Base de dados : MEDLINE
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[PMID]:28537141
[Au] Autor:Taguchi Y; Saburi W; Imai R; Mori H
[Ad] Endereço:a Research Faculty of Agriculture , Hokkaido University , Sapporo , Japan.
[Ti] Título:Evaluation of acceptor selectivity of Lactococcus lactis ssp. lactis trehalose 6-phosphate phosphorylase in the reverse phosphorolysis and synthesis of a new sugar phosphate.
[So] Source:Biosci Biotechnol Biochem;81(8):1512-1519, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Trehalose 6-phosphate phosphorylase (TrePP), a member of glycoside hydrolase family 65, catalyzes the reversible phosphorolysis of trehalose 6-phosphate (Tre6P) with inversion of the anomeric configuration to produce ß-d-glucose 1-phosphate (ß-Glc1P) and d-glucose 6-phosphate (Glc6P). TrePP in Lactococcus lactis ssp. lactis (LlTrePP) is, alongside the phosphotransferase system, involved in the metabolism of trehalose. In this study, recombinant LlTrePP was produced and characterized. It showed its highest reverse phosphorolytic activity at pH 4.8 and 40°C, and was stable in the pH range 5.0-8.0 and at up to 30°C. Kinetic analyses indicated that reverse phosphorolysis of Tre6P proceeded through a sequential bi bi mechanism involving the formation of a ternary complex of the enzyme, ß-Glc1P, and Glc6P. Suitable acceptor substrates were Glc6P, and, at a low level, d-mannose 6-phosphate (Man6P). From ß-Glc1P and Man6P, a novel sugar phosphate, α-d-Glcp-(1↔1)-α-d-Manp6P, was synthesized with 51% yield.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Glucosiltransferases/metabolismo
Lactococcus lactis/enzimologia
Fosfatos Açúcares/biossíntese
Trealose/análogos & derivados
Trealose/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glucofosfatos/metabolismo
Glucosiltransferases/genética
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Lactococcus lactis/química
Manosefosfatos/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Fosfatos Açúcares/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Glucosephosphates); 0 (Mannosephosphates); 0 (Recombinant Proteins); 0 (Sugar Phosphates); 3672-15-9 (mannose-6-phosphate); 4484-88-2 (trehalose-6-phosphate); 54482-78-9 (2-deoxyglucose-1-phosphate); B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (trehalose-6-phosphate phosphorylase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170525
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1329620


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[PMID]:28403831
[Au] Autor:Bledsoe SW; Henry C; Griffiths CA; Paul MJ; Feil R; Lunn JE; Stitt M; Lagrimini LM
[Ad] Endereço:EAG Laboratories, 4780 Discovery Drive, Columbia, MO, 65201, USA.
[Ti] Título:The role of Tre6P and SnRK1 in maize early kernel development and events leading to stress-induced kernel abortion.
[So] Source:BMC Plant Biol;17(1):74, 2017 Apr 12.
[Is] ISSN:1471-2229
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Drought stress during flowering is a major contributor to yield loss in maize. Genetic and biotechnological improvement in yield sustainability requires an understanding of the mechanisms underpinning yield loss. Sucrose starvation has been proposed as the cause for kernel abortion; however, potential targets for genetic improvement have not been identified. Field and greenhouse drought studies with maize are expensive and it can be difficult to reproduce results; therefore, an in vitro kernel culture method is presented as a proxy for drought stress occurring at the time of flowering in maize (3 days after pollination). This method is used to focus on the effects of drought on kernel metabolism, and the role of trehalose 6-phosphate (Tre6P) and the sucrose non-fermenting-1-related kinase (SnRK1) as potential regulators of this response. RESULTS: A precipitous drop in Tre6P is observed during the first two hours after removing the kernels from the plant, and the resulting changes in transcript abundance are indicative of an activation of SnRK1, and an immediate shift from anabolism to catabolism. Once Tre6P levels are depleted to below 1 nmol∙g FW in the kernel, SnRK1 remained active throughout the 96 h experiment, regardless of the presence or absence of sucrose in the medium. Recovery on sucrose enriched medium results in the restoration of sucrose synthesis and glycolysis. Biosynthetic processes including the citric acid cycle and protein and starch synthesis are inhibited by excision, and do not recover even after the re-addition of sucrose. It is also observed that excision induces the transcription of the sugar transporters SUT1 and SWEET1, the sucrose hydrolyzing enzymes CELL WALL INVERTASE 2 (INCW2) and SUCROSE SYNTHASE 1 (SUSY1), the class II TREHALOSE PHOSPHATE SYNTHASES (TPS), TREHALASE (TRE), and TREHALOSE PHOSPHATE PHOSPHATASE (ZmTPPA.3), previously shown to enhance drought tolerance (Nuccio et al., Nat Biotechnol (October 2014):1-13, 2015). CONCLUSIONS: The impact of kernel excision from the ear triggers a cascade of events starting with the precipitous drop in Tre6P levels. It is proposed that the removal of Tre6P suppression of SnRK1 activity results in transcription of putative SnRK1 target genes, and the metabolic transition from biosynthesis to catabolism. This highlights the importance of Tre6P in the metabolic response to starvation. We also present evidence that sugars can mediate the activation of SnRK1. The precipitous drop in Tre6P corresponds to a large increase in transcription of ZmTPPA.3, indicating that this specific enzyme may be responsible for the de-phosphorylation of Tre6P. The high levels of Tre6P in the immature embryo are likely important for preventing kernel abortion.
[Mh] Termos MeSH primário: Proteínas de Plantas/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Sementes/embriologia
Estresse Fisiológico/efeitos dos fármacos
Fosfatos Açúcares/farmacologia
Trealose/análogos & derivados
Zea mays/embriologia
Zea mays/fisiologia
[Mh] Termos MeSH secundário: Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Metaboloma/efeitos dos fármacos
Modelos Biológicos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Sementes/efeitos dos fármacos
Sementes/genética
Estresse Fisiológico/genética
Sacarose/farmacologia
Trealose/farmacologia
Zea mays/efeitos dos fármacos
Zea mays/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (RNA, Messenger); 0 (Sugar Phosphates); 4484-88-2 (trehalose-6-phosphate); 57-50-1 (Sucrose); B8WCK70T7I (Trehalose); EC 2.7.1.- (SNF1-related protein kinases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1186/s12870-017-1018-2


  3 / 2372 MEDLINE  
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[PMID]:28196976
[Au] Autor:Kuzuyama T
[Ad] Endereço:Biotechnology Research Center, The University of Tokyo, Tokyo, Japan.
[Ti] Título:Biosynthetic studies on terpenoids produced by Streptomyces.
[So] Source:J Antibiot (Tokyo);70(7):811-818, 2017 Jul.
[Is] ISSN:0021-8820
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Terpenoids are a large and highly diverse group of natural products. All terpenoids are biosynthesized from isoprenyl diphosphate formed by the consecutive condensation of the five-carbon monomer isopentenyl diphosphate (IPP) to its isomer dimethylallyl diphosphate (DMAPP). Two distinct biosynthetic pathways produce the essential primary metabolites IPP and DMAPP: the 2-C-methylerythritol 4-phosphate pathway and the mevalonate pathway. The isoprenyl substrates can be cyclized by terpene cyclase into single-ring or multi-ring products, which can be further diversified by subsequent modification reactions, such as hydroxylation and glycosylation. This review article describes the biosynthetic pathways of terpenoids produced by Streptomyces and their related novel enzymes.
[Mh] Termos MeSH primário: Produtos Biológicos/isolamento & purificação
Streptomyces/metabolismo
Terpenos/isolamento & purificação
[Mh] Termos MeSH secundário: Vias Biossintéticas
Eritritol/análogos & derivados
Eritritol/metabolismo
Ácido Mevalônico/metabolismo
Fosfatos Açúcares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (2-C-methylerythritol 4-phosphate); 0 (Biological Products); 0 (Sugar Phosphates); 0 (Terpenes); RA96B954X6 (Erythritol); S5UOB36OCZ (Mevalonic Acid)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170720
[Lr] Data última revisão:
170720
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1038/ja.2017.12


  4 / 2372 MEDLINE  
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[PMID]:28192710
[Au] Autor:Liu C; Dunaway-Mariano D; Mariano PS
[Ad] Endereço:Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, NM 87131, USA.
[Ti] Título:Rational design of reversible inhibitors for trehalose 6-phosphate phosphatases.
[So] Source:Eur J Med Chem;128:274-286, 2017 Mar 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In some organisms, environmental stress triggers trehalose biosynthesis that is catalyzed collectively by trehalose 6-phosphate synthase, and trehalose 6-phosphate phosphatase (T6PP). T6PP catalyzes the hydrolysis of trehalose 6-phosphate (T6P) to trehalose and inorganic phosphate and is a promising target for the development of antibacterial, antifungal and antihelminthic therapeutics. Herein, we report the design, synthesis and evaluation of a library of aryl d-glucopyranoside 6-sulfates to serve as prototypes for small molecule T6PP inhibitors. Steady-state kinetic techniques were used to measure inhibition constants (K ) of a panel of structurally diverse T6PP orthologs derived from the pathogens Brugia malayi, Ascaris suum, Mycobacterium tuberculosis, Shigella boydii and Salmonella typhimurium. The binding affinities of the most active inhibitor of these T6PP orthologs, 4-n-octylphenyl α-d-glucopyranoside 6-sulfate (9a), were found to be in the low micromolar range. The K of 9a with the B. malayi T6PP ortholog is 5.3 ± 0.6 µM, 70-fold smaller than the substrate Michaelis constant. The binding specificity of 9a was demonstrated using several representative sugar phosphate phosphatases from the HAD enzyme superfamily, the T6PP protein fold family of origin. Lastly, correlations drawn between T6PP active site structure, inhibitor structure and inhibitor binding affinity suggest that the aryl d-glucopyranoside 6-sulfate prototypes will find future applications as a platform for development of tailored second-generation T6PP inhibitors.
[Mh] Termos MeSH primário: Desenho de Drogas
Inibidores Enzimáticos/farmacologia
Glucosiltransferases/antagonistas & inibidores
Monossacarídeos/farmacologia
Fosfatos Açúcares/metabolismo
Trealose/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Brugia Malayi/enzimologia
Inibidores Enzimáticos/química
Ensaios de Triagem em Larga Escala
Seres Humanos
Mycobacterium tuberculosis/enzimologia
Salmonella typhimurium/enzimologia
Shigella boydii/enzimologia
Trealose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-n-octylphenyl alpha-D-glucopyranoside-6-sulfate); 0 (Enzyme Inhibitors); 0 (Monosaccharides); 0 (Sugar Phosphates); 4484-88-2 (trehalose-6-phosphate); B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.15 (trehalose-6-phosphate synthase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170418
[Lr] Data última revisão:
170418
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170214
[St] Status:MEDLINE


  5 / 2372 MEDLINE  
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[PMID]:28139350
[Au] Autor:Kudoh K; Hotta S; Sekine M; Fujii R; Uchida A; Kubota G; Kawano Y; Ihara M
[Ad] Endereço:Department of Bioscience and Food Production Science, Interdisciplinary Graduate School of Science and Technology, Shinshu University, 8304 Minamiminowa, Nagano 399-4511, Japan.
[Ti] Título:Overexpression of endogenous 1-deoxy-d-xylulose 5-phosphate synthase (DXS) in cyanobacterium Synechocystis sp. PCC6803 accelerates protein aggregation.
[So] Source:J Biosci Bioeng;123(5):590-596, 2017 May.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:1-Deoxy-d-xylulose 5-phosphate synthase (DXS) is a rate-limiting enzyme in the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway, which is responsible for the production of precursors of all isoprenoids. In a previous study, we had examined the overexpression of an endogenous DXS in a Synechocystis sp. PCC6803 mutant (DXS_ox), and found that the dxs mRNA level was 4-fold higher than that in the wild-type (WT) strain. However, the DXS protein level was only 1.5-fold higher, leading to the assumption that the level might be regulated by post-transcriptional events. In this study, we have additionally introduced an exogenous isoprene synthase (IspS; which can release MEP pathway products from the cell as gaseous isoprene) into the WT and DXS_ox strains (WT-isP and DXSox-isP strains, respectively), and their detailed DXS expression profiles were investigated from the induction phase through to the late-logarithmic phase. In the induction phase, the isoprene productivity of the DXSox-isP strain was slightly but significantly (1.4- to 1.8-fold) higher than that of the WT-isP strain, whereas the levels were comparable in the other phases. Interestingly, the ratios of soluble:insoluble DXS protein were remarkably low in the DXSox-isP strain during the induction phase to the early-logarithmic phase, resulting in a moderate level of soluble DXS. All our results suggested that the high translation rate of DXS disturbs the refolding process of DXS. To enhance the concentration of the active DXS in cyanobacteria, the enhancement of the DXS maturation system or the introduction of exogenous and robust DXS proteins might be necessary.
[Mh] Termos MeSH primário: Agregados Proteicos
Synechocystis/genética
Synechocystis/metabolismo
Transferases/genética
Transferases/metabolismo
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/biossíntese
Alquil e Aril Transferases/genética
Alquil e Aril Transferases/metabolismo
Butadienos
Eritritol/análogos & derivados
Eritritol/metabolismo
Gases/metabolismo
Hemiterpenos/biossíntese
Engenharia Metabólica
Pentanos
Pentosefosfatos/biossíntese
RNA Mensageiro/análise
Solubilidade
Fosfatos Açúcares/metabolismo
Terpenos/metabolismo
Transferases/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-deoxylulose 5-phosphate); 0 (2-C-methylerythritol 4-phosphate); 0 (Butadienes); 0 (Gases); 0 (Hemiterpenes); 0 (Pentanes); 0 (Pentosephosphates); 0 (Protein Aggregates); 0 (RNA, Messenger); 0 (Sugar Phosphates); 0 (Terpenes); 0A62964IBU (isoprene); EC 2.- (Transferases); EC 2.2.1.- (deoxyxylulose-5-phosphate synthase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (isoprene synthase); RA96B954X6 (Erythritol)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


  6 / 2372 MEDLINE  
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[PMID]:28063198
[Au] Autor:Wierzbicki IH; Zielke RA; Korotkov KV; Sikora AE
[Ad] Endereço:Department of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, OR, USA.
[Ti] Título:Functional and structural studies on the Neisseria gonorrhoeae GmhA, the first enzyme in the glycero-manno-heptose biosynthesis pathways, demonstrate a critical role in lipooligosaccharide synthesis and gonococcal viability.
[So] Source:Microbiologyopen;6(2), 2017 Apr.
[Is] ISSN:2045-8827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sedoheptulose-7-phosphate isomerase, GmhA, is the first enzyme in the biosynthesis of nucleotide-activated-glycero-manno-heptoses and an attractive, yet underexploited, target for development of broad-spectrum antibiotics. We demonstrated that GmhA homologs in Neisseria gonorrhoeae and N. meningitidis (hereafter called GmhA and GmhA , respectively) were interchangeable proteins essential for lipooligosaccharide (LOS) synthesis, and their depletion had adverse effects on neisserial viability. In contrast, the Escherichia coli ortholog failed to complement GmhA depletion. Furthermore, we showed that GmhA is a cytoplasmic enzyme with induced expression at mid-logarithmic phase, upon iron deprivation and anaerobiosis, and conserved in contemporary gonococcal clinical isolates including the 2016 WHO reference strains. The untagged GmhA crystallized as a tetramer in the closed conformation with four zinc ions in the active site, supporting that this is most likely the catalytically active conformation of the enzyme. Finally, site-directed mutagenesis studies showed that the active site residues E65 and H183 were important for LOS synthesis but not for GmhA function in bacterial viability. Our studies bring insights into the importance and mechanism of action of GmhA and may ultimately facilitate targeting the enzyme with small molecule inhibitors.
[Mh] Termos MeSH primário: Proteínas de Bactérias/ultraestrutura
Carboidratos Epimerases/ultraestrutura
Heptoses/biossíntese
Lipopolissacarídeos/biossíntese
Neisseria gonorrhoeae/enzimologia
Neisseria meningitidis/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Carboidratos Epimerases/genética
Domínio Catalítico/genética
Mutagênese Sítio-Dirigida
Neisseria gonorrhoeae/genética
Neisseria meningitidis/genética
Fosfatos Açúcares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Heptoses); 0 (Lipopolysaccharides); 0 (Sugar Phosphates); 0 (lipid-linked oligosaccharides); 2646-35-7 (sedoheptulose 7-phosphate); 4305-74-2 (glycero-manno-heptose); EC 5.1.3.- (Carbohydrate Epimerases); EC 5.1.3.- (sedoheptulose-7-phosphate isomerase, Neisseria gonorrhoeae)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE
[do] DOI:10.1002/mbo3.432


  7 / 2372 MEDLINE  
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[PMID]:28045507
[Au] Autor:Balachandran N; To F; Berti PJ
[Ad] Endereço:Department of Chemistry & Chemical Biology and ‡Department of Biochemistry & Biomedical Sciences, McMaster University , 1280 Main Street West, Hamilton, Ontario L8S 4M1, Canada.
[Ti] Título:Linear Free Energy Relationship Analysis of Transition State Mimicry by 3-Deoxy-d-arabino-heptulosonate-7-phosphate (DAHP) Oxime, a DAHP Synthase Inhibitor and Phosphate Mimic.
[So] Source:Biochemistry;56(4):592-601, 2017 Jan 31.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:3-Deoxy-d-arabino-heptulosonate-7-phosphate (DAHP) synthase catalyzes an aldol-like reaction of phosphoenolpyruvate (PEP) with erythrose 4-phosphate (E4P) to form DAHP in the first step of the shikimate biosynthetic pathway. DAHP oxime, in which an oxime replaces the ketone, is a potent inhibitor, with K = 1.5 µM. Linear free energy relationship (LFER) analysis of DAHP oxime inhibition using DAHP synthase mutants revealed an excellent correlation between transition state stabilization and inhibition. The equations of LFER analysis were rederived to formalize the possibility of proportional, rather than equal, changes in the free energies of transition state stabilization and inhibitor binding, in accord with the fact that the majority of LFER analyses in the literature demonstrate nonunity slopes. A slope of unity, m = 1, indicates that catalysis and inhibitor binding are equally sensitive to perturbations such as mutations or modified inhibitor/substrate structures. Slopes <1 or >1 indicate that inhibitor binding is less sensitive or more sensitive, respectively, to perturbations than is catalysis. LFER analysis using the tetramolecular specificity constant, that is, plotting log(K K K /k ) versus log(K ), revealed a slope, m, of 0.34, with r = 0.93. This provides evidence that DAHP oxime is mimicking the first irreversible transition state of the DAHP synthase reaction, presumably phosphate departure from the tetrahedral intermediate. This is evidence that the oxime group can act as a functional, as well as structural, mimic of phosphate groups.
[Mh] Termos MeSH primário: 3-Desoxi-7-Fosfo-Heptulonato Sintase/antagonistas & inibidores
Proteínas de Bactérias/antagonistas & inibidores
Inibidores Enzimáticos/química
Oximas/química
Proteínas Recombinantes de Fusão/química
Fosfatos Açúcares/química
[Mh] Termos MeSH secundário: 3-Desoxi-7-Fosfo-Heptulonato Sintase/química
3-Desoxi-7-Fosfo-Heptulonato Sintase/genética
3-Desoxi-7-Fosfo-Heptulonato Sintase/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Biocatálise
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Cinética
Modelos Moleculares
Mimetismo Molecular
Mutação
Fosfoenolpiruvato/química
Fosfoenolpiruvato/metabolismo
Ligação Proteica
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Ácido Chiquímico/química
Ácido Chiquímico/metabolismo
Fosfatos Açúcares/metabolismo
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzyme Inhibitors); 0 (Oximes); 0 (Recombinant Fusion Proteins); 0 (Sugar Phosphates); 2627-73-8 (3-deoxy-D-arabino-heptulosonate-7-phosphate); 29MS2WI2NU (Shikimic Acid); 585-18-2 (erythrose 4-phosphate); 73-89-2 (Phosphoenolpyruvate); EC 2.5.1.54 (3-Deoxy-7-Phosphoheptulonate Synthase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01211


  8 / 2372 MEDLINE  
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[PMID]:27903647
[Au] Autor:Asención Diez MD; Miah F; Stevenson CE; Lawson DM; Iglesias AA; Bornemann S
[Ad] Endereço:the Laboratorio de Enzimología Molecular, Instituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas, CCT-Santa Fe, Colectora Ruta Nac 168 Km 0, 3000 Santa Fe, Argentina.
[Ti] Título:The Production and Utilization of GDP-glucose in the Biosynthesis of Trehalose 6-Phosphate by Streptomyces venezuelae.
[So] Source:J Biol Chem;292(3):945-954, 2017 Jan 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trehalose-6-phosphate synthase OtsA from streptomycetes is unusual in that it uses GDP-glucose as the donor substrate rather than the more commonly used UDP-glucose. We now confirm that OtsA from Streptomyces venezuelae has such a preference for GDP-glucose and can utilize ADP-glucose to some extent too. A crystal structure of the enzyme shows that it shares twin Rossmann-like domains with the UDP-glucose-specific OtsA from Escherichia coli However, it is structurally more similar to Streptomyces hygroscopicus VldE, a GDP-valienol-dependent pseudoglycosyltransferase enzyme. Comparison of the donor binding sites reveals that the amino acids associated with the binding of diphosphoribose are almost all identical in these three enzymes. By contrast, the amino acids associated with binding guanine in VldE (Asn, Thr, and Val) are similar in S. venezuelae OtsA (Asp, Ser, and Phe, respectively) but not conserved in E. coli OtsA (His, Leu, and Asp, respectively), providing a rationale for the purine base specificity of S. venezuelae OtsA. To establish which donor is used in vivo, we generated an otsA null mutant in S. venezuelae The mutant had a cell density-dependent growth phenotype and accumulated galactose 1-phosphate, glucose 1-phosphate, and GDP-glucose when grown on galactose. To determine how the GDP-glucose is generated, we characterized three candidate GDP-glucose pyrophosphorylases. SVEN_3027 is a UDP-glucose pyrophosphorylase, SVEN_3972 is an unusual ITP-mannose pyrophosphorylase, and SVEN_2781 is a pyrophosphorylase that is capable of generating GDP-glucose as well as GDP-mannose. We have therefore established how S. venezuelae can make and utilize GDP-glucose in the biosynthesis of trehalose 6-phosphate.
[Mh] Termos MeSH primário: Açúcares de Guanosina Difosfato/metabolismo
Streptomyces/metabolismo
Fosfatos Açúcares/biossíntese
Trealose/análogos & derivados
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Escherichia coli/genética
Escherichia coli/metabolismo
Galactose/genética
Galactose/metabolismo
Glucosiltransferases/genética
Glucosiltransferases/metabolismo
Açúcares de Guanosina Difosfato/genética
Streptomyces/genética
Fosfatos Açúcares/genética
Trealose/biossíntese
Trealose/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (GDP-gulose); 0 (Guanosine Diphosphate Sugars); 0 (Sugar Phosphates); 4484-88-2 (trehalose-6-phosphate); B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.15 (trehalose-6-phosphate synthase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.758664


  9 / 2372 MEDLINE  
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[PMID]:27856234
[Au] Autor:Kudoh K; Kubota G; Fujii R; Kawano Y; Ihara M
[Ad] Endereço:Department of Bioscience and Food Production Science, Interdisciplinary Graduate School of Science and Technology, Shinshu University, 8304 Minamiminowa, Nagano 399-4511, Japan.
[Ti] Título:Exploration of the 1-deoxy-d-xylulose 5-phosphate synthases suitable for the creation of a robust isoprenoid biosynthesis system.
[So] Source:J Biosci Bioeng;123(3):300-307, 2017 Mar.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:1-Deoxy-d-xylulose 5-phosphate synthase (DXS) is a rate-limiting enzyme in the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway, which is responsible for production of two precursors of all isoprenoids, isopentenyl diphosphate and dimethylallyl diphosphate (DMAPP). Previously, we attempted the overexpression of endogenous DXS in Synechocystis sp. PCC6803, and revealed that although the mRNA level was 4-fold higher, the DXS protein level was only 1.5-fold higher compared with those of the original strain, suggesting the lability of endogenous DXS protein. Therefore, for the creation of a robust isoprenoid synthesis system, it is necessary to build a novel MEP pathway by combining stable enzymes. In this study, we expressed 11 dxs genes from 9 organisms in Escherichia coli and analyzed their protein solubility. Furthermore, we purified the recombinant DXSes and evaluated their specific activities and protease tolerance, thermostability, and feedback inhibition tolerance. Among DXSes we examined in this study, the highest protein solubility was observed in Paracoccus aminophilus DXS (PaDXS). The DXS with the highest activity was one from Rhodobacter capsulatus (RcDXSA). The highest protease tolerance, thermostability, and tolerance of feedback inhibition were found in Bacillus subtilis DXS (BsDXS), RcDXSA, PaDXS, BsDXS, respectively. These DXSes can be potentially used for the design of robust isoprenoid synthesis system.
[Mh] Termos MeSH primário: Escherichia coli/genética
Escherichia coli/metabolismo
Terpenos/metabolismo
Transferases/genética
Transferases/metabolismo
[Mh] Termos MeSH secundário: Bacillus subtilis/enzimologia
Bacillus subtilis/genética
Estabilidade Enzimática
Eritritol/análogos & derivados
Eritritol/biossíntese
Hemiterpenos/biossíntese
Hemiterpenos/metabolismo
Compostos Organofosforados/metabolismo
Paracoccus/enzimologia
Paracoccus/genética
Pentosefosfatos/biossíntese
Peptídeo Hidrolases/metabolismo
Rhodobacter capsulatus/enzimologia
Rhodobacter capsulatus/genética
Solubilidade
Fosfatos Açúcares/biossíntese
Synechocystis/genética
Synechocystis/metabolismo
Transferases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-deoxylulose 5-phosphate); 0 (2-C-methylerythritol 4-phosphate); 0 (Hemiterpenes); 0 (Organophosphorus Compounds); 0 (Pentosephosphates); 0 (Sugar Phosphates); 0 (Terpenes); 358-71-4 (isopentenyl pyrophosphate); 358-72-5 (3,3-dimethylallyl pyrophosphate); EC 2.- (Transferases); EC 2.2.1.- (deoxyxylulose-5-phosphate synthase); EC 3.4.- (Peptide Hydrolases); RA96B954X6 (Erythritol)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE


  10 / 2372 MEDLINE  
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[PMID]:27796871
[Au] Autor:Magalhães RS; De Lima KC; de Almeida DS; De Mesquita JF; Eleutherio EC
[Ad] Endereço:Department of Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
[Ti] Título:Trehalose-6-Phosphate as a Potential Lead Candidate for the Development of Tps1 Inhibitors: Insights from the Trehalose Biosynthesis Pathway in Diverse Yeast Species.
[So] Source:Appl Biochem Biotechnol;181(3):914-924, 2017 Mar.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In some pathogens, trehalose biosynthesis is induced in response to stress as a protection mechanism. This pathway is an attractive target for antimicrobials as neither the enzymes, Tps1, and Tps2, nor is trehalose present in humans. Accumulation of T6P in Candida albicans, achieved by deletion of TPS2, resulted in strong reduction of fungal virulence. In this work, the effect of T6P on Tps1 activity was evaluated. Saccharomyces cerevisiae, C. albicans, and Candida tropicalis were used as experimental models. As expected, a heat stress induced both trehalose accumulation and increased Tps1 activity. However, the addition of 125 µM T6P to extracts obtained from stressed cells totally abolished or reduced in 50 and 60 % the induction of Tps1 activity in S. cerevisiae, C. tropicalis, and C. albicans, respectively. According to our results, T6P is an uncompetitive inhibitor of S. cerevisiae Tps1. This kind of inhibitor is able to decrease the rate of reaction to zero at increased concentrations. Based on the similarities found in sequence and function between Tps1 of S. cerevisiae and some pathogens and on the inhibitory effect of T6P on Tps1 activity observed in vitro, novel drugs can be developed for the treatment of infectious diseases caused by organisms whose infectivity and survival on the host depend on trehalose.
[Mh] Termos MeSH primário: Candida albicans/enzimologia
Candida tropicalis/enzimologia
Inibidores Enzimáticos/química
Glucosiltransferases/antagonistas & inibidores
Saccharomyces cerevisiae/enzimologia
Fosfatos Açúcares/química
Trealose/análogos & derivados
[Mh] Termos MeSH secundário: Candida albicans/patogenicidade
Candida tropicalis/patogenicidade
Candidíase/tratamento farmacológico
Candidíase/enzimologia
Inibidores Enzimáticos/farmacologia
Especificidade da Espécie
Fosfatos Açúcares/farmacologia
Trealose/química
Trealose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Sugar Phosphates); 4484-88-2 (trehalose-6-phosphate); B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.15 (trehalose-6-phosphate synthase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2258-6



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