Amido Phosphoribosyltransferase by Folate Derivatives Sarah L. Schoettle, Richard I. Christopherson ...https://link.springer.com/book/10.1007%2F978-1-4615-2584-4
SMART: Secondary literature for AICARFT IMPCHas domain
Genomic structure of rat amidophosphoribosyltransferase (ATase; EC 188.8.131.52), which catalyzes the first committed step in de ... Rat genomic structure of amidophosphoribosyltransferase, cDNA sequence of aminoimidazole ribonucleotide carboxylase, and cell ...http://smart.embl-heidelberg.de/smart/show_secondary.cgi?domain=AICARFT_IMPCHas
Untersuchungen von Sink / Source Verhältnissen in transgenen Kartoffeln (Solanum tuberosum), welche den PsGPT und AtNTT1...
GPT , NTT , Amidophosphoribosyltransferase , Kartoffel , Stärke. German. GPT , NTT , Amidophosphoribosyltransferase , starch , ...http://kups.ub.uni-koeln.de/2877/
Principles of Biochemistry/Nucleic acid III: Sythesis of nucleotides - Wikibooks, open books for an open world
In de novo generation of purines, the enzyme amidophosphoribosyltransferase acts upon PRPP to create phosphoribosylamine. Six ...https://en.wikibooks.org/wiki/Principles_of_Biochemistry/Nucleic_acid_III:_Sythesis_of_nucleotides
Phosphoribosylamine - Wikipedia
It is generated from Phosphoribosyl pyrophosphate (PRPP). Amidophosphoribosyltransferase Phosphoribosyl pyrophosphate. ...https://en.wikipedia.org/wiki/Phosphoribosylamine
- Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme responsible for catalyzing the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the ammonia group from a glutamine side-chain. (wikipedia.org)
- Also known as Amidophosphoribosyltransferase (ATase) (Glutamine phosphoribosylpyrophosphate amidotransferase). (mybiosource.com)
- The reciprocal plots for 5-phosphoribosyl-1-pyrophosphate (PRPP) of liver and hepatoma enzymes gave apparent KmS of 2 microM for adenine phosphoribosyltransferase and 4 microM for HGPRT, showing two orders of magnitude higher affinities for PRPP than that of the rate-limiting enzyme of de novo purine synthesis, amidophosphoribosyltransferase (EC 184.108.40.206) (Km = 400 to 900 microM). (pku.edu.cn)