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Pesquisa : D03.633.100.759.646.454.340.350 [Categoria DeCS]
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[PMID]:28104756
[Au] Autor:López-Gutiérrez B; Dinglasan RR; Izquierdo L
[Ad] Endereço:ISGlobal, Barcelona Ctr. Int. Health Res. (CRESIB), Hospital Clínic - Universitat de Barcelona, Barcelona, Spain.
[Ti] Título:Sugar nucleotide quantification by liquid chromatography tandem mass spectrometry reveals a distinct profile in sexual stage parasites.
[So] Source:Biochem J;474(6):897-905, 2017 Mar 07.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The obligate intracellular lifestyle of and the difficulties in obtaining sufficient amounts of biological material have hampered the study of specific metabolic pathways in the malaria parasite. Thus, for example, the pools of sugar nucleotides required to fuel glycosylation reactions have never been studied in-depth in well-synchronized asexual parasites or in other stages of its life cycle. These metabolites are of critical importance, especially considering the renewed interest in the presence of -, -, and other glycans in key parasite proteins. In this work, we adapted a liquid chromatography tandem mass spectrometry (LC-MS/MS) method based on the use of porous graphitic carbon (PGC) columns and MS-friendly solvents to quantify sugar nucleotides in the malaria parasite. We report the thorough quantification of the pools of these metabolites throughout the intraerythrocytic cycle of The sensitivity of the method enabled, for the first time, the targeted analysis of these glycosylation precursors in gametocytes, the parasite sexual stages that are transmissible to the mosquito vector.
[Mh] Termos MeSH primário: Guanosina Difosfato Fucose/metabolismo
Guanosina Difosfato Manose/metabolismo
Açúcares de Guanosina Difosfato/metabolismo
Plasmodium falciparum/metabolismo
Uridina Difosfato Galactose/metabolismo
Uridina Difosfato Glucose/metabolismo
Uridina Difosfato N-Acetilgalactosamina/metabolismo
[Mh] Termos MeSH secundário: Cromatografia Líquida
Eritrócitos/parasitologia
Gametogênese/fisiologia
Guanosina Difosfato Fucose/análise
Guanosina Difosfato Manose/análise
Açúcares de Guanosina Difosfato/análise
Seres Humanos
Estágios do Ciclo de Vida/fisiologia
Plasmodium falciparum/crescimento & desenvolvimento
Espectrometria de Massas em Tandem
Uridina Difosfato Galactose/análise
Uridina Difosfato Glucose/análise
Uridina Difosfato N-Acetilgalactosamina/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Guanosine Diphosphate Sugars); 15839-70-0 (Guanosine Diphosphate Fucose); 2956-16-3 (Uridine Diphosphate Galactose); 3123-67-9 (Guanosine Diphosphate Mannose); 5750-57-2 (guanosine diphosphate glucose); 7277-98-7 (Uridine Diphosphate N-Acetylgalactosamine); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20161030


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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


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[PMID]:26703456
[Au] Autor:Wu Z; Zhao G; Li T; Qu J; Guan W; Wang J; Ma C; Li X; Zhao W; Wang PG; Li L
[Ad] Endereço:Department of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
[Ti] Título:Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7.
[So] Source:Glycobiology;26(5):493-500, 2016 May.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Colitose, also known as 3,6-dideoxy-L-galactose or 3-deoxy-L-fucose, is one of only five naturally occurring 3,6-dideoxyhexoses. Colitose was found in lipopolysaccharide of a number of infectious bacteria, including Escherichia coli O55 & O111 and Vibrio cholera O22 & O139. To date, no colitosyltransferase (ColT) has been characterized, probably due to the inaccessibility of the sugar donor, GDP-colitose. In this study, starting with chemically prepared colitose, 94.6 mg of GDP-colitose was prepared via a facile and efficient one-pot two-enzyme system involving an L-fucokinase/GDP-L-Fuc pyrophosphorylase and an inorganic pyrophosphatase (EcPpA). WbgN, a putative ColT from E. coliO55:H5 was then cloned, overexpressed, purified and biochemically characterized by using GDP-colitose as a sugar donor. Activity assay and structural identification of the synthetic product clearly demonstrated that wbgN encodes an α1,2-ColT. Biophysical study showed that WbgN does not require metal ion, and is highly active at pH 7.5-9.0. In addition, acceptor specificity study indicated that WbgN exclusively recognizes lacto-N-biose (Galß1,3-GlcNAc). Most interestingly, it was found that WbgN exhibits similar activity toward GDP-l-Fuc (kcat/Km= 9.2 min(-1)mM(-1)) as that toward GDP-colitose (kcat/Km= 12 min(-1)mM(-1)). Finally, taking advantage of this, type 1 H-antigen was successfully synthesized in preparative scale.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Escherichia coli/enzimologia
Glucosiltransferases/química
Glucosiltransferases/metabolismo
[Mh] Termos MeSH secundário: Desoxiaçúcares/química
Desoxiaçúcares/genética
Desoxiaçúcares/metabolismo
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Glucosiltransferases/genética
Açúcares de Guanosina Difosfato/química
Açúcares de Guanosina Difosfato/genética
Açúcares de Guanosina Difosfato/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Deoxy Sugars); 0 (Escherichia coli Proteins); 0 (Guanosine Diphosphate Sugars); 0 (guanosine diphosphate-colitose); 4221-05-0 (colitose); EC 2.4.1.- (Glucosyltransferases)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170501
[Lr] Data última revisão:
170501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151226
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwv169


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[PMID]:24508535
[Au] Autor:Gao Y; Jiang Y; Liu Q; Wang R; Liu X; Liu B
[Ad] Endereço:College of Food and Bioengineering, Qilu University of Technology, Jinan, Shandong 250353, PR China.
[Ti] Título:Enzymatic and regulatory properties of the trehalose-6-phosphate synthase from the thermoacidophilic archaeon Thermoplasma acidophilum.
[So] Source:Biochimie;101:215-20, 2014 Jun.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Trehalose-6-phosphate synthase plays an important role in trehalose metabolism. It catalyzes the transfer of glucose from UDP-glucose (UDPG) to glucose 6-phosphate to produce trehalose-6-phosphate. Herein we describe the characterization of a trehalose-6-phosphate synthase from the thermoacidophilic archaeon Thermoplasma acidophilum. The dimeric enzyme could utilize UDPG, ADP-Glucose (ADPG) and GDP-Glucose (GDPG) as glycosyl donors and various phosphorylated monosaccharides as glycosyl acceptors. The optimal temperature and pH were found to be 60 °C and pH 6, and the enzyme exhibited notable pH and thermal stability. The enzymatic activity could be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate. Moreover, the protein was considerably resistant to additives ethanol, EDTA, urea, DTT, SDS, ß-mercaptoethanol, methanol, isopropanol and n-butanol. Molecular modeling and mutagenesis analysis revealed that the N-loop region was important for the catalytic efficiency of the enzyme, indicating different roles of N-loop sequences in different trehalose-6-phosphate synthases.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Glucosiltransferases/química
Thermoplasma/enzimologia
[Mh] Termos MeSH secundário: Adenosina Difosfato Glucose/química
Sequência de Aminoácidos
Substituição de Aminoácidos
Proteínas Arqueais/genética
Domínio Catalítico
Estabilidade Enzimática
Glucosiltransferases/genética
Glicosilação
Açúcares de Guanosina Difosfato/química
Concentração de Íons de Hidrogênio
Magnésio/química
Modelos Moleculares
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Desnaturação Proteica
Estrutura Quaternária de Proteína
Especificidade por Substrato
Uridina Difosfato Glucose/química
Zinco/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Guanosine Diphosphate Sugars); 2140-58-1 (Adenosine Diphosphate Glucose); 5750-57-2 (guanosine diphosphate glucose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.15 (trehalose-6-phosphate synthase); I38ZP9992A (Magnesium); J41CSQ7QDS (Zinc); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:140421
[Lr] Data última revisão:
140421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140211
[St] Status:MEDLINE


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[PMID]:24380627
[Au] Autor:Lin CI; Sasaki E; Zhong A; Liu HW
[Ad] Endereço:Division of Medicinal Chemistry, College of Pharmacy, and Department of Chemistry, University of Texas at Austin , Austin, Texas 78712, United States.
[Ti] Título:In vitro characterization of LmbK and LmbO: identification of GDP-D-erythro-α-D-gluco-octose as a key intermediate in lincomycin A biosynthesis.
[So] Source:J Am Chem Soc;136(3):906-9, 2014 Jan 22.
[Is] ISSN:1520-5126
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lincomycin A is a clinically useful antibiotic isolated from Streptomyces lincolnensis. It contains an unusual methylmercapto-substituted octose, methylthiolincosamide (MTL). While it has been demonstrated that the C8 backbone of MTL moiety is derived from D-fructose 6-phosphate and D-ribose 5-phosphate via a transaldol reaction catalyzed by LmbR, the subsequent enzymatic transformations leading to the MTL moiety remain elusive. Here, we report the identification of GDP-D-erythro-α-D-gluco-octose (GDP-D-α-D-octose) as a key intermediate in the MTL biosynthetic pathway. Our data show that the octose 1,8-bisphosphate intermediate is first converted to octose 1-phosphate by a phosphatase, LmbK. The subsequent conversion of the octose 1-phosphate to GDP-D-α-D-octose is catalyzed by the octose 1-phosphate guanylyltransferase, LmbO. These results provide significant insight into the lincomycin biosynthetic pathway, because the activated octose likely serves as the acceptor for the installation of the C1 sulfur appendage of MTL.
[Mh] Termos MeSH primário: Açúcares de Guanosina Difosfato/metabolismo
Lincomicina/biossíntese
Monossacarídeos/metabolismo
Nucleotidiltransferases/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Streptomyces/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Guanosine Diphosphate Sugars); 0 (Monosaccharides); BOD072YW0F (Lincomycin); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.- (guanylyltransferase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140102
[St] Status:MEDLINE
[do] DOI:10.1021/ja412194w


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[PMID]:23774504
[Au] Autor:Zhou H; Sun L; Li J; Xu C; Yu F; Liu Y; Ji C; He J
[Ad] Endereço:Department of Biological Sciences, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:The crystal structure of human GDP-L-fucose synthase.
[So] Source:Acta Biochim Biophys Sin (Shanghai);45(9):720-5, 2013 Sep.
[Is] ISSN:1745-7270
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Human GDP-l-fucose synthase, also known as FX protein, synthesizes GDP-l-fucose from its substrate GDP-4-keto-6-deoxy-d-mannose. The reaction involves epimerization at both C-3 and C-5 followed by an NADPH-dependent reduction of the carbonyl at C-4. In this paper, the first crystal structure of human FX protein was determined at 2.37 Å resolution. The asymmetric unit of the crystal structure contains four molecules which form two homodimers. Each molecule consists of two domains, a Rossmann-fold NADPH-binding motif and a carboxyl terminal domain. Compared with the Escherichia coli GDP-l-fucose synthase, the overall structures of these two enzymes have four major differences. There are four loops in the structure of human FX protein corresponding to two α-helices and two ß-sheets in that of the E. coli enzyme. Besides, there are seven different amino acid residues binding with NAPDH comparing human FX protein with that from E. coli. The structure of human FX reveals the key catalytic residues and could be useful for the design of drugs for the treatment of inflammation, auto-immune diseases, and possibly certain types of cancer.
[Mh] Termos MeSH primário: Carboidratos Epimerases/química
Cetona Oxirredutases/química
Multimerização Proteica
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Biocatálise
Carboidratos Epimerases/genética
Carboidratos Epimerases/metabolismo
Cristalografia por Raios X
Escherichia coli/enzimologia
Escherichia coli/genética
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Guanosina Difosfato Manose/análogos & derivados
Guanosina Difosfato Manose/metabolismo
Açúcares de Guanosina Difosfato/metabolismo
Seres Humanos
Cetona Oxirredutases/genética
Cetona Oxirredutases/metabolismo
Modelos Moleculares
NADP/química
NADP/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (GDP-gulose); 0 (Guanosine Diphosphate Sugars); 0 (Recombinant Proteins); 18186-48-6 (GDP-4-keto-6-deoxymannose); 3123-67-9 (Guanosine Diphosphate Mannose); 53-59-8 (NADP); EC 1.1.1.271 (TSTA3 protein, human); EC 1.2.- (Ketone Oxidoreductases); EC 5.1.3.- (Carbohydrate Epimerases)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:130821
[Lr] Data última revisão:
130821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130619
[St] Status:MEDLINE
[do] DOI:10.1093/abbs/gmt066


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[PMID]:23695979
[Au] Autor:Mortimer JC; Yu X; Albrecht S; Sicilia F; Huichalaf M; Ampuero D; Michaelson LV; Murphy AM; Matsunaga T; Kurz S; Stephens E; Baldwin TC; Ishii T; Napier JA; Weber AP; Handford MG; Dupree P
[Ad] Endereço:Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom.
[Ti] Título:Abnormal glycosphingolipid mannosylation triggers salicylic acid-mediated responses in Arabidopsis.
[So] Source:Plant Cell;25(5):1881-94, 2013 May.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Arabidopsis thaliana protein GOLGI-LOCALIZED NUCLEOTIDE SUGAR TRANSPORTER (GONST1) has been previously identified as a GDP-d-mannose transporter. It has been hypothesized that GONST1 provides precursors for the synthesis of cell wall polysaccharides, such as glucomannan. Here, we show that in vitro GONST1 can transport all four plant GDP-sugars. However, gonst1 mutants have no reduction in glucomannan quantity and show no detectable alterations in other cell wall polysaccharides. By contrast, we show that a class of glycosylated sphingolipids (glycosylinositol phosphoceramides [GIPCs]) contains Man and that this mannosylation is affected in gonst1. GONST1 therefore is a Golgi GDP-sugar transporter that specifically supplies GDP-Man to the Golgi lumen for GIPC synthesis. gonst1 plants have a dwarfed phenotype and a constitutive hypersensitive response with elevated salicylic acid levels. This suggests an unexpected role for GIPC sugar decorations in sphingolipid function and plant defense signaling. Additionally, we discuss these data in the context of substrate channeling within the Golgi.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Glicoesfingolipídeos/metabolismo
Manose/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Ácido Salicílico/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Transporte Biológico/genética
Parede Celular/genética
Parede Celular/metabolismo
Glicosilação
Complexo de Golgi/metabolismo
Guanosina Difosfato Fucose/metabolismo
Guanosina Difosfato Manose/metabolismo
Açúcares de Guanosina Difosfato/metabolismo
Immunoblotting
Proteínas de Membrana Transportadoras/genética
Microscopia de Fluorescência
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (GONST1 protein, Arabidopsis); 0 (Glycosphingolipids); 0 (Guanosine Diphosphate Sugars); 0 (Membrane Transport Proteins); 15839-70-0 (Guanosine Diphosphate Fucose); 3123-67-9 (Guanosine Diphosphate Mannose); 5750-57-2 (guanosine diphosphate glucose); O414PZ4LPZ (Salicylic Acid); PHA4727WTP (Mannose)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130523
[St] Status:MEDLINE
[do] DOI:10.1105/tpc.113.111500


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[PMID]:23664878
[Au] Autor:Wang S; Tanaka H; Hindsgaul O; Lam JS; Brockhausen I
[Ad] Endereço:Department of Medicine, Queen's University, Kingston, Ontario, Canada K7L 3N6.
[Ti] Título:A convenient synthesis of GDP-D-rhamnose: the donor substrate for D-rhamnosyltransferase WbpZ from Pseudomonas aeruginosa PAO1.
[So] Source:Bioorg Med Chem Lett;23(12):3491-5, 2013 Jun 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gram negative bacteria have lipopolysaccharides (LPS) that are critical for their survival. LPS molecules are composed of antigenic exopolysaccharide chains (O antigens). We are interested in discovering the enzymes involved in the biosynthesis of O antigens in Pseudomonas aeruginosa. The common polysaccharide antigen contains α-linked D-rhamnose residues. We have now synthesized GDP-D-rhamnose by a convenient synthesis in aqueous solution, and have shown that it can be used without extensive purification as the donor substrate for D-rhamnosyltransferase (WbpZ) from the P. aeruginosa strain PAO1. The availability of this nucleotide sugar preparation allows for characterization of D-rhamnosyltransferases.
[Mh] Termos MeSH primário: Açúcares de Guanosina Difosfato/síntese química
Hexosiltransferases/metabolismo
Pseudomonas aeruginosa/enzimologia
[Mh] Termos MeSH secundário: Açúcares de Guanosina Difosfato/química
Açúcares de Guanosina Difosfato/metabolismo
Pseudomonas aeruginosa/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (GDP-rhamnose); 0 (Guanosine Diphosphate Sugars); EC 2.4.1.- (Hexosyltransferases); EC 2.4.1.- (LPS rhamnosyltransferases)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:130520
[Lr] Data última revisão:
130520
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130514
[St] Status:MEDLINE


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[PMID]:23470736
[Au] Autor:Chiku K; Tsunemi K; Yamamoto M; Ohnishi-Kameyama M; Yoshida M; Ishii T; Taguchi F; Iwaki M; Ichinose Y; Ono H
[Ad] Endereço:National Food Research Institute, Tsukuba, Ibaraki, Japan.
[Ti] Título:Defects in D-rhamnosyl residue biosynthetic genes affect lipopolysaccharide structure, motility, and cell-surface hydrophobicity in Pseudomonas syringae pathovar glycinea race 4.
[So] Source:Biosci Biotechnol Biochem;77(3):505-10, 2013.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:D-rhamnose (D-Rha) residue is a major component of lipopolysaccharides (LPSs) in strains of the phytopathogen Pseudomonas syringae pathovar glycinea. To investigate the effects of a deficiency in GDP-D-rhamnose biosynthetic genes on LPS structure and pathogenicity, we generated three mutants defective in D-Rha biosynthetic genes, encoding proteins GDP-D-mannose 4,6-dehydratase (GMD), GDP-4-keto-6-deoxy-D-mannose reductase (RMD), and a putative α-D-rhamnosyltransferase (WbpZ) in P. syringae pv. glycinea race 4. The Δgmd, Δrmd, and ΔwbpZ mutants had a reduced O-antigen polysaccharide consisting of D-Rha residues as compared with the wild type (WT). The swarming motility of the Δgmd, Δrmd, and ΔwbpZ mutant strains decreased and hydrophobicity and adhesion ability increased as compared with WT. Although the mutants had truncated O-antigen polysaccharides, and altered surface properties, they showed virulence to soybean, as WT did.
[Mh] Termos MeSH primário: Interações Hidrofóbicas e Hidrofílicas
Movimento
Antígenos O/química
Antígenos O/metabolismo
Pseudomonas syringae/citologia
Pseudomonas syringae/genética
Ramnose/biossíntese
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Aderência Bacteriana
Genes Bacterianos/genética
Açúcares de Guanosina Difosfato/biossíntese
Mutação
Polissacarídeos/análise
Pseudomonas syringae/efeitos dos fármacos
Pseudomonas syringae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (GDP-rhamnose); 0 (Guanosine Diphosphate Sugars); 0 (O Antigens); 0 (Polysaccharides); QN34XC755A (Rhamnose)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130309
[St] Status:MEDLINE


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[PMID]:22282517
[Au] Autor:Ovchinnikova OG; Liu B; Guo D; Kocharova NA; Shashkov AS; Chen M; Feng L; Rozalski A; Knirel YA; Wang L
[Ad] Endereço:TEDA School of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, 300457 Tianjin, PR China.
[Ti] Título:Localization and molecular characterization of putative O antigen gene clusters of Providencia species.
[So] Source:Microbiology;158(Pt 4):1024-36, 2012 Apr.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Enterobacteria of the genus Providencia are opportunistic human pathogens associated with urinary tract and wound infections, as well as enteric diseases. The lipopolysaccharide (LPS) O antigen confers major antigenic variability upon the cell surface and is used for serotyping of Gram-negative bacteria. Recently, Providencia O antigen structures have been extensively studied, but no data on the location and organization of the O antigen gene cluster have been reported. In this study, the four Providencia genome sequences available were analysed, and the putative O antigen gene cluster was identified in the polymorphic locus between the cpxA and yibK genes. This finding provided the necessary information for designing primers, and cloning and sequencing the O antigen gene clusters from five more Providencia alcalifaciens strains. The gene functions predicted in silico were in agreement with the known O antigen structures; furthermore, annotation of the genes involved in the three-step synthesis of GDP-colitose (gmd, colD and colC) was supported by cloning and biochemical characterization of the corresponding enzymes. In one strain (P. alcalifaciens O39), no polysaccharide product of the gene cluster in the cpxA-yibK locus was found, and hence genes for synthesis of the existing O antigen are located elsewhere in the genome. In addition to the putative O antigen synthesis genes, homologues of wza, wzb, wzc and (in three strains) wzi, required for the surface expression of capsular polysaccharides, were found upstream of yibK in all species except Providencia rustigianii, suggesting that the LPS of these species may be attributed to the so-called K LPS (K(LPS)). The data obtained open a way for development of a PCR-based typing method for identification of Providencia isolates.
[Mh] Termos MeSH primário: Família Multigênica
Antígenos O/genética
Providencia/genética
[Mh] Termos MeSH secundário: Clonagem Molecular
DNA Bacteriano/genética
Loci Gênicos
Açúcares de Guanosina Difosfato/biossíntese
Dados de Sequência Molecular
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Guanosine Diphosphate Sugars); 0 (O Antigens); 0 (guanosine diphosphate-colitose)
[Em] Mês de entrada:1208
[Cu] Atualização por classe:120330
[Lr] Data última revisão:
120330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120128
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.055210-0



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