Base de dados : MEDLINE
Pesquisa : D08.811.913.400 [Categoria DeCS]
Referências encontradas : 3465 [refinar]
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[PMID]:29338263
[Au] Autor:Dai L; Li J; Yang J; Zhu Y; Men Y; Zeng Y; Cai Y; Dong C; Dai Z; Zhang X; Sun Y
[Ad] Endereço:National Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences , 32 Xiqi Road, Tianjin Airport Economic Area, Tianjin 300308, China.
[Ti] Título:Use of a Promiscuous Glycosyltransferase from Bacillus subtilis 168 for the Enzymatic Synthesis of Novel Protopanaxatriol-Type Ginsenosides.
[So] Source:J Agric Food Chem;66(4):943-949, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ginsenosides are the principal bioactive ingredients of Panax ginseng and possess diverse notable pharmacological activities. UDP-glycosyltransferase (UGT)-mediated glycosylation of the C6-OH and C20-OH of protopanaxatriol (PPT) is the prominent biological modification that contributes to the immense structural and functional diversity of PPT-type ginsenosides. In this study, the glycosylation of PPT and PPT-type ginsenosides was achieved using a promiscuous glycosyltransferase (Bs-YjiC) from Bacillus subtilis 168. PPT was selected as the probe for the in vitro glycodiversification of PPT-type ginsenosides using diverse UDP-sugars as sugar donors. Structural analysis of the newly biosynthesized products demonstrated that Bs-YjiC can transfer a glucosyl moiety to the free C3-OH, C6-OH, and C12-OH of PPT. Five PPT-type ginsenosides were biosynthesized, including ginsenoside Rh1 and four unnatural ginsenosides. The present study suggests flexible microbial UGTs play an important role in the enzymatic synthesis of novel ginsenosides.
[Mh] Termos MeSH primário: Bacillus subtilis/enzimologia
Ginsenosídeos/biossíntese
Glicosiltransferases/metabolismo
Sapogeninas/metabolismo
[Mh] Termos MeSH secundário: Glicosilação
Açúcares de Uridina Difosfato/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ginsenosides); 0 (Sapogenins); 0 (Uridine Diphosphate Sugars); 34080-08-5 (protopanaxatriol); EC 2.4.- (Glycosyltransferases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b03907


  2 / 3465 MEDLINE  
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[PMID]:29020603
[Au] Autor:Inan C; Muratoglu H; Arif BM; Demirbag Z
[Ad] Endereço:Department of Biology, Faculty of Sciences, Karadeniz Technical University, Trabzon, Turkey; Department of Molecular Biology and Genetics, Faculty of Sciences, Karadeniz Technical University, Trabzon, Turkey.
[Ti] Título:Transcriptional analysis of the putative glycosyltransferase gene (amv248) of the Amsacta moorei entomopoxvirus.
[So] Source:Virus Res;243:25-30, 2018 01 02.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Amsacta moorei entomopoxvirus (AMEV), the most studied member of the genus Betaentomopoxvirus, was initially isolated from Red Hairy caterpillar larvae, Amsacta moorei. According to genome sequence and previous studies it was shown that amv248 encodes a putative glycosyltransferase that is the only conserved attachment protein in betaentomopoxviruses. Transcriptional analysis of the amv248 gene by RT-PCR and qPCR showed that transcription starts at 6h post infection (hpi). Also, transcription was not affected by a DNA replication inhibitor but was severely curtailed by a protein synthesis inhibitor. These results indicate that amv248 belongs to the intermediate class of gene expression. 5' and 3' untranslated regions analysis revealed that transcription initiates at position -126 relative to the translational start site, and ends between 50 and 83 bases after the stop codon. To narrow down the size and location of the gene's promoter, the upstream region as well as several different sized deletions thereof were generated and cloned upstream of a luciferase reporter gene. The constructs were used to measure the Firefly and Renilla luciferase activities in dual assays. The results showed that luciferase activity decreased when bases -198 to -235 of amv248 upstream region were missing. Sequence analysis among the intermediate gene promoters of AMEV showed that TTTAT(T/A)TT(T/A) TTA is possibly a common motif, however, further investigations are needed to confirm this conclusion.
[Mh] Termos MeSH primário: Entomopoxvirinae/enzimologia
Glicosiltransferases/genética
Mariposas/virologia
Transcrição Genética
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Animais
Entomopoxvirinae/classificação
Entomopoxvirinae/genética
Entomopoxvirinae/isolamento & purificação
Glicosiltransferases/metabolismo
Larva/virologia
Regiões Promotoras Genéticas
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Viral Proteins); EC 2.4.- (Glycosyltransferases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE


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[PMID]:27775150
[Au] Autor:Schmölzer K; Lemmerer M; Gutmann A; Nidetzky B
[Ad] Endereço:Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
[Ti] Título:Integrated process design for biocatalytic synthesis by a Leloir Glycosyltransferase: UDP-glucose production with sucrose synthase.
[So] Source:Biotechnol Bioeng;114(4):924-928, 2017 04.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleotide sugar-dependent ("Leloir") glycosyltransferases (GTs), represent a new paradigm for the application of biocatalytic glycosylations to the production of fine chemicals. However, it remains to be shown that GT processes meet the high efficiency targets of industrial biotransformations. We demonstrate in this study of uridine-5'-diphosphate glucose (UDP-glc) production by sucrose synthase (from Acidithiobacillus caldus) that a holistic process design, involving coordinated development of biocatalyst production, biotransformation, and downstream processing (DSP) was vital for target achievement at ∼100 g scale synthesis. Constitutive expression in Escherichia coli shifted the recombinant protein production mainly to the stationary phase and enhanced the specific enzyme activity to a level (∼480 U/g ) suitable for whole-cell biotransformation. The UDP-glc production had excellent performance metrics of ∼100 g /L, 86% yield (based on UDP), and a total turnover number of 103 g /g at a space-time yield of 10 g/L/h. Using efficient chromatography-free DSP, the UDP-glc was isolated in a single batch with ≥90% purity and in 73% isolated yield. Overall, the process would allow production of ∼0.7 kg of isolated product/L E. coli bioreactor culture, thus demonstrating how integrated process design promotes the practical use of a GT conversion. Biotechnol. Bioeng. 2017;114: 924-928. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Glucosiltransferases/metabolismo
Glicosiltransferases/metabolismo
Uridina Difosfato Glucose/análise
Uridina Difosfato Glucose/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Escherichia coli/metabolismo
Glicosilação
Nucleotídeos
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Nucleotides); 0 (Recombinant Proteins); EC 2.4.- (Glycosyltransferases); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.13 (sucrose synthase); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171216
[Lr] Data última revisão:
171216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26204


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[PMID]:28462843
[Au] Autor:Xu Y; Smith R; Vivoli M; Ema M; Goos N; Gehrke S; Harmer NJ; Wagner GK
[Ad] Endereço:King's College London, Department of Chemistry, Faculty of Natural & Mathematical Sciences, Britannia House, 7 Trinity Street, London SE1 1DB, UK.
[Ti] Título:Covalent inhibitors of LgtC: A blueprint for the discovery of non-substrate-like inhibitors for bacterial glycosyltransferases.
[So] Source:Bioorg Med Chem;25(12):3182-3194, 2017 06 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Non-substrate-like inhibitors of glycosyltransferases are sought after as chemical tools and potential lead compounds for medicinal chemistry, chemical biology and drug discovery. Here, we describe the discovery of a novel small molecular inhibitor chemotype for LgtC, a retaining α-1,4-galactosyltransferase involved in bacterial lipooligosaccharide biosynthesis. The new inhibitors, which are structurally unrelated to both the donor and acceptor of LgtC, have low micromolar inhibitory activity, comparable to the best substrate-based inhibitors. We provide experimental evidence that these inhibitors react covalently with LgtC. Results from detailed enzymological experiments with wild-type and mutant LgtC suggest the non-catalytic active site residue Cys246 as a likely target residue for these inhibitors. Analysis of available sequence and structural data reveals that non-catalytic cysteines are a common motif in the active site of many bacterial glycosyltransferases. Our results can therefore serve as a blueprint for the rational design of non-substrate-like, covalent inhibitors against a broad range of other bacterial glycosyltransferases.
[Mh] Termos MeSH primário: Proteínas de Bactérias/antagonistas & inibidores
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Glicosiltransferases/antagonistas & inibidores
Neisseria meningitidis/enzimologia
Pasteurella multocida/enzimologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Domínio Catalítico/efeitos dos fármacos
Bovinos
Descoberta de Drogas
Glicosiltransferases/química
Glicosiltransferases/metabolismo
Seres Humanos
Meningite Meningocócica/tratamento farmacológico
Meningite Meningocócica/microbiologia
Simulação de Acoplamento Molecular
Neisseria meningitidis/química
Infecções por Pasteurella/tratamento farmacológico
Infecções por Pasteurella/microbiologia
Pasteurella multocida/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzyme Inhibitors); EC 2.4.- (Glycosyltransferases); EC 2.4.- (LgtC protein, Neisseria)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171208
[Lr] Data última revisão:
171208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:29020037
[Au] Autor:King R; Urban M; Lauder RP; Hawkins N; Evans M; Plummer A; Halsey K; Lovegrove A; Hammond-Kosack K; Rudd JJ
[Ad] Endereço:Department of Computational and Analytical Sciences, Rothamsted Research, Harpenden, Herts, United Kingdom.
[Ti] Título:A conserved fungal glycosyltransferase facilitates pathogenesis of plants by enabling hyphal growth on solid surfaces.
[So] Source:PLoS Pathog;13(10):e1006672, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pathogenic fungi must extend filamentous hyphae across solid surfaces to cause diseases of plants. However, the full inventory of genes which support this is incomplete and many may be currently concealed due to their essentiality for the hyphal growth form. During a random T-DNA mutagenesis screen performed on the pleomorphic wheat (Triticum aestivum) pathogen Zymoseptoria tritici, we acquired a mutant unable to extend hyphae specifically when on solid surfaces. In contrast "yeast-like" growth, and all other growth forms, were unaffected. The inability to extend surface hyphae resulted in a complete loss of virulence on plants. The affected gene encoded a predicted type 2 glycosyltransferase (ZtGT2). Analysis of >800 genomes from taxonomically diverse fungi highlighted a generally widespread, but discontinuous, distribution of ZtGT2 orthologues, and a complete absence of any similar proteins in non-filamentous ascomycete yeasts. Deletion mutants of the ZtGT2 orthologue in the taxonomically un-related fungus Fusarium graminearum were also severely impaired in hyphal growth and non-pathogenic on wheat ears. ZtGT2 expression increased during filamentous growth and electron microscopy on deletion mutants (ΔZtGT2) suggested the protein functions to maintain the outermost surface of the fungal cell wall. Despite this, adhesion to leaf surfaces was unaffected in ΔZtGT2 mutants and global RNAseq-based gene expression profiling highlighted that surface-sensing and protein secretion was also largely unaffected. However, ΔZtGT2 mutants constitutively overexpressed several transmembrane and secreted proteins, including an important LysM-domain chitin-binding virulence effector, Zt3LysM. ZtGT2 likely functions in the synthesis of a currently unknown, potentially minor but widespread, extracellular or outer cell wall polysaccharide which plays a key role in facilitating many interactions between plants and fungi by enabling hyphal growth on solid matrices.
[Mh] Termos MeSH primário: Fusarium/patogenicidade
Glicosiltransferases/metabolismo
Hifas/crescimento & desenvolvimento
Triticum/microbiologia
Virulência/genética
[Mh] Termos MeSH secundário: DNA Bacteriano/genética
Regulação Fúngica da Expressão Gênica
Glicosiltransferases/genética
Mutação
Filogenia
Doenças das Plantas/microbiologia
Esporos Fúngicos
Triticum/enzimologia
Triticum/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (T-DNA); EC 2.4.- (Glycosyltransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006672


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[PMID]:28867436
[Au] Autor:Chen JJ; Zhang JX; Zhang XQ; Qi MJ; Shi MZ; Yang J; Zhang KZ; Guo C; Han YL
[Ad] Endereço:Department of Pharmacy, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, 600 Yi Shan Road, Shanghai 200233, China.
[Ti] Título:Effects of diosmetin on nine cytochrome P450 isoforms, UGTs and three drug transporters in vitro.
[So] Source:Toxicol Appl Pharmacol;334:1-7, 2017 Nov 01.
[Is] ISSN:1096-0333
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diosmetin (3', 5, 7-trihydroxy-4'-methoxyflavone), a natural flavonoid from traditional Chinese herbs, has been used in various medicinal products because of its anticancer, antimicrobial, antioxidant, estrogenic and anti-inflammatory activity. However, flavonoids could affect the metabolic enzymes and cause drug-drug interactions (DDI), reducing the efficacy of co-administered drugs and potentially resulting in serious adverse reactions. To evaluate its potential to interact with co-administered drugs, the IC value of phase I cytochrome P450 enzymes (CYPs), phase II UDP-glucuronyltransferases (UGTs) and hepatic uptake transporters (organic cation transporters (OCTs), organic anion transporter polypeptides (OATPs) and Na -taurocholate cotransporting polypeptides (NTCPs)) were examined in vitro by LC-MS/MS. Diosmetin showed strong inhibition of CYP1A2 in a concentration-dependent manner. The intensity of the inhibitory effect was followed by CYP2C8, CYP2C9, CYP2C19 and CYP2E1. For CYP2A6, CYP2B6, CYP2D6 and CYP3A4, diosmetin was found to have no significant inhibitory effects, and the induction effect on CYPs was not significant. For UGTs, diosmetin had a minimal inhibitory effect. In addition, the inhibitory effects of diosmetin on OATP and OCT1 were weak, and it had little effect on NTCP. This finding indicated that drug-drug interactions induced by diosmetin may occur through co-administration of drugs metabolized by CYP1A2.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/metabolismo
Flavonoides/química
Flavonoides/farmacologia
Glicosiltransferases/metabolismo
Hepatócitos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte
Sistema Enzimático do Citocromo P-450/genética
Glicosiltransferases/genética
Hepatócitos/metabolismo
Seres Humanos
Isoenzimas
Masculino
Estrutura Molecular
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Flavonoids); 0 (Isoenzymes); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 2.4.- (Glycosyltransferases); TWZ37241OT (diosmetin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


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[PMID]:28860194
[Au] Autor:Scott NE; Giogha C; Pollock GL; Kennedy CL; Webb AI; Williamson NA; Pearson JS; Hartland EL
[Ad] Endereço:From the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia, nichollas.scott@unimelb.edu.au.
[Ti] Título:The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD).
[So] Source:J Biol Chem;292(42):17337-17350, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The inhibition of host innate immunity pathways is essential for the persistence of attaching and effacing pathogens such as enteropathogenic (EPEC) and during mammalian infections. To subvert these pathways and suppress the antimicrobial response, attaching and effacing pathogens use type III secretion systems to introduce effectors targeting key signaling pathways in host cells. One such effector is the arginine glycosyltransferase NleB1 (NleB in ) that modifies conserved arginine residues in death domain-containing host proteins with -acetylglucosamine (GlcNAc), thereby blocking extrinsic apoptosis signaling. Ectopically expressed NleB1 modifies the host proteins Fas-associated via death domain (FADD), TNFRSF1A-associated via death domain (TRADD), and receptor-interacting serine/threonine protein kinase 1 (RIPK1). However, the full repertoire of arginine GlcNAcylation induced by pathogen-delivered NleB1 is unknown. Using an affinity proteomic approach for measuring arginine-GlcNAcylated glycopeptides, we assessed the global profile of arginine GlcNAcylation during ectopic expression of NleB1, EPEC infection , or infection NleB overexpression resulted in arginine GlcNAcylation of multiple host proteins. However, NleB delivery during EPEC and infection caused rapid and preferential modification of Arg in FADD. This FADD modification was extremely stable and insensitive to physiological temperatures, glycosidases, or host cell degradation. Despite its stability and effect on the inhibition of apoptosis, arginine GlcNAcylation did not elicit any proteomic changes, even in response to prolonged NleB1 expression. We conclude that, at normal levels of expression during bacterial infection, NleB1/NleB antagonizes death receptor-induced apoptosis of infected cells by modifying FADD in an irreversible manner.
[Mh] Termos MeSH primário: Apoptose
Citrobacter rodentium/enzimologia
Escherichia coli Enteropatogênica/enzimologia
Infecções por Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Proteína de Domínio de Morte Associada a Fas/metabolismo
Glicosiltransferases/metabolismo
Processamento de Proteína Pós-Traducional
Fatores de Virulência/metabolismo
[Mh] Termos MeSH secundário: Citrobacter rodentium/patogenicidade
Escherichia coli Enteropatogênica/patogenicidade
Infecções por Escherichia coli/genética
Infecções por Escherichia coli/patologia
Proteínas de Escherichia coli/genética
Proteína de Domínio de Morte Associada a Fas/genética
Glicosiltransferases/genética
Células HeLa
Seres Humanos
Estabilidade Proteica
Proteína Serina-Treonina Quinases de Interação com Receptores/genética
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Proteína de Domínio de Morte Associada a Receptor de TNF/genética
Proteína de Domínio de Morte Associada a Receptor de TNF/metabolismo
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (FADD protein, human); 0 (Fas-Associated Death Domain Protein); 0 (NleB protein, E coli); 0 (TNF Receptor-Associated Death Domain Protein); 0 (Virulence Factors); EC 2.4.- (Glycosyltransferases); EC 2.7.11.1 (RIPK1 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.805036


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[PMID]:28844388
[Au] Autor:Zhu H; Wu Z; Gadi MR; Wang S; Guo Y; Edmunds G; Guan W; Fang J
[Ad] Endereço:National Glycoengineering Research Center, Shandong Provincial Key Laboratory of Glycochemistry and Glycobiology, Shandong University, Jinan, Shandong 250100, China; Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
[Ti] Título:Cation exchange assisted binding-elution strategy for enzymatic synthesis of human milk oligosaccharides (HMOs).
[So] Source:Bioorg Med Chem Lett;27(18):4285-4287, 2017 09 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A cation exchange assisted binding-elution (BE) strategy for enzymatic synthesis of human milk oligosaccharides (HMOs) was developed. An amino linker was used to provide the cation ion under acidic condition which can be readily bound to cation exchange resin and then eluted off by saturated ammonium bicarbonate. Ammonium bicarbonate in the collections was easily removed by vacuum evaporation. This strategy circumvented the incompatible issue between glycosyltransferases and solid support or large polymers, and no purification was needed for intermediate products. With current approach, polyLacNAc backbones of HMOs and fucosylated HMOs were synthesized smoothly.
[Mh] Termos MeSH primário: Glicosiltransferases/metabolismo
Leite Humano/química
Oligossacarídeos/biossíntese
[Mh] Termos MeSH secundário: Bicarbonatos/química
Bicarbonatos/metabolismo
Cátions/química
Cátions/metabolismo
Relação Dose-Resposta a Droga
Glicosiltransferases/química
Seres Humanos
Leite Humano/metabolismo
Estrutura Molecular
Oligossacarídeos/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bicarbonates); 0 (Cations); 0 (Oligosaccharides); 45JP4345C9 (ammonium bicarbonate); EC 2.4.- (Glycosyltransferases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


  9 / 3465 MEDLINE  
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[PMID]:28809486
[Au] Autor:Elharar Y; Podilapu AR; Guan Z; Kulkarni SS; Eichler J
[Ad] Endereço:Department of Life Sciences, Ben Gurion University of the Negev , Beersheva 8410501, Israel.
[Ti] Título:Assembling Glycan-Charged Dolichol Phosphates: Chemoenzymatic Synthesis of a Haloferax volcanii N-Glycosylation Pathway Intermediate.
[So] Source:Bioconjug Chem;28(9):2461-2470, 2017 Sep 20.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-glycosylation, the covalent attachment of glycans to select protein target Asn residues, is a post-translational modification performed by all three domains of life. In the halophilic archaea Haloferax volcanii, in which understanding of this universal protein-processing event is relatively well-advanced, genes encoding the components of the archaeal glycosylation (Agl) pathway responsible for the assembly and attachment of an N-linked pentasaccharide have been identified. As elsewhere, the N-linked glycan is assembled on phosphodolichol carriers before transfer to target Asn residues. However, as little is presently known of the Hfx. volcanii Agl pathway at the protein level, the seemingly unique ability of Archaea to use dolichol phosphate (DolP) as the glycan lipid carrier, rather than dolichol pyrophosphate used by eukaryotes, remains poorly understood. With this in mind, a chemoenzymatic approach was taken to biochemically study AglG, one of the five glycosyltransferases of the pathway. Accordingly, a novel regio- and stereoselective reduction of naturally isolated polyprenol gave facile access to S-dolichol via asymmetric transfer hydrogenation under very mild conditions. This compound was used to generate glucose-charged DolP, a precursor of the N-linked pentasaccharide, as well as DolP-glucose-glucuronic acid and DolP-glucuronic acid. AglG, purified from Hfx. volcanii membranes in hypersaline conditions, like those encountered in situ, was subsequently combined with uridine diphosphate (UDP)-glucuronic acid and DolP-glucose to yield DolP-glucose-glucuronic acid. The in vitro system for the study of AglG activity developed here represents the first such tool for studying halophilic glycosyltransferases and will allow for a detailed understanding of archaeal N-glycosylation.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Fosfatos de Dolicol/metabolismo
Glicosiltransferases/metabolismo
Haloferax volcanii/metabolismo
Polissacarídeos/metabolismo
[Mh] Termos MeSH secundário: Glicosilação
Oligossacarídeos/metabolismo
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Dolichol Phosphates); 0 (Oligosaccharides); 0 (Polysaccharides); EC 2.4.- (Glycosyltransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00436


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[PMID]:28796424
[Au] Autor:Görl J; Possiel C; Sotriffer C; Seibel J
[Ad] Endereço:Department of Organic Chemistry, Universität Würzburg, Am Hubland, 97074, Würzburg, Germany.
[Ti] Título:Extending the Scope of GTFR Glucosylation Reactions with Tosylated Substrates for Rare Sugars Synthesis.
[So] Source:Chembiochem;18(20):2012-2015, 2017 Oct 18.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Functionalized rare sugars were synthesized with 2-, 3-, and 6-tosylated glucose derivatives as acceptor substrates by transglucosylation with sucrose and the glucansucrase GTFR from Streptococcus oralis. The 2- and 3-tosylated glucose derivatives yielded the corresponding 1,6-linked disaccharides (isomaltose analogues), whereas the 6-tosylated glucose derivatives resulted in 1,3-linked disaccharides (nigerose analogue) with high regioselectivity in up to 95 % yield. Docking studies provided insight into the binding mode of the acceptors and suggested two different orientations that were responsible for the change in regioselectivity.
[Mh] Termos MeSH primário: Glucose/síntese química
Glicosiltransferases/metabolismo
[Mh] Termos MeSH secundário: Técnicas de Química Sintética
Glucose/química
Glucose/metabolismo
Glicosilação
Glicosiltransferases/química
Simulação de Acoplamento Molecular
Conformação Proteica
Streptococcus oralis/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.4.- (Glycosyltransferases); EC 2.4.1.140 (alternansucrase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700320



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