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[PMID]:24412338
[Au] Autor:Li T; Wen L; Williams A; Wu B; Li L; Qu J; Meisner J; Xiao Z; Fang J; Wang PG
[Ad] Endereço:Department of Chemistry, Center for Therapeutics and Diagnostics, Georgia State University, Atlanta, GA 30303, USA.
[Ti] Título:Chemoenzymatic synthesis of ADP-d-glycero-ß-d-manno-heptose and study of the substrate specificity of HldE.
[So] Source:Bioorg Med Chem;22(3):1139-47, 2014 Feb 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-d-glycero-ß-d-manno-heptose (ADP-d, d-heptose) was reported using chemically synthesized d, d-heptose-7-phosphate and the ADP-d, d-heptose biosynthetic enzymes HldE and GmhB. Moreover, the result of investigating substrate specificity of the kinase action of HldE revealed that HldE had highly restricted substrate specificity towards structurally modified heptose-7-phosphate analogs.
[Mh] Termos MeSH primário: Açúcares de Adenosina Difosfato/síntese química
Complexos Multienzimáticos/metabolismo
Nucleotidiltransferases/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
[Mh] Termos MeSH secundário: Açúcares de Adenosina Difosfato/metabolismo
Técnicas de Química Sintética
Especificidade por Substrato
Fosfatos Açúcares/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Multienzyme Complexes); 0 (Sugar Phosphates); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.7.- (Nucleotidyltransferases); EC 3.1.3.- (D,D heptose 7-phosphate kinase-D,D-heptose 1-phosphate adenylyltransferase, E coli)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140114
[St] Status:MEDLINE


  2 / 97 MEDLINE  
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[PMID]:20506248
[Au] Autor:Kowatz T; Morrison JP; Tanner ME; Naismith JH
[Ad] Endereço:Biomolecular Sciences Research Complex, The University of St Andrews, Fife KY16 9RH, United Kingdom.
[Ti] Título:The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism.
[So] Source:Protein Sci;19(7):1337-43, 2010 Jul.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteria synthesize a wide array of unusual carbohydrate molecules, which they use in a variety of ways. The carbohydrate L-glycero-D-manno-heptose is an important component of lipopolysaccharide and is synthesized in a complex series of enzymatic steps. One step involves the epimerization at the C6'' position converting ADP-D-glycero-D-manno-heptose into ADP-L-glycero-D-manno-heptose. The enzyme responsible is a member of the short chain dehydrogenase superfamily, known as ADP-L-glycero-D-manno-heptose 6-epimerase (AGME). The structure of the enzyme was known but the arrangement of the catalytic site with respect to the substrate is unclear. We now report the structure of AGME bound to a substrate mimic, ADP-beta-D-mannose, which has the same stereochemical configuration as the substrate. The complex identifies the key residues and allows mechanistic insight into this novel enzyme.
[Mh] Termos MeSH primário: Açúcares de Adenosina Difosfato/metabolismo
Carboidratos Epimerases/química
Carboidratos Epimerases/metabolismo
Cristalografia por Raios X/métodos
[Mh] Termos MeSH secundário: Sítios de Ligação/genética
Carboidratos Epimerases/genética
Domínio Catalítico/genética
Heptoses/metabolismo
Mutação
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Heptoses); 0 (adenosine diphosphate-mannose); 4305-74-2 (glycero-manno-heptose); EC 5.1.3.- (ADP-L-glycero-D-mannoheptose-6-epimerase); EC 5.1.3.- (Carbohydrate Epimerases)
[Em] Mês de entrada:1009
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100528
[St] Status:MEDLINE
[do] DOI:10.1002/pro.410


  3 / 97 MEDLINE  
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[PMID]:18778276
[Au] Autor:Morán-Zorzano MT; Montero M; Muñoz FJ; Alonso-Casajús N; Viale AM; Eydallin G; Sesma MT; Baroja-Fernández E; Pozueta-Romero J
[Ti] Título:Cytoplasmic Escherichia coli ADP sugar pyrophosphatase binds to cell membranes in response to extracellular signals as the cell population density increases.
[So] Source:FEMS Microbiol Lett;288(1):25-32, 2008 Nov.
[Is] ISSN:0378-1097
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:ADP sugar pyrophosphatase (AspP) is a member of the 'Nudix' (Nucleoside diphosphate linked to some other moiety X) hydrolase family of enzymes that catalyzes the hydrolytic breakdown of ADP-glucose (ADPG) linked to glycogen biosynthesis. In a previous work, we showed that AspP activity is strongly enhanced by both glucose-1,6-bisphosphate and nucleotide-sugars, and by macromolecular crowding. In this work, we show that AspP binds to cell membranes as the bacterial population density increases, c. 30% of the total enzyme remaining membrane associated as glycogen depletes during the stationary phase. This process is not dependent on the stationary transcription factor RpoS, the producer of the bacterial quorum-sensing autoinducer 2 (LuxS), the presence of glycogen granules or glucose availability, but is stimulated by small soluble heat-labile molecule(s) occurring in cell-free spent supernatants of stationary cultures that are acid stabile and base labile. These data further point to AspP as a highly regulated enzyme, and provide a first set of evidences indicating that glycogen metabolism is subjected to regulation by intercellular communication in Escherichia coli.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Escherichia coli/enzimologia
Escherichia coli/crescimento & desenvolvimento
Espaço Extracelular/metabolismo
Pirofosfatases/metabolismo
[Mh] Termos MeSH secundário: Açúcares de Adenosina Difosfato/metabolismo
Proteínas de Bactérias/genética
Membrana Celular/enzimologia
Membrana Celular/genética
Citoplasma/enzimologia
Citoplasma/genética
Escherichia coli/citologia
Escherichia coli/genética
Espaço Extracelular/genética
Regulação Enzimológica da Expressão Gênica
Ligação Proteica
Transporte Proteico
Pirofosfatases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Bacterial Proteins); EC 3.6.1.- (Pyrophosphatases); EC 3.6.1.13 (ADPribose pyrophosphatase)
[Em] Mês de entrada:0902
[Cu] Atualização por classe:081231
[Lr] Data última revisão:
081231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080910
[St] Status:MEDLINE
[do] DOI:10.1111/j.1574-6968.2008.01319.x


  4 / 97 MEDLINE  
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[PMID]:17455913
[Au] Autor:Mayer A; Tanner ME
[Ad] Endereço:Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z1.
[Ti] Título:Intermediate release by ADP-L-glycero-D-manno-heptose 6-epimerase.
[So] Source:Biochemistry;46(20):6149-55, 2007 May 22.
[Is] ISSN:0006-2960
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ADP-l-glycero-d-manno-heptose 6-epimerase (HldD or AGME, formerly RfaD) catalyzes the interconversion of ADP-beta-d-glycero-d-manno-heptose (ADP-d,d-Hep) and ADP-beta-l-glycero-d-manno-heptose (ADP-l,d-Hep). The latter compound provides the heptose moiety that is used in lipopolysaccharide biosynthesis by Gram-negative bacteria. Several lines of evidence suggest that the enzyme uses a direct oxidation/reduction mechanism involving a tightly bound NADP+ cofactor. An initial oxidation at C-6'' gives a 6''-keto intermediate, and a subsequent reduction on the opposite face of the carbonyl group generates the epimeric product. The reorientation required for the nonstereoselective reduction could take place within a single active site, or it could involve the release of the intermediate and rebinding in an altered conformation. To distinguish between these possibilities, two isotopically labeled substrates (ADP-d,d-Hep) were prepared that contained 18O and 2H isotopes at C-7'' and C-6'', respectively. A crossover experiment was used to determine whether unlabeled or doubly labeled products were formed upon epimerization of a mixture of the two singly labeled compounds. After an initial epimeric equilibrium was reached, no crossover could be detected, indicating that intermediate release is not intrinsic to the overall mechanism. After extended incubation, however, scrambling of the labels could be detected, indicating that a low background rate of intermediate release does occur. To directly detect the release of the intermediate, the labeled compounds were independently epimerized in the presence of a ketone-trapping reagent, phenylhydrazine. The corresponding phenylhydrazones were identified by mass spectrometry, and the absence of any 2H isotope in the adduct obtained from the deuterated starting compound confirmed that the oxidation had occurred at C-6''.
[Mh] Termos MeSH primário: Carboidratos Epimerases/química
Carboidratos Epimerases/metabolismo
Escherichia coli K12/enzimologia
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
[Mh] Termos MeSH secundário: Açúcares de Adenosina Difosfato/química
Açúcares de Adenosina Difosfato/metabolismo
Catálise
Medição da Troca de Deutério
Hidrogênio/metabolismo
NADP/metabolismo
Isótopos de Oxigênio/metabolismo
Conformação Proteica
Soluções
Espectrometria de Massas por Ionização por Electrospray
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Escherichia coli Proteins); 0 (Oxygen Isotopes); 0 (Solutions); 53-59-8 (NADP); 7YNJ3PO35Z (Hydrogen); 80186-87-4 (adenosine 5'-diphosphate-glycero-mannoheptose); EC 5.1.3.- (ADP-L-glycero-D-mannoheptose-6-epimerase); EC 5.1.3.- (Carbohydrate Epimerases)
[Em] Mês de entrada:0707
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070426
[St] Status:MEDLINE


  5 / 97 MEDLINE  
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[PMID]:17316025
[Au] Autor:Morrison JP; Tanner ME
[Ad] Endereço:Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z1.
[Ti] Título:A two-base mechanism for Escherichia coli ADP-L-glycero-D-manno-heptose 6-epimerase.
[So] Source:Biochemistry;46(12):3916-24, 2007 Mar 27.
[Is] ISSN:0006-2960
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ADP-l-glycero-d-manno-heptose 6-epimerase (HldD or AGME, formerly RfaD) catalyzes the inversion of configuration at C-6' ' of the heptose moiety of ADP-d-glycero-d-manno-heptose and ADP-l-glycero-d-manno-heptose. The epimerase HldD operates in the biosynthetic pathway of l-glycero-d-manno-heptose, which is a conserved sugar in the core region of lipopolysaccharide (LPS) of Gram-negative bacteria. Previous studies support a mechanism in which HldD uses its tightly bound NADP+ cofactor to oxidize directly at C-6' ', generating a ketone intermediate. A reduction of the ketone from the opposite face then occurs, generating the epimeric product. How the epimerase is able access both faces of the ketone intermediate with correct alignment of the three required components, NADPH, the ketone carbonyl, and a catalytic acid/base residue, is addressed here. It is proposed that the epimerase active site contains two catalytic pockets, each of which bears a catalytic acid/base residue that facilitates reduction of the C-6' ' ketone but leads to a distinct epimeric product. The ketone carbonyl may access either pocket via rotation about the C-5' '-C-6' ' bond of the sugar nucleotide and in doing so presents opposing faces to the bound cofactor. Evidence in support of the two-base mechanism is found in studies of two single mutants of the Escherichia coli K-12 epimerase, Y140F and K178M, both of which have severely compromised epimerase activities that are more than 3 orders of magnitude lower than that of the wild type. The catalytic competency of these two mutants in promoting redox chemistry is demonstrated with an alternate catalytic activity that requires only one catalytic base: dismutation of a C-6' ' aldehyde substrate analogue (ADP-beta-d-manno-hexodialdose) to an acid and an alcohol (ADP-beta-d-mannuronic acid and ADP-beta-d-mannose). This study identifies the two catalytic bases as tyrosine 140 and lysine 178. A one-step enzymatic conversion of mannose into ADP-beta-mannose is also described and used to make C-6' '-substituted derivatives of this sugar nucleotide.
[Mh] Termos MeSH primário: Carboidratos Epimerases/metabolismo
Escherichia coli K12/enzimologia
Proteínas de Escherichia coli/metabolismo
Lipopolissacarídeos/biossíntese
Modelos Químicos
[Mh] Termos MeSH secundário: Açúcares de Adenosina Difosfato/metabolismo
Substituição de Aminoácidos
Sítios de Ligação/genética
Carboidratos Epimerases/genética
Escherichia coli K12/genética
Proteínas de Escherichia coli/genética
Manose/metabolismo
Mutação de Sentido Incorreto
NADP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Escherichia coli Proteins); 0 (Lipopolysaccharides); 0 (adenosine diphosphate-mannose); 53-59-8 (NADP); EC 5.1.3.- (ADP-L-glycero-D-mannoheptose-6-epimerase); EC 5.1.3.- (Carbohydrate Epimerases); PHA4727WTP (Mannose)
[Em] Mês de entrada:0705
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070224
[St] Status:MEDLINE


  6 / 97 MEDLINE  
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[PMID]:17306798
[Au] Autor:Morán-Zorzano MT; Viale AM; Muñoz FJ; Alonso-Casajús N; Eydallín GG; Zugasti B; Baroja-Fernández E; Pozueta-Romero J
[Ad] Endereço:Instituto de Agrobiotecnología, Universidad Pública de Navarra/Gobierno de Navarra/Consejo Superior de Investigaciones Científicas, Carretera de Mutilva s/n, 31192 Mutilva Baja, Navarra, Spain.
[Ti] Título:Escherichia coli AspP activity is enhanced by macromolecular crowding and by both glucose-1,6-bisphosphate and nucleotide-sugars.
[So] Source:FEBS Lett;581(5):1035-40, 2007 Mar 06.
[Is] ISSN:0014-5793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Escherichia coli ADP-sugar pyrophosphatase (AspP) is a "Nudix" hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to glycogen biosynthesis. Moderate increases of AspP activity in the cell are accompanied by significant reductions of the glycogen content. In vitro analyses showed that AspP activity is strongly enhanced by macromolecular crowding and by both glucose-1,6-bisphosphate and nucleotide-sugars, providing a first set of indicative evidences that AspP is a highly regulated enzyme. To our knowledge, AspP is the sole bacterial enzyme described to date which is activated by both G1,6P(2) and nucleotide-sugars.
[Mh] Termos MeSH primário: Escherichia coli/enzimologia
Glucose-6-Fosfato/análogos & derivados
Açúcares de Nucleosídeo Difosfato/farmacologia
Pirofosfatases/metabolismo
[Mh] Termos MeSH secundário: Açúcares de Adenosina Difosfato/metabolismo
Açúcares de Adenosina Difosfato/farmacologia
Ativação Enzimática/efeitos dos fármacos
Escherichia coli/efeitos dos fármacos
Escherichia coli/metabolismo
Glucose-6-Fosfato/farmacologia
Glicogênio/metabolismo
Cinética
Substâncias Macromoleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Macromolecular Substances); 0 (Nucleoside Diphosphate Sugars); 0 (glucose-1,6-bisphosphate); 56-73-5 (Glucose-6-Phosphate); 9005-79-2 (Glycogen); EC 3.6.1.- (Pyrophosphatases)
[Em] Mês de entrada:0704
[Cu] Atualização por classe:070227
[Lr] Data última revisão:
070227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070220
[St] Status:MEDLINE


  7 / 97 MEDLINE  
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[PMID]:16632256
[Au] Autor:De Leon GP; Elowe NH; Koteva KP; Valvano MA; Wright GD
[Ad] Endereço:Antimicrobial Research Centre, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.
[Ti] Título:An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis.
[So] Source:Chem Biol;13(4):437-41, 2006 Apr.
[Is] ISSN:1074-5521
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The lipopolysaccharide (LPS)-rich outer membrane of gram-negative bacteria provides a protective barrier that insulates these organisms from the action of numerous antibiotics. Breach of the LPS layer can therefore provide access to the cell interior to otherwise impermeant toxic molecules and can expose vulnerable binding sites for immune system components such as complement. Inhibition of LPS biosynthesis, leading to a truncated LPS molecule, is an alternative strategy for antibacterial drug development in which this vital cellular structure is weakened. A significant challenge for in vitro screens of small molecules for inhibition of LPS biosynthesis is the difficulty in accessing the complex carbohydrate substrates. We have optimized an assay of the enzymes required for LPS heptose biosynthesis that simultaneously surveys five enzyme activities by using commercially available substrates and report its use in a small-molecule screen that identifies an inhibitor of heptose synthesis.
[Mh] Termos MeSH primário: Açúcares de Adenosina Difosfato/biossíntese
Inibidores Enzimáticos/farmacologia
Glicosiltransferases/antagonistas & inibidores
Lipopolissacarídeos/biossíntese
[Mh] Termos MeSH secundário: Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Avaliação Pré-Clínica de Medicamentos
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Escherichia coli/metabolismo
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Negativas/enzimologia
Bactérias Gram-Negativas/metabolismo
Cinética
Testes de Sensibilidade Microbiana
Complexos Multienzimáticos/antagonistas & inibidores
Nucleotidiltransferases/antagonistas & inibidores
Fosfotransferases (Aceptor do Grupo Álcool)/antagonistas & inibidores
Proteínas Recombinantes/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Enzyme Inhibitors); 0 (Lipopolysaccharides); 0 (Multienzyme Complexes); 0 (Recombinant Proteins); EC 2.4.- (Glycosyltransferases); EC 2.4.99.- (heptosyltransferase); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.7.- (Nucleotidyltransferases); EC 3.1.3.- (D,D heptose 7-phosphate kinase-D,D-heptose 1-phosphate adenylyltransferase, E coli)
[Em] Mês de entrada:0607
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:060425
[St] Status:MEDLINE


  8 / 97 MEDLINE  
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[PMID]:15932222
[Au] Autor:Read JA; Ahmed RA; Tanner ME
[Ad] Endereço:Department of Chemistry, University of British Columbia, Vancouver, BC, Canada.
[Ti] Título:Efficient chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose and a mechanistic study of ADP-L-glycero-D-manno-heptose 6-epimerase.
[So] Source:Org Lett;7(12):2457-60, 2005 Jun 09.
[Is] ISSN:1523-7060
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:[reaction: see text] A chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose (ADP-D,D-Hep) is described in which D,D-Hep 7-phosphate is converted to ADP-D,D-Hep by two biosynthetic enzymes. This strategy allows access to the 6''-deuterated analogue, which upon incubation with the epimerase showed complete retention of the isotopic label at the 6''-position. This provides evidence for a direct oxidation mechanism in which the hydride initially transferred to the NADP+ cofactor is subsequently returned to the same carbon in a nonstereospecific manner.
[Mh] Termos MeSH primário: Açúcares de Adenosina Difosfato/síntese química
Carboidratos Epimerases/química
Carboidratos Epimerases/metabolismo
[Mh] Termos MeSH secundário: Estrutura Molecular
NADP/metabolismo
Oxirredução
Fosfatos/metabolismo
Estereoisomerismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Phosphates); 53-59-8 (NADP); 80186-87-4 (adenosine 5'-diphosphate-glycero-mannoheptose); EC 5.1.3.- (ADP-L-glycero-D-mannoheptose-6-epimerase); EC 5.1.3.- (Carbohydrate Epimerases)
[Em] Mês de entrada:0603
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:050604
[St] Status:MEDLINE


  9 / 97 MEDLINE  
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[PMID]:15519322
[Au] Autor:Khaled A; Ivannikova T; Augé C
[Ad] Endereço:Laboratoire de Chimie Organique Multifonctionnelle, UMR 8614, GDR 2590, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), Université Paris-Sud, Bât 420, F-91405 Orsay, France.
[Ti] Título:Synthesis of unnatural sugar nucleotides and their evaluation as donor substrates in glycosyltransferase-catalyzed reactions.
[So] Source:Carbohydr Res;339(16):2641-9, 2004 Nov 15.
[Is] ISSN:0008-6215
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:New unnatural sugar nucleotides, UDP-Fuc and CDP-Fuc were synthesized from fucose-beta-1-phosphate and nucleotide monophosphates activated as morpholidates. Furthermore, a nucleotide analogue was prepared by phosphorylation of 1-(beta-D-ribofuranosyl)cyanuric acid, itself obtained as a protected derivative by condensation of the persilylated derivative of cyanuric acid with 1-O-acetyl-2,3,5-tri-O-benzoyl-beta-D-ribofuranose in 74% yield. This phosphate activated according to the same procedure was condensed with fucose-beta-1-phosphate, affording a new sugar nucleotide conjugate (NDP-Fuc) which was evaluated together with UDP-Fuc, CDP-Fuc and ADP-Fuc, as fucose donors in alpha-(1-->4/3)-fucosyltransferase (FucT-III) catalyzed reaction. Fucose transfer could be observed with each of the donors and kinetic parameters were determined using a fluorescent acceptor substrate. Efficiency of the four analogues towards FucT-III was in the following order: UDP-Fuc=ADP-Fuc>NDP-Fuc>CDP-Fuc. According to the same strategy ADP-GlcNAc was prepared from AMP-morpholidate and N-acetylglucosamine-alpha-1-phosphate; tested as a glucosaminyl donor towards Neisseria meningitidis N-acetylglucosaminyl transferase (LgtA), ADP-GlcNAc was recognized with 0.1% efficiency as compared with UDP-GlcNAc, the natural donor substrate.
[Mh] Termos MeSH primário: Glicosiltransferases/metabolismo
Açúcares de Nucleosídeo Difosfato/síntese química
[Mh] Termos MeSH secundário: Açúcares de Adenosina Difosfato/síntese química
Açúcares de Adenosina Difosfato/metabolismo
Proteínas de Bactérias/metabolismo
Catálise
Fucosiltransferases/metabolismo
Cinética
N-Acetilglucosaminiltransferases/metabolismo
Açúcares de Nucleosídeo Difosfato/metabolismo
Relação Estrutura-Atividade
Especificidade por Substrato
Açúcares de Uridina Difosfato/síntese química
Açúcares de Uridina Difosfato/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Bacterial Proteins); 0 (Nucleoside Diphosphate Sugars); 0 (Uridine Diphosphate Sugars); EC 2.4.- (Glycosyltransferases); EC 2.4.1.- (Fucosyltransferases); EC 2.4.1.- (LgtA protein, bacteria); EC 2.4.1.- (N-Acetylglucosaminyltransferases); EC 2.4.1.65 (3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase)
[Em] Mês de entrada:0504
[Cu] Atualização por classe:080815
[Lr] Data última revisão:
080815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:041103
[St] Status:MEDLINE


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[PMID]:11751812
[Au] Autor:Kneidinger B; Marolda C; Graninger M; Zamyatina A; McArthur F; Kosma P; Valvano MA; Messner P
[Ad] Endereço:Zentrum für Ultrastrukturforschung und Ludwig Boltzmann-Institut für Molekulare Nanotechnologie, A-1180 Vienna, Austria.
[Ti] Título:Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli.
[So] Source:J Bacteriol;184(2):363-9, 2002 Jan.
[Is] ISSN:0021-9193
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The steps involved in the biosynthesis of the ADP-L-glycero-beta-D-manno-heptose (ADP-L-beta-D-heptose) precursor of the inner core lipopolysaccharide (LPS) have not been completely elucidated. In this work, we have purified the enzymes involved in catalyzing the intermediate steps leading to the synthesis of ADP-D-beta-D-heptose and have biochemically characterized the reaction products by high-performance anion-exchange chromatography. We have also constructed a deletion in a novel gene, gmhB (formerly yaeD), which results in the formation of an altered LPS core. This mutation confirms that the GmhB protein is required for the formation of ADP-D-beta-D-heptose. Our results demonstrate that the synthesis of ADP-D-beta-D-heptose in Escherichia coli requires three proteins, GmhA (sedoheptulose 7-phosphate isomerase), HldE (bifunctional D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase), and GmhB (D,D-heptose 1,7-bisphosphate phosphatase), as well as ATP and the ketose phosphate precursor sedoheptulose 7-phosphate. A previously characterized epimerase, formerly named WaaD (RfaD) and now renamed HldD, completes the pathway to form the ADP-L-beta-D-heptose precursor utilized in the assembly of inner core LPS.
[Mh] Termos MeSH primário: Açúcares de Adenosina Difosfato/biossíntese
Proteínas de Escherichia coli
Escherichia coli/enzimologia
Isomerases/metabolismo
Complexos Multienzimáticos/metabolismo
Nucleotidiltransferases/metabolismo
Fosfoproteínas Fosfatases/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Racemases e Epimerases/metabolismo
[Mh] Termos MeSH secundário: Escherichia coli/genética
Expressão Gênica
Isomerases/genética
Lipopolissacarídeos
Complexos Multienzimáticos/classificação
Nucleotidiltransferases/classificação
Fenótipo
Fosfoproteínas Fosfatases/classificação
Fosfoproteínas Fosfatases/genética
Monoéster Fosfórico Hidrolases/classificação
Monoéster Fosfórico Hidrolases/genética
Fosfotransferases (Aceptor do Grupo Álcool)/classificação
Proteínas Quinases/metabolismo
Racemases e Epimerases/classificação
Terminologia como Assunto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenosine Diphosphate Sugars); 0 (Escherichia coli Proteins); 0 (Lipopolysaccharides); 0 (Multienzyme Complexes); 80186-87-4 (adenosine 5'-diphosphate-glycero-mannoheptose); EC 2.7.- (Protein Kinases); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.7.- (Nucleotidyltransferases); EC 3.1.3.- (D,D heptose 7-phosphate kinase-D,D-heptose 1-phosphate adenylyltransferase, E coli); EC 3.1.3.- (D,D-heptose 1,7-bisphosphate phosphatase, E coli); EC 3.1.3.16 (Phosphoprotein Phosphatases); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 5.- (Isomerases); EC 5.1.- (Racemases and Epimerases); EC 5.1.3.- (GmhA protein, E coli)
[Em] Mês de entrada:0201
[Cu] Atualização por classe:170219
[Lr] Data última revisão:
170219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:011226
[St] Status:MEDLINE



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