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Pesquisa : D08.811.913.400.725.130 [Categoria DeCS]
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[PMID]:26140362
[Au] Autor:Goswami MT; Chen G; Chakravarthi BV; Pathi SS; Anand SK; Carskadon SL; Giordano TJ; Chinnaiyan AM; Thomas DG; Palanisamy N; Beer DG; Varambally S
[Ad] Endereço:Michigan Center for Translational Pathology, Ann Arbor, MI 48109, USA.
[Ti] Título:Role and regulation of coordinately expressed de novo purine biosynthetic enzymes PPAT and PAICS in lung cancer.
[So] Source:Oncotarget;6(27):23445-61, 2015 Sep 15.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cancer cells exhibit altered metabolism including aerobic glycolysis that channels several glycolytic intermediates into de novo purine biosynthetic pathway. We discovered increased expression of phosphoribosyl amidotransferase (PPAT) and phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) enzymes of de novo purine biosynthetic pathway in lung adenocarcinomas. Transcript analyses from next-generation RNA sequencing and gene expression profiling studies suggested that PPAT and PAICS can serve as prognostic biomarkers for aggressive lung adenocarcinoma. Immunohistochemical analysis of PAICS performed on tissue microarrays showed increased expression with disease progression and was significantly associated with poor prognosis. Through gene knockdown and over-expression studies we demonstrate that altering PPAT and PAICS expression modulates pyruvate kinase activity, cell proliferation and invasion. Furthermore we identified genomic amplification and aneuploidy of the divergently transcribed PPAT-PAICS genomic region in a subset of lung cancers. We also present evidence for regulation of both PPAT and PAICS and pyruvate kinase activity by L-glutamine, a co-substrate for PPAT. A glutamine antagonist, 6-Diazo-5-oxo-L-norleucine (DON) blocked glutamine mediated induction of PPAT and PAICS as well as reduced pyruvate kinase activity. In summary, this study reveals the regulatory mechanisms by which purine biosynthetic pathway enzymes PPAT and PAICS, and pyruvate kinase activity is increased and exposes an existing metabolic vulnerability in lung cancer cells that can be explored for pharmacological intervention.
[Mh] Termos MeSH primário: Adenocarcinoma/metabolismo
Amidofosforribosiltransferase/metabolismo
Carboxiliases/metabolismo
Neoplasias Pulmonares/metabolismo
Peptídeo Sintases/metabolismo
[Mh] Termos MeSH secundário: Idoso
Aneuploidia
Animais
Biomarcadores Tumorais/metabolismo
Linhagem Celular Tumoral
Proliferação Celular
Galinhas
Diazo-Oxo-Norleucina/química
Feminino
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Glutamina/química
Glutamina/metabolismo
Seres Humanos
Masculino
Camundongos
Meia-Idade
Invasividade Neoplásica
Transplante de Neoplasias
Análise de Sequência com Séries de Oligonucleotídeos
Prognóstico
Purinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Purines); 03J0H273KZ (Diazooxonorleucine); 0RH81L854J (Glutamine); EC 2.4.2.14 (Amidophosphoribosyltransferase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.21 (phosphoribosylaminoimidazole carboxylase); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.6 (phosphoribosylaminoimidazole-succinocarboxamide synthetase); W60KTZ3IZY (purine)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150704
[St] Status:MEDLINE


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[PMID]:26070680
[Au] Autor:Pisithkul T; Jacobson TB; O'Brien TJ; Stevenson DM; Amador-Noguez D
[Ad] Endereço:Graduate Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, Wisconsin, USA Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, USA Great Lake Bioenergy Research Center, University of Wisconsin-Madison, Madison, Wisconsin, USA.
[Ti] Título:Phenolic Amides Are Potent Inhibitors of De Novo Nucleotide Biosynthesis.
[So] Source:Appl Environ Microbiol;81(17):5761-72, 2015 Sep 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An outstanding challenge toward efficient production of biofuels and value-added chemicals from plant biomass is the impact that lignocellulose-derived inhibitors have on microbial fermentations. Elucidating the mechanisms that underlie their toxicity is critical for developing strategies to overcome them. Here, using Escherichia coli as a model system, we investigated the metabolic effects and toxicity mechanisms of feruloyl amide and coumaroyl amide, the predominant phenolic compounds in ammonia-pretreated biomass hydrolysates. Using metabolomics, isotope tracers, and biochemical assays, we showed that these two phenolic amides act as potent and fast-acting inhibitors of purine and pyrimidine biosynthetic pathways. Feruloyl or coumaroyl amide exposure leads to (i) a rapid buildup of 5-phosphoribosyl-1-pyrophosphate (PRPP), a key precursor in nucleotide biosynthesis, (ii) a rapid decrease in the levels of pyrimidine biosynthetic intermediates, and (iii) a long-term generalized decrease in nucleotide and deoxynucleotide levels. Tracer experiments using (13)C-labeled sugars and [(15)N]ammonia demonstrated that carbon and nitrogen fluxes into nucleotides and deoxynucleotides are inhibited by these phenolic amides. We found that these effects are mediated via direct inhibition of glutamine amidotransferases that participate in nucleotide biosynthetic pathways. In particular, feruloyl amide is a competitive inhibitor of glutamine PRPP amidotransferase (PurF), which catalyzes the first committed step in de novo purine biosynthesis. Finally, external nucleoside supplementation prevents phenolic amide-mediated growth inhibition by allowing nucleotide biosynthesis via salvage pathways. The results presented here will help in the development of strategies to overcome toxicity of phenolic compounds and facilitate engineering of more efficient microbial producers of biofuels and chemicals.
[Mh] Termos MeSH primário: Amidas/farmacologia
Inibidores Enzimáticos/farmacologia
Escherichia coli/metabolismo
Fenol/farmacologia
Purinas/biossíntese
Pirimidinas/biossíntese
[Mh] Termos MeSH secundário: Amidofosforribosiltransferase/antagonistas & inibidores
Amidofosforribosiltransferase/genética
Amidofosforribosiltransferase/metabolismo
Vias Biossintéticas/efeitos dos fármacos
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Escherichia coli/genética
Proteínas de Escherichia coli/antagonistas & inibidores
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Amides); 0 (Enzyme Inhibitors); 0 (Escherichia coli Proteins); 0 (Purines); 0 (Pyrimidines); 339NCG44TV (Phenol); EC 2.4.2.14 (Amidophosphoribosyltransferase); K8CXK5Q32L (pyrimidine); W60KTZ3IZY (purine)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150614
[St] Status:MEDLINE
[do] DOI:10.1128/AEM.01324-15


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[PMID]:25023436
[Au] Autor:Shi T; Wang Y; Wang Z; Wang G; Liu D; Fu J; Chen T; Zhao X
[Ti] Título:Deregulation of purine pathway in Bacillus subtilis and its use in riboflavin biosynthesis.
[So] Source:Microb Cell Fact;13:101, 2014 Jul 15.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Purine nucleotides are essential metabolites for living organisms because they are involved in many important processes, such as nucleic acid synthesis, energy supply, and biosynthesis of several amino acids and riboflavin. Owing to the pivotal roles of purines in cell physiology, the pool of intracellular purine nucleotides must be maintained under strict control, and hence the de novo purine biosynthetic pathway is tightly regulated by transcription repression and inhibition mechanism. Deregulation of purine pathway is essential for this pathway engineering in Bacillus subtilis. RESULTS: Deregulation of purine pathway was attempted to improve purine nucleotides supply, based on a riboflavin producer B. subtilis strain with modification of its rib operon. To eliminate transcription repression, the pur operon repressor PurR and the 5'-UTR of pur operon containing a guanine-sensing riboswitch were disrupted. Quantitative RT-PCR analysis revealed that the relative transcription levels of purine genes were up-regulated about 380 times. Furthermore, site-directed mutagenesis was successfully introduced into PRPP amidotransferase (encoded by purF) to remove feedback inhibition by homologous alignment and analysis. Overexpression of the novel mutant PurF (D293V, K316Q and S400W) significantly increased PRPP amidotransferase activity and triggered a strong refractory effect on purine nucleotides mediated inhibition. Intracellular metabolite target analysis indicated that the purine nucleotides supply in engineered strains was facilitated by a stepwise gene-targeted deregulation. With these genetic manipulations, we managed to enhance the metabolic flow through purine pathway and consequently increased riboflavin production 3-fold (826.52 mg/L) in the purF-VQW mutant strain. CONCLUSIONS: A sequential optimization strategy was applied to deregulate the rib operon and purine pathway of B. subtilis to create genetic diversities and to improve riboflavin production. Based on the deregulation of purine pathway at transcription and metabolic levels, an extended application is recommended for the yield of products, like inosine, guanosine, adenosine and folate which are directly stemming from purine pathway in B. subtilis.
[Mh] Termos MeSH primário: Bacillus subtilis/metabolismo
Vias Biossintéticas
Purinas/metabolismo
Riboflavina/biossíntese
[Mh] Termos MeSH secundário: Amidofosforribosiltransferase/metabolismo
Sequência de Aminoácidos
Bacillus subtilis/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Retroalimentação Fisiológica
Regulação Bacteriana da Expressão Gênica
Dados de Sequência Molecular
Mutação/genética
Nucleotídeos/metabolismo
Óperon/genética
Purinas/química
Riboflavina/química
Alinhamento de Sequência
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Nucleotides); 0 (Purines); EC 2.4.2.14 (Amidophosphoribosyltransferase); TLM2976OFR (Riboflavin); W60KTZ3IZY (purine)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:150805
[Lr] Data última revisão:
150805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140716
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-014-0101-8


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[PMID]:23483322
[Au] Autor:Batool S; Nawaz MS; Kamal MA
[Ad] Endereço:Functional Informatics Laboratory National Center for Bioinformatics, Quaid-I-Azam University, Islamabad, Pakistan.
[Ti] Título:In silico analysis of the amido phosphoribosyltransferase inhibition by PY873, PY899 and a derivative of isophthalic acid.
[So] Source:Invest New Drugs;31(5):1355-63, 2013 Oct.
[Is] ISSN:1573-0646
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Selectively decreasing the availability of precursors for the de novo biosynthesis of purine nucleotides is a valid approach towards seeking a cure for leukaemia. Nucleotides and deoxynucleotides are required by living cells for syntheses of RNA, DNA, and cofactors such as NADP(+), FAD(+), coenzyme A and ATP. Nucleotides contain purine and pyrimidine bases, which can be synthesized through salvage pathway as well. Amido phosphoribosyltransferase (APRT), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme that in humans is encoded by the PPAT (phosphoribosyl pyrophosphate amidotransferase) gene. APRT catalyzes the first committed step of the de novo pathway using its substrate, phosphoribosyl pyrophosphate (PRPP). As APRT is inhibited by many folate analogues, therefore, in this study we focused on the inhibitory effects of three folate analogues on APRT activity. This is extension of our previous wet lab work to analyze and dissect molecular interaction and inhibition mechanism using molecular modeling and docking tools in the current study. Comparative molecular docking studies were carried out for three diamino folate derivatives employing a model of the human enzyme that was built using the 3D structure of Bacillus subtilis APRT (PDB ID; 1GPH) as the template. Binding orientation of interactome indicates that all compounds having nominal cluster RMSD in same active site's deep narrow polar fissure. On the basis of comparative conformational analysis, electrostatic interaction, binding free energy and binding orientation of interactome, we support the possibility that these molecules could behave as APRT inhibitors and therefore may block purine de novo biosynthesis. Consequently, we suggest that PY899 is the most active biological compound that would be a more potent inhibitor for APRT inhibition than PY873 and DIA, which also confirms previous wet lab report.
[Mh] Termos MeSH primário: Amidofosforribosiltransferase/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Antagonistas do Ácido Fólico/farmacologia
Ácidos Ftálicos/farmacologia
Piridinas/farmacologia
Pirimidinas/farmacologia
Quinazolinas/farmacologia
[Mh] Termos MeSH secundário: Amidofosforribosiltransferase/química
Sequência de Aminoácidos
Bacillus subtilis/enzimologia
Sítios de Ligação
Simulação por Computador
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2,4-diamino-6-(3,4,5-trimethoxyanilino)methylpyrido(3,2-d)pyrimidine); 0 (2,4-diamino-6-(3,4,5-trimethoxybenzyl)-5,6,7,8-tetrahydroquinazoline); 0 (Enzyme Inhibitors); 0 (Folic Acid Antagonists); 0 (Phthalic Acids); 0 (Pyridines); 0 (Pyrimidines); 0 (Quinazolines); EC 2.4.2.14 (Amidophosphoribosyltransferase)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130314
[St] Status:MEDLINE
[do] DOI:10.1007/s10637-013-9944-9


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[PMID]:23357222
[Au] Autor:Merzetti E; Hackett JM; Clark DV
[Ad] Endereço:Department of Biology, University of New Brunswick, P.O. Box 4400, Fredericton, NB, Canada E3B 5A3. e.merzetti@mun.ca
[Ti] Título:Transcriptional regulation of the purine de novo synthesis gene Prat in Drosophila melanogaster.
[So] Source:Gene;518(2):280-6, 2013 Apr 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The first step of the purine de novo synthesis pathway is catalyzed by amidophosphoribosyltransferase (E.C.2.4.2.14) which is encoded by two Prat genes in D. melanogaster, Prat and Prat2. Prat is a retrogene duplication of Prat2, where each gene has a distinct expression pattern. Prat transcription is restricted to proliferating tissues such as imaginal discs and the female germ line. Three conserved putative DNA replication-related element binding factor (DREF) sites lie upstream of the Prat coding region. These elements are upstream of many genes important in cell proliferation. We have found that DREF binds directly upstream of Prat and that the DRE sites associated with its activity are necessary for Prat expression; furthermore, we have determined that a second cis-acting element is present upstream of the Prat gene. Finally, the genes Distal-less, Mi-2 and dMyc, which influence Dref activity, do not appear to affect Prat transcription.
[Mh] Termos MeSH primário: Amidofosforribosiltransferase/genética
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Drosophila melanogaster/metabolismo
Regulação da Expressão Gênica
Fatores de Transcrição/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Amidofosforribosiltransferase/metabolismo
Animais
Autoantígenos/genética
Sequência de Bases
Proteínas de Ligação a DNA/genética
Proteínas de Drosophila/metabolismo
Feminino
Proteínas de Homeodomínio/genética
Discos Imaginais/metabolismo
Purinas/biossíntese
Alinhamento de Sequência
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantigens); 0 (DNA-Binding Proteins); 0 (Dref protein, Drosophila); 0 (Drosophila Proteins); 0 (Homeodomain Proteins); 0 (Mi-2 protein, Drosophila); 0 (Purines); 0 (Transcription Factors); 0 (diminutive protein, Drosophila); 0 (distal-less protein, insect); EC 2.4.2.14 (Amidophosphoribosyltransferase); EC 2.4.2.14 (PRAT protein, Drosophila); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:130304
[Lr] Data última revisão:
130304
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130130
[St] Status:MEDLINE


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[PMID]:23133571
[Au] Autor:Koenigsknecht MJ; Lambrecht JA; Fenlon LA; Downs DM
[Ad] Endereço:Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
[Ti] Título:Perturbations in histidine biosynthesis uncover robustness in the metabolic network of Salmonella enterica.
[So] Source:PLoS One;7(10):e48207, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphoribosylamine (PRA) is an intermediate in the biosynthetic pathway that is common to thiamine and purines. Glutamine phosphoribosyl pyrophosphate (PRPP) amidotransferase is the product of the purF gene in Salmonella enterica and catalyzes the synthesis of PRA from PRPP and glutamine. Strains lacking PurF require exogenous addition of purines for growth. However, under some growth conditions or with specific secondary mutations these strains grow in the absence of exogenous thiamine. Mutant alleles of hisA, which encodes 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino) methylideneamino] imidazole-4-carboxamide (ProFAR) isomerase, allowed PurF-independent PRA formation. The alleles of hisA that suppressed the requirement for exogenous thiamine resulted in proteins with reduced enzymatic activity. Data presented here showed that decreased activity of HisA altered metabolite pools and allowed PRA formation from ProFAR. Possible mechanisms of this conversion were proposed. The results herein emphasize the plasticity of the metabolic network and specifically highlight the potential for chemical syntheses to contribute to network robustness.
[Mh] Termos MeSH primário: Amidofosforribosiltransferase/genética
Histidina/metabolismo
Salmonella enterica/metabolismo
[Mh] Termos MeSH secundário: Alelos
Amidofosforribosiltransferase/metabolismo
Cromatografia Líquida de Alta Pressão/métodos
DNA/metabolismo
Histidina/química
Redes e Vias Metabólicas/fisiologia
Modelos Químicos
Modelos Genéticos
Mutação
Óperon
Purinas/metabolismo
Tiamina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Purines); 4QD397987E (Histidine); 9007-49-2 (DNA); EC 2.4.2.14 (Amidophosphoribosyltransferase); X66NSO3N35 (Thiamine)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:161116
[Lr] Data última revisão:
161116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121108
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0048207


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[PMID]:22934352
[Au] Autor:He K; Ma Y; Du S; Xie X; Xu Q; Chen N
[Ad] Endereço:College of Biotechnology, Tianjin University of Science and Technology, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin 300457, China. hkfgwww@sina.com
[Ti] Título:[Effects of overexpression of key enzyme genes on guanosine accumulation in Bacillus amyloliquefaciens].
[So] Source:Wei Sheng Wu Xue Bao;52(6):718-25, 2012 Jun 04.
[Is] ISSN:0001-6209
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To study the effects of overexpression of key enzyme genes (prs, purF and guaB) on guanosine production in Bacillus amyloliquefaciens TA208. METHODS: The prs, purF, guaB and prs-purF genes were inserted into constructed expression plasmid PBE43. All these constructed plasmids were electroporated into B. amyloliquefaciens TA208. The transcriptional level of various genes in the resulting strains was tested by real-time quantitative PCR. The activity of inosine 5'-monophosphate dehydrogenase in the resulting strains was detected. Finally, cell growth, glucose consumption and guanosine production of 4 engineering strains along with control strain were examined. RESULTS: The transcriptional analysis showed that overexpression of prs, purF and guaB gene accompanied by their own transcription level up-regulated. Overexpression of prs or purF genes alone slightly down-regulated the transcriptional level of purine operon, but overexpression of guaB gene independently did not disturb the transcription of prs gene and purine operon. Enzyme activity analysis showed that overexpression of prs or purF gene did not change the activity of inosine 5'-monophosphate dehydrogenase and its activity increased by 126% through overexpression of guaB gene. Finally, by fermentation flask test, we found that overexpression of prs and purF gene alone could not promote guanosine accumulation. However, overexpression of guaB gene resulted in an increase in the production of guanosine, which was 20.7% higher than the control strain. The guanosine concentration and the conversion ratio from glucose to guanosine in the host strain containing co-expression plasmid were 14.4% and 6.8% higher than the control strain. CONCLUSION: Overexpression of guaB gene could enhance the guanosine yield in the culture broth. However, for prs and purF gene, only co-expression of them could lead to a significant improvement of guanosine production in B. amyloliquefaciens. It should provide a valuable insight into the construction of industrially important strains for guanosine production by metabolic engineering.
[Mh] Termos MeSH primário: Amidofosforribosiltransferase/biossíntese
Bacillus/enzimologia
Bacillus/genética
Guanosina/metabolismo
IMP Desidrogenase/biossíntese
Ribose-Fosfato Pirofosfoquinase/biossíntese
[Mh] Termos MeSH secundário: Amidofosforribosiltransferase/genética
Amidofosforribosiltransferase/metabolismo
Bacillus/metabolismo
Genes Bacterianos
IMP Desidrogenase/genética
IMP Desidrogenase/metabolismo
Engenharia Metabólica
Plasmídeos/genética
Ribose-Fosfato Pirofosfoquinase/genética
Ribose-Fosfato Pirofosfoquinase/metabolismo
Transfecção
Regulação para Cima
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
12133JR80S (Guanosine); EC 1.1.1.205 (IMP Dehydrogenase); EC 2.4.2.14 (Amidophosphoribosyltransferase); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120901
[St] Status:MEDLINE


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[PMID]:22532604
[Au] Autor:Rosar C; Kanonenberg K; Nanda AM; Mielewczik M; Bräutigam A; Novák O; Strnad M; Walter A; Weber AP
[Ad] Endereço:Institute for Plant Biochemistry, Heinrich-Heine-Universität, Universitätsstrasse 1, D-40225 Düsseldorf, Germany.
[Ti] Título:The leaf reticulate mutant dov1 is impaired in the first step of purine metabolism.
[So] Source:Mol Plant;5(6):1227-41, 2012 Nov.
[Is] ISSN:1752-9867
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A series of reticulated Arabidopsis thaliana mutants were previously described. All mutants show a reticulate leaf pattern, namely green veins on a pale leaf lamina. They have an aberrant mesophyll structure but an intact layer of bundle sheath cells around the veins. Here, we unravel the function of the previously described reticulated EMS-mutant dov1 (differential development of vascular associated cells 1). By positional cloning, we identified the mutated gene, which encodes glutamine phosphoribosyl pyrophosphate aminotransferase 2 (ATase2), an enzyme catalyzing the first step of purine nucleotide biosynthesis. dov1 is allelic to the previously characterized cia1-2 mutant that was isolated in a screen for mutants with impaired chloroplast protein import. We show that purine-derived total cytokinins are lowered in dov1 and crosses with phytohormone reporter lines revealed differential reporter activity patterns in dov1. Metabolite profiling unraveled that amino acids that are involved in purine biosynthesis are increased in dov1. This study identified the molecular basis of an established mutant line, which has the potential for further investigation of the interaction between metabolism and leaf development.
[Mh] Termos MeSH primário: Amidofosforribosiltransferase/genética
Amidofosforribosiltransferase/metabolismo
Arabidopsis/enzimologia
Arabidopsis/genética
Mutação
Folhas de Planta/genética
Purinas/metabolismo
[Mh] Termos MeSH secundário: Alelos
Arabidopsis/citologia
Arabidopsis/metabolismo
Sequência de Bases
Diferenciação Celular
Clonagem Molecular
Citocininas/metabolismo
Células do Mesofilo/citologia
Células do Mesofilo/metabolismo
Fotossíntese
Reguladores de Crescimento de Planta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytokinins); 0 (Plant Growth Regulators); 0 (Purines); EC 2.4.2.14 (Amidophosphoribosyltransferase)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:121127
[Lr] Data última revisão:
121127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120426
[St] Status:MEDLINE
[do] DOI:10.1093/mp/sss045


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[PMID]:22132968
[Au] Autor:Shinohara Y; Suzuki Y; Hasegawa H; Nakamura M; Nishiyama T; Hiratsuka A; Ichida K
[Ad] Endereço:Department of Pathophysiology, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan. sinohara@toyaku.ac.jp
[Ti] Título:Stable isotope dilution mass spectrometric assay for PRPP using enzymatic procedures.
[So] Source:Nucleosides Nucleotides Nucleic Acids;30(12):1140-6, 2011 Dec.
[Is] ISSN:1532-2335
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:5-Phosphoribosyl-1-pyrophosphate (PRPP) is an important regulator of de novo purine synthesis. A method for the measurement of PRPP in erythrocytes was designed, which is based on the determination of [(13)C(5)]glutamate derived from [(13)C(5)]glutamine following the utilization of PRPP by the action of amidophosphoribosyltransferase. The present study describes a gas chromatographic-mass spectrometric method for determination of [(13)C(5)]glutamate using [(13)C(2)]glutamate as an internal standard. The methods involved purification by anion-exchange chromatography using a BondElut SAX and derivatization with isobutyl chlorocarbonate in water-methanol-pyridine. Quantitation was performed by selected ion monitoring of the protonated molecular ions in the chemical ionization mode. The intra-day reproducibility in the amounts of [(13)C(5)]glutamate determined was in good agreement with the actual amounts added in erythrocytes. A linear relationship was found between the amount of PRPP added and the amount of [(13)C(5)]glutamate formed from [(13)C(5)]glutamine using amidophosphoribosyltransferase.
[Mh] Termos MeSH primário: Amidofosforribosiltransferase/metabolismo
Marcação por Isótopo/métodos
Espectrometria de Massas/métodos
Fosforribosil Pirofosfato/análise
[Mh] Termos MeSH secundário: Isótopos de Carbono
Glutamina/metabolismo
Seres Humanos
Técnicas de Diluição do Indicador
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbon Isotopes); 0RH81L854J (Glutamine); 7540-64-9 (Phosphoribosyl Pyrophosphate); EC 2.4.2.14 (Amidophosphoribosyltransferase)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111203
[St] Status:MEDLINE
[do] DOI:10.1080/15257770.2011.591746


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[PMID]:21763446
[Au] Autor:Qin L; Gong X; Xie J; Jiang D; Cheng J; Li G; Huang J; Fu Y
[Ad] Endereço:State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, Hubei Province, China.
[Ti] Título:Phosphoribosylamidotransferase, the first enzyme for purine de novo synthesis, is required for conidiation in the sclerotial mycoparasite Coniothyrium minitans.
[So] Source:Fungal Genet Biol;48(10):956-65, 2011 Oct.
[Is] ISSN:1096-0937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coniothyrium minitans is an important sclerotial parasite of the fungal phytopathogen, Sclerotinia sclerotiorum. Previously, we constructed a T-DNA insertional library, and screened for many conidiation-deficient mutants from this library. Here, we report a T-DNA insertional mutant ZS-1T21882 that completely lost conidiation. In mutant ZS-1T21882, the T-DNA was integrated into a gene (CmPrat-1) which encodes phosphoribosylamidotransferase (PRAT, EC 2.4.2.14), an enzyme catalyzing the first committed step in de novo purine nucleotide synthesis. Gene replacement and complementation experiments confirmed that phosphoribosylamidotransferase is essential for conidiation of C. minitans. Mutant ZS-1T21882 did not grow on modified Czapek-Dox broth (MCD), but it grew well on MCD amended with IMP or AMP. The conidial production of this mutant was dependent on the dosage of IMP amended. At low concentrations, such as 0.1 mM and 0.25 mM, the mutant produced very few pycnidia, while up to 0.75 mM or higher, the conidiation of this mutant was restored completely. cAMP could not restore the conidiation of mutant ZS-1T21882 when amended into MCD, but could when amended into PDA. Neither GMP nor cGMP could restore the conidiation in MCD or in PDA. Our findings suggest that phosphoribosylamidotransferase is essential for conidiation of C. minitans via adenosine related molecules. Furthermore, when dual cultured with its host, this mutant produced conidia in the host mycelium and on the sclerotia of S. sclerotiorum, but not in dead mycelium or on dead sclerotia, suggesting that C. minitans is likely to able to obtain adenosine or related components from its host during parasitization.
[Mh] Termos MeSH primário: Adenosina/biossíntese
Amidofosforribosiltransferase/metabolismo
Ascomicetos/enzimologia
Esporos Fúngicos/enzimologia
[Mh] Termos MeSH secundário: Amidofosforribosiltransferase/biossíntese
Sequência de Aminoácidos
Ascomicetos/fisiologia
AMP Cíclico/genética
AMP Cíclico/metabolismo
DNA Bacteriano/genética
Dados de Sequência Molecular
Mutação/genética
Mutação/fisiologia
Micélio/enzimologia
Transdução de Sinais
Esporos Fúngicos/genética
Esporos Fúngicos/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (T-DNA); E0399OZS9N (Cyclic AMP); EC 2.4.2.14 (Amidophosphoribosyltransferase); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1112
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110719
[St] Status:MEDLINE
[do] DOI:10.1016/j.fgb.2011.06.007



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