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[PMID]:28114831
[Au] Autor:Zavala A; Kovacec V; Levín G; Moglioni A; Miranda MV; García E; Bonofiglio L; Mollerach M
[Ad] Endereço:a Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Departamento de Microbiología , Inmunología y Biotecnología, Cátedra de Microbiología , Buenos Aires , Argentina.
[Ti] Título:Screening assay for inhibitors of a recombinant Streptococcus pneumoniae UDP-glucose pyrophosphorylase.
[So] Source:J Enzyme Inhib Med Chem;32(1):203-207, 2017 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The UDP-glucose pyrophosphorylase of Streptococcus pneumoniae (GalU ) is absolutely required for the biosynthesis of capsular polysaccharide, the sine qua non virulence factor of pneumococcus. Since the eukaryotic enzymes are completely unrelated to their prokaryotic counterparts, we propose that the GalU enzyme is a critical target to fight the pneumococcal disease. A recombinant GalU was overexpressed and purified. An enzymatic assay that is rapid, sensitive and easy to perform was developed. This assay was appropriate for screening chemical libraries for searching GalU inhibitors. This work represents a fundamental step in the exploration of novel antipneumococcal drugs.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Avaliação Pré-Clínica de Medicamentos/métodos
Inibidores Enzimáticos/farmacologia
Streptococcus pneumoniae/efeitos dos fármacos
Streptococcus pneumoniae/enzimologia
UTP-Glucose-1-Fosfato Uridililtransferase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Antibacterianos/síntese química
Antibacterianos/química
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Testes de Sensibilidade Microbiana
Estrutura Molecular
Proteínas Recombinantes/metabolismo
Relação Estrutura-Atividade
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Enzyme Inhibitors); 0 (Recombinant Proteins); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170223
[Lr] Data última revisão:
170223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170125
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2016.1247055


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Alves, José Donizeti
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[PMID]:27979176
[Au] Autor:Livramento KGD; Borém FM; José AC; Santos AV; Livramento DED; Alves JD; Paiva LV
[Ad] Endereço:Federal University of Lavras, CEP 37200-000 Lavras, MG, Brazil. Electronic address: kalynkagabriella@yahoo.com.br.
[Ti] Título:Proteomic analysis of coffee grains exposed to different drying process.
[So] Source:Food Chem;221:1874-1882, 2017 Apr 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many biochemical events occur inside grains during post-harvest processes. Several methods have been developed to relate the chemical composition of the coffee grain to the beverage quality, including identification of possible molecular markers for flavor characterizing. This study was aimed at evaluating the changes in the proteomic profile of pulped and natural C. arabica grains dried in a yard or dryer at 60°C. It was observed that fruits dried in a dryer at 60°C showed an altered proteomic profile, with a reduction in the most abundant proteins compared to those yard-dried grains. Among the identified proteins, those involved in the metabolism of sugars and stress response were highlighted. Results have shown that post-harvest processes that impact coffee quality are related to changes in protein abundance, indicating that proteomic analysis may be effective in the identification of biochemical changes in coffee grains subjected to different post-harvest processes.
[Mh] Termos MeSH primário: Coffea/química
Café/química
Dessecação
Manipulação de Alimentos
Proteômica
[Mh] Termos MeSH secundário: beta-Globulinas/análise
Gliceraldeído-3-Fosfato Desidrogenases/análise
Proteínas de Choque Térmico/análise
Proteínas de Plantas/análise
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Espectrometria de Massas em Tandem
UTP-Glucose-1-Fosfato Uridililtransferase/análise
alfa-Galactosidase/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Coffee); 0 (Heat-Shock Proteins); 0 (Plant Proteins); EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 3.2.1.22 (alpha-Galactosidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


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[PMID]:27630054
[Au] Autor:Jónás Á; Fekete E; Németh Z; Flipphi M; Karaffa L
[Ad] Endereço:Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen , H-4032, P.O. Box 64, Debrecen , Hungary.
[Ti] Título:D-galactose catabolism in Penicillium chrysogenum: Expression analysis of the structural genes of the Leloir pathway.
[So] Source:Acta Biol Hung;67(3):318-32, 2016 Sep.
[Is] ISSN:0236-5383
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:In this study, we analyzed the expression of the structural genes encoding the five enzymes comprising the Leloir pathway of D-galactose catabolism in the industrial cell factory Penicillium chrysogenum on various carbon sources. The genome of P. chrysogenum contains a putative galactokinase gene at the annotated locus Pc13g10140, the product of which shows strong structural similarity to yeast galactokinase that was expressed on lactose and D-galactose only. The expression profile of the galactose-1-phosphate uridylyl transferase gene at annotated locus Pc15g00140 was essentially similar to that of galactokinase. This is in contrast to the results from other fungi such as Aspergillus nidulans, Trichoderma reesei and A. niger, where the ortholog galactokinase and galactose-1-phosphate uridylyl transferase genes were constitutively expressed. As for the UDP-galactose-4-epimerase encoding gene, five candidates were identified. We could not detect Pc16g12790, Pc21g12170 and Pc20g06140 expression on any of the carbon sources tested, while for the other two loci (Pc21g10370 and Pc18g01080) transcripts were clearly observed under all tested conditions. Like the 4-epimerase specified at locus Pc21g10370, the other two structural Leloir pathway genes - UDP-glucose pyrophosphorylase (Pc21g12790) and phosphoglucomutase (Pc18g01390) - were expressed constitutively at high levels as can be expected from their indispensable function in fungal cell wall formation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Enzimas/metabolismo
Galactose/metabolismo
Penicillium chrysogenum/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Enzimas/genética
Fermentação
Galactoquinase/genética
Galactoquinase/metabolismo
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Nucleotidiltransferases/genética
Nucleotidiltransferases/metabolismo
Penicillium chrysogenum/genética
Penicillium chrysogenum/crescimento & desenvolvimento
Fosfoglucomutase/genética
Fosfoglucomutase/metabolismo
Especificidade por Substrato
Fatores de Tempo
UDPglucose 4-Epimerase/genética
UDPglucose 4-Epimerase/metabolismo
UTP-Glucose-1-Fosfato Uridililtransferase/genética
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzymes); EC 2.7.1.6 (Galactokinase); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 5.1.3.2 (UDPglucose 4-Epimerase); EC 5.4.2.2 (Phosphoglucomutase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE
[do] DOI:10.1556/018.67.2016.3.9


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[PMID]:27389087
[Au] Autor:Wang Q; Yang ZL; Zou Q; Yuan Y; Li J; Liang L; Zeng G; Chen S
[Ad] Endereço:a Minimally Invasive Surgery Center , Central South University , Changsha , China.
[Ti] Título:SHP2 and UGP2 are Biomarkers for Progression and Poor Prognosis of Gallbladder Cancer.
[So] Source:Cancer Invest;34(6):255-64, 2016 Jul 02.
[Is] ISSN:1532-4192
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Biomarkers for the diagnosis, prognosis, and targeting therapy of gallbladder cancers are not clinically available. This study demonstrated that the percentage of cases with positive SHP2 and UGP2 expression significantly correlated with the percentage of cases with positive vimentin, ß-catenin, MMP2, MMP9, and Ki-67 expression, large tumor size, high TNM stage, lymph node metastasis, and survival in patients with adenocarcinomas and squamous cell/adenosquamous carcinomas. Positive SHP2 and UGP2 expression are independent poor-prognostic factors in both types of tumors. Our study suggested that positive SHP2 and UGP2 expression correlated with clinicopathological and biological behaviors, and poor-prognosis of gallbladder cancer.
[Mh] Termos MeSH primário: Biomarcadores Tumorais
Neoplasias da Vesícula Biliar/diagnóstico
Neoplasias da Vesícula Biliar/metabolismo
Proteína Tirosina Fosfatase não Receptora Tipo 11/metabolismo
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Progressão da Doença
Feminino
Neoplasias da Vesícula Biliar/mortalidade
Neoplasias da Vesícula Biliar/terapia
Seres Humanos
Imuno-Histoquímica
Estimativa de Kaplan-Meier
Masculino
Meia-Idade
Gradação de Tumores
Metástase Neoplásica
Estadiamento de Neoplasias
Prognóstico
Carga Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170206
[Lr] Data última revisão:
170206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.1080/07357907.2016.1193745


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[PMID]:26813656
[Au] Autor:Medeot DB; Romina Rivero M; Cendoya E; Contreras-Moreira B; Rossi FA; Fischer SE; Becker A; Jofré E
[Ad] Endereço:1Department of Natural Sciences, FCEFQyN, National University of Río Cuarto, Ruta Nacional 36 Km 601, Córdoba, Argentina 2Department of Molecular Biology, FCEFQyN, National University of Río Cuarto, Ruta Nacional 36 Km 601, Córdoba, Argentina.
[Ti] Título:Sinorhizobium meliloti low molecular mass phosphotyrosine phosphatase SMc02309 modifies activity of the UDP-glucose pyrophosphorylase ExoN involved in succinoglycan biosynthesis.
[So] Source:Microbiology;162(3):552-63, 2016 Mar.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In Gram-negative bacteria, tyrosine phosphorylation has been shown to play a role in the control of exopolysaccharide (EPS) production. This study demonstrated that the chromosomal ORF SMc02309 from Sinorhizobium meliloti 2011 encodes a protein with significant sequence similarity to low molecular mass protein-tyrosine phosphatases (LMW-PTPs), such as the Escherichia coli Wzb. Unlike other well-characterized EPS biosynthesis gene clusters, which contain neighbouring LMW-PTPs and kinase, the S. meliloti succinoglycan (EPS I) gene cluster located on megaplasmid pSymB does not encode a phosphatase. Biochemical assays revealed that the SMc02309 protein hydrolyses p-nitrophenyl phosphate (p-NPP) with kinetic parameters similar to other bacterial LMW-PTPs. Furthermore, we show evidence that SMc02309 is not the LMW-PTP of the bacterial tyrosine-kinase (BY-kinase) ExoP. Nevertheless, ExoN, a UDP-glucose pyrophosphorylase involved in the first stages of EPS I biosynthesis, is phosphorylated at tyrosine residues and constitutes an endogenous substrate of the SMc02309 protein. Additionally, we show that the UDP-glucose pyrophosphorylase activity is modulated by SMc02309-mediated tyrosine dephosphorylation. Moreover, a mutation in the SMc02309 gene decreases EPS I production and delays nodulation on Medicago sativa roots.
[Mh] Termos MeSH primário: Polissacarídeos Bacterianos/biossíntese
Proteínas Tirosina Fosfatases/metabolismo
Sinorhizobium meliloti/enzimologia
Sinorhizobium meliloti/metabolismo
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Mh] Termos MeSH secundário: Medicago sativa/microbiologia
Nodulação
Raízes de Plantas/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Polysaccharides, Bacterial); 73667-50-2 (succinoglycan); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 3.1.3.48 (Protein Tyrosine Phosphatases)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160128
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.000239


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[PMID]:26756813
[Au] Autor:Xi Y; Cheng D; Zeng X; Cao J; Jiang W
[Ad] Endereço:College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua Donglu, Beijing 100083, PR China.
[Ti] Título:Evidences for Chlorogenic Acid--A Major Endogenous Polyphenol Involved in Regulation of Ripening and Senescence of Apple Fruit.
[So] Source:PLoS One;11(1):e0146940, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To learn how the endogenous polyphenols may play a role in fruit ripening and senescence, apple pulp discs were used as a model to study the influences of chlorogenic acid (CHA, a major polyphenol in apple pulp) on fruit ripening and senescence. Apple ('Golden Delicious') pulp discs prepared from pre-climacteric fruit were treated with 50 mg L(-1) CHA and incubated in flasks with 10 mM MES buffer (pH 6.0, 11% sorbitol). Compared to the control samples, treatment with CHA significantly reduced ethylene production and respiration rate, and enhanced levels of firmness and soluble solids content of the pulp discs during incubation at 25°C. These results suggested that CHA could retard senescence of the apple pulp discs. Proteomics analysis with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry (MALDI-TOF/TOF) revealed that the expressions of several key proteins correlated to fruit ripening and senescence were affected by the treatment with CHA. Further study showed that treating the pulp discs with CHA remarkably reduced levels of lipoxygenase, ß-galactosidase, NADP-malic enzyme, and enzymatic activities of lipoxygenase and UDP-glucose pyrophosphorylase, all of which are known as promoters of fruit ripening and senescence. These results could provide new insights into the functions of endogenous phenolic compounds in fruit ripening and senescence.
[Mh] Termos MeSH primário: Ácido Clorogênico/química
Frutas/fisiologia
Malus/fisiologia
Polifenóis/química
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Etilenos/química
Lipoxigenase/metabolismo
Malato Desidrogenase/metabolismo
NADP/química
Fenol/química
Proteômica
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Temperatura Ambiente
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
Difosfato de Uridina/química
beta-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ethylenes); 0 (Polyphenols); 318ADP12RI (Chlorogenic Acid); 339NCG44TV (Phenol); 53-59-8 (NADP); 58-98-0 (Uridine Diphosphate); 91GW059KN7 (ethylene); EC 1.1.1.37 (Malate Dehydrogenase); EC 1.1.1.40 (malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)); EC 1.13.11.12 (Lipoxygenase); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0146940


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[PMID]:26613730
[Au] Autor:Li H; Zhang Y; Gao Y; Lan Y; Yin X; Huang L
[Ad] Endereço:College of Medicine, Hangzhou Normal University, No.1378 Wenyi Xi Road, Hangzhou, 311121, Zhejiang, People's Republic of China. lihaifengwater@163.com.
[Ti] Título:Characterization of UGPase from Aureobasidium pullulans NRRL Y-12974 and Application in Enhanced Pullulan Production.
[So] Source:Appl Biochem Biotechnol;178(6):1141-53, 2016 Mar.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UDPG pyrophosphatase (UGPase) plays an important role in carbohydrate metabolism, catalyzing a reversible production of uridine diphosphate glucose (UDPG) and pyrophosphate (PPi) from Glc-1-P and UTP. UGPase gene from Aureobasidium pullulans NRRL Y-12974 was cloned, overexpressed in Escherichia coli. The recombinant UGPase possess molecular mass of 55 KDa and specific activity of 7.33 U/mg protein. The K m values of rUGPase were 5.045 µM against UTP and 3.333 µM against Glc-1-P. The V max values of rUGPase were 3.467 µM min(-1)against UTP and 2.817 µM min(-1) against Glc-1-P. And, it does not catalyze Glc-1-P and ATP, nor galactose-1-P and UTP. Homolgous expression of UGPase in native organism can improve the intracellular UDPG concentration by 4.7-fold time. The yield of pullulan in engineering strain A4 was improved to 18.2 g g(-1) cell dry weight which is 1.3-fold time of parent strain. No obvious change of growth was found between engineering strain and parent strain. To the best of our knowledge, this is the first report of improving pullulan yield in A. pullulans using metabolic engineering technique.
[Mh] Termos MeSH primário: Ascomicetos/enzimologia
Glucanos/biossíntese
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Mh] Termos MeSH secundário: Eletroforese em Gel de Poliacrilamida
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glucans); 8ZQ0AYU1TT (pullulan); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151129
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-015-1934-2


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[PMID]:26162893
[Au] Autor:Zhu BH; Shi HP; Yang GP; Lv NN; Yang M; Pan KH
[Ad] Endereço:Key Laboratory of Mariculture, Ministry of Education, Ocean University of China, Qingdao 266003, China. Electronic address: zhubaohua@ouc.edu.cn.
[Ti] Título:Silencing UDP-glucose pyrophosphorylase gene in Phaeodactylum tricornutum affects carbon allocation.
[So] Source:N Biotechnol;33(1):237-44, 2016 Jan 25.
[Is] ISSN:1876-4347
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The effects of the suppression of UDP-glucose pyrophosphorylase (UGPase) on chrysolaminaran biosynthesis and carbon allocation were investigated in Phaeodactylum tricornutum. The 69% decrease in UGPase activity was accompanied by a 4.89 fold reduction in Ugp transcript abundance. Inactivation of UGPase in P. tricornutum led to a significant decrease in chrysolaminaran content and an increase in lipid synthesis. These findings suggest that UGPase is a rate-limiting enzyme and may play an important role in chrysolaminarin biosynthesis and carbon allocation. Our results support a theoretical deduction that Ugp is a good candidate for improving lipid synthesis in diatoms.
[Mh] Termos MeSH primário: Carbono/metabolismo
Diatomáceas/enzimologia
Inativação Gênica
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Diatomáceas/crescimento & desenvolvimento
Vetores Genéticos/metabolismo
Dados de Sequência Molecular
Reação em Cadeia da Polimerase
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Análise de Sequência de DNA
Transformação Genética
UTP-Glucose-1-Fosfato Uridililtransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); 7440-44-0 (Carbon); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151111
[Lr] Data última revisão:
151111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150712
[St] Status:MEDLINE


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[PMID]:26529232
[Au] Autor:Damerow S; Hoppe C; Bandini G; Zarnovican P; Buettner FF; Buettner FR; Lüder CG; Ferguson MA; Routier FH
[Ad] Endereço:Department of Cellular Chemistry, Hannover Medical School, Hannover, Germany.
[Ti] Título:Depletion of UDP-Glucose and UDP-Galactose Using a Degron System Leads to Growth Cessation of Leishmania major.
[So] Source:PLoS Negl Trop Dis;9(11):e0004205, 2015 Nov.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal) by the UDP-Glc 4´-epimerase intimately connects the biosynthesis of these two nucleotide sugars. Their de novo biosynthesis involves transformation of glucose-6-phosphate into glucose-1-phosphate by the phosphoglucomutase and subsequent activation into UDP-Glc by the specific UDP-Glc pyrophosphorylase (UGP). Besides UGP, Leishmania parasites express an uncommon UDP-sugar pyrophosphorylase (USP) able to activate both galactose-1-phosphate and glucose-1-phosphate in vitro. Targeted gene deletion of UGP alone was previously shown to principally affect expression of lipophosphoglycan, resulting in a reduced virulence. Since our attempts to delete both UGP and USP failed, deletion of UGP was combined with conditional destabilisation of USP to control the biosynthesis of UDP-Glc and UDP-Gal. Stabilisation of the enzyme produced by a single USP allele was sufficient to maintain the steady-state pools of these two nucleotide sugars and preserve almost normal glycoinositolphospholipids galactosylation, but at the apparent expense of lipophosphoglycan biosynthesis. However, under destabilising conditions, the absence of both UGP and USP resulted in depletion of UDP-Glc and UDP-Gal and led to growth cessation and cell death, suggesting that either or both of these metabolites is/are essential.
[Mh] Termos MeSH primário: Leishmania major/crescimento & desenvolvimento
Leishmania major/metabolismo
Uridina Difosfato Galactose/deficiência
Uridina Difosfato Glucose/deficiência
[Mh] Termos MeSH secundário: Deleção de Genes
Regulação da Expressão Gênica
UTP-Glucose-1-Fosfato Uridililtransferase/genética
UTP-Hexose-1-Fosfato Uridililtransferase/genética
Uridina Difosfato Galactose/metabolismo
Uridina Difosfato Glucose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
2956-16-3 (Uridine Diphosphate Galactose); EC 2.7.7.10 (UTP-Hexose-1-Phosphate Uridylyltransferase); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151104
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0004205


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[PMID]:26498530
[Au] Autor:Yi DG; Huh WK
[Ad] Endereço:Department of Biological Sciences, Seoul National University, Seoul 151-747, Republic of Korea.
[Ti] Título:UDP-glucose pyrophosphorylase Ugp1 is involved in oxidative stress response and long-term survival during stationary phase in Saccharomyces cerevisiae.
[So] Source:Biochem Biophys Res Commun;467(4):657-63, 2015 Nov 27.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ugp1, UDP-glucose pyrophosphorylase, plays an important role in carbohydrate metabolism because it provides UDP-glucose that is a pivotal metabolite in several metabolic pathways in Saccharomyces cerevisiae. In this study, we show that a considerable reduction of glycogen and trehalose content in ugp1 knockdown cells is rescued by complementing the expression of Ugp1, indicating that Ugp1 is required for the production of storage carbohydrates. Because of the specific function of trehalose as a stress protectant, Ugp1 expression contributed to oxidative stress response and long-term cell survival during stationary phase. Furthermore, the modulation of Ugp1 level readjusted glycogen and trehalose accumulation in the protein kinase A (PKA)-related gene mutants. The PKA-dependent phenotypes of oxidative stress resistance and long-term cell survival were also alleviated via adjustment of Ugp1 level. Collectively, our data suggest that the regulation of UPG1 influences several PKA-dependent processes by adjusting the levels of various carbohydrates.
[Mh] Termos MeSH primário: Estresse Oxidativo
Saccharomyces cerevisiae/enzimologia
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Mh] Termos MeSH secundário: Sobrevivência Celular
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Glicogênio/metabolismo
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/metabolismo
Trealose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9005-79-2 (Glycogen); B8WCK70T7I (Trehalose); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:151113
[Lr] Data última revisão:
151113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151027
[St] Status:MEDLINE



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