Base de dados : MEDLINE
Pesquisa : D08.811.682.664 [Categoria DeCS]
Referências encontradas : 29 [refinar]
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  1 / 29 MEDLINE  
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[PMID]:28080034
[Au] Autor:Fitzpatrick PF; Chadegani F; Zhang S; Dougherty V
[Ad] Endereço:Department of Biochemistry and Structural Biology, University of Texas Health Science Center , San Antonio, Texas 78229, United States.
[Ti] Título:Mechanism of Flavoprotein l-6-Hydroxynicotine Oxidase: pH and Solvent Isotope Effects and Identification of Key Active Site Residues.
[So] Source:Biochemistry;56(6):869-875, 2017 Feb 14.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The flavoenzyme l-6-hydroxynicotine oxidase is a member of the monoamine oxidase family that catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine. While the enzyme has long been understood to catalyze oxidation of the carbon-carbon bond, it has recently been shown to catalyze oxidation of a carbon-nitrogen bond [Fitzpatrick, P. F., et al. (2016) Biochemistry 55, 697-703]. The effects of pH and mutagenesis of active site residues have now been utilized to study the mechanism and roles of active site residues. Asn166 and Tyr311 bind the substrate, while Lys287 forms a water-mediated hydrogen bond with flavin N5. The N166A and Y311F mutations result in ∼30- and ∼4-fold decreases in k /K and k for (S)-6-hydroxynicotine, respectively, with larger effects on the k /K value for (S)-6-hydroxynornicotine. The K287M mutation results in ∼10-fold decreases in these parameters and a 6000-fold decrease in the k /K value for oxygen. The shapes of the pH profiles are not altered by the N166A and Y311F mutations. There is no solvent isotope effect on the k /K value for amines. The results are consistent with a model in which both the charged and neutral forms of the amine can bind, with the former rapidly losing a proton to a hydrogen bond network of water and amino acids in the active site prior to the transfer of hydride to the flavin.
[Mh] Termos MeSH primário: Arthrobacter/enzimologia
Proteínas de Bactérias/metabolismo
Flavoproteínas/metabolismo
Modelos Moleculares
Nicotina/análogos & derivados
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/metabolismo
Flavoproteínas/química
Flavoproteínas/genética
Ligações de Hidrogênio
Concentração de Íons de Hidrogênio
Hidrólise
Lisina/química
Mutagênese Sítio-Dirigida
Mutação
Nicotina/química
Nicotina/metabolismo
Ressonância Magnética Nuclear Biomolecular
Oxirredução
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/química
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solventes/química
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-hydroxynicotine); 0 (Bacterial Proteins); 0 (Flavoproteins); 0 (Recombinant Proteins); 0 (Solvents); 146-14-5 (Flavin-Adenine Dinucleotide); 42HK56048U (Tyrosine); 6M3C89ZY6R (Nicotine); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01160


  2 / 29 MEDLINE  
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[PMID]:27526386
[Au] Autor:Guerrero-González ML; Ortega-Amaro MA; Juárez-Montiel M; Jiménez-Bremont JF
[Ad] Endereço:Facultad de Agronomía y Veterinaria, Universidad Autónoma de San Luis Potosí, San Luis Potosí, Mexico.
[Ti] Título:Arabidopsis Polyamine oxidase-2 uORF is required for downstream translational regulation.
[So] Source:Plant Physiol Biochem;108:381-390, 2016 Nov.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In eukaryotic mRNAs, small upstream open reading frames (uORFs) located in the 5'-untranslated region control the translation of the downstream main ORF. Polyamine oxidase (PAO) enzymes catalyze the oxidation of higher polyamines such as spermidine and spermine, and therefore contribute to the maintenance of intracellular polyamine content and to the regulation of physiological processes through their catabolic products. Recently, we reported that the Arabidopsis thaliana Polyamine Oxidase 2 (AtPAO2) is post-transcriptionally regulated by its 5'-UTR region through an uORF. In the present study, we analyzed whether the translation of the uORF is needed for the translational repression of the main ORF, and whether the inactivation of the uORF had an effect on the translational control mediated by polyamines. To this aim, we generated diverse single mutations in the uORF sequence; these mutant 5'-UTRs were fused to the GUS reporter gene, and tested in onion monolayer cells and A. thaliana transgenic seedlings. Removal of the start codon or introduction of a premature stop codon in the AtPAO2 uORF sequence abolished the negative regulation of the GUS expression exerted by the wild-type AtPAO2 uORF. An artificial uORF (32 amino acids in length) generated by the addition of a single nucleotide in AtPAO2 uORF proved to be less repressive than the wild-type uORF. Thus, our findings suggest that translation of the AtPAO2 uORF is necessary for the translational repression of the main ORF.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Fases de Leitura Aberta
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/genética
Biossíntese de Proteínas/genética
[Mh] Termos MeSH secundário: Arabidopsis/efeitos dos fármacos
Proteínas de Arabidopsis/metabolismo
Códon de Iniciação
Mutação da Fase de Leitura
Regulação da Expressão Gênica de Plantas
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Plantas Geneticamente Modificadas
Poliaminas/farmacologia
Plântulas/efeitos dos fármacos
Plântulas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Codon, Initiator); 0 (Polyamines); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.- (PAO2 protein, Arabidopsis); EC 1.5.3.- (polyamine oxidase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170813
[Lr] Data última revisão:
170813
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE


  3 / 29 MEDLINE  
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[PMID]:25410133
[Au] Autor:Zdor RE
[Ad] Endereço:Department of Biology, Andrews University, Berrien Springs, MI, USA.
[Ti] Título:Bacterial cyanogenesis: impact on biotic interactions.
[So] Source:J Appl Microbiol;118(2):267-74, 2015 Feb.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The ability of bacteria to influence organisms that they associate with via metabolite production is one of the hallmarks of microbial interactions. One metabolite of interest is the metabolic poison cyanide. Production of this metabolite is an unique characteristic of certain bacteria that inhabit a wide array of habitats ranging from the human body to the rhizosphere. This review focuses on four targets of cyanogenic bacteria: the human lung, plant pathogens, plants and invertebrates. For a number of cyanogenic bacteria, the contribution of cyanide to the interaction has been rigorously tested using mutants altered in cyanide production. Both deleterious and stimulatory effects of cyanogenic bacteria on other organisms have been documented. In addition, the HCN synthase-encoding gene cluster hcnABC has served as a marker of cyanogenic capability in the soil environment revealing both genetic diversity at this locus and regulatory influences by other organisms. The pervasive nature of cyanogenesis in a number of different ecological contexts encourages exploration of this bacterial ability and its possible optimization for improving human health, crop production and pest control.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Cianeto de Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Fibrose Cística/microbiologia
Seres Humanos
Invertebrados
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/genética
Desenvolvimento Vegetal
Plantas/metabolismo
Microbiologia do Solo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
2WTB3V159F (Hydrogen Cyanide); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); EC 1.4.99.5 (glycine dehydrogenase (cyanide-forming))
[Em] Mês de entrada:1509
[Cu] Atualização por classe:150123
[Lr] Data última revisão:
150123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141121
[St] Status:MEDLINE
[do] DOI:10.1111/jam.12697


  4 / 29 MEDLINE  
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[PMID]:23464874
[Au] Autor:Yang Y; Bu D; Zhao X; Sun P; Wang J; Zhou L
[Ad] Endereço:State Key Laboratory of Animal Nutrition, Institute of Animal Science, Chinese Academy of Agricultural Sciences , Beijing 100193, China.
[Ti] Título:Proteomic analysis of cow, yak, buffalo, goat and camel milk whey proteins: quantitative differential expression patterns.
[So] Source:J Proteome Res;12(4):1660-7, 2013 Apr 05.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To aid in unraveling diverse genetic and biological unknowns, a proteomic approach was used to analyze the whey proteome in cow, yak, buffalo, goat, and camel milk based on the isobaric tag for relative and absolute quantification (iTRAQ) techniques. This analysis is the first to produce proteomic data for the milk from the above-mentioned animal species: 211 proteins have been identified and 113 proteins have been categorized according to molecular function, cellular components, and biological processes based on gene ontology annotation. The results of principal component analysis showed significant differences in proteomic patterns among goat, camel, cow, buffalo, and yak milk. Furthermore, 177 differentially expressed proteins were submitted to advanced hierarchical clustering. The resulting clustering pattern included three major sample clusters: (1) cow, buffalo, and yak milk; (2) goat, cow, buffalo, and yak milk; and (3) camel milk. Certain proteins were chosen as characterization traits for a given species: whey acidic protein and quinone oxidoreductase for camel milk, biglycan for goat milk, uncharacterized protein (Accession Number: F1MK50 ) for yak milk, clusterin for buffalo milk, and primary amine oxidase for cow milk. These results help reveal the quantitative milk whey proteome pattern for analyzed species. This provides information for evaluating adulteration of specific specie milk and may provide potential directions for application of specific milk protein production based on physiological differences among animal species.
[Mh] Termos MeSH primário: Proteínas do Leite/análise
Leite/química
Proteômica/métodos
[Mh] Termos MeSH secundário: Animais
Biglicano/metabolismo
Búfalos
Camelus
Bovinos
Análise por Conglomerados
Clusterina/metabolismo
Cabras
Proteínas do Leite/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/metabolismo
Análise de Componente Principal
Especificidade da Espécie
Proteínas do Soro do Leite
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biglycan); 0 (Clusterin); 0 (Milk Proteins); 0 (Whey Proteins); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:161128
[Lr] Data última revisão:
161128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130308
[St] Status:MEDLINE
[do] DOI:10.1021/pr301001m


  5 / 29 MEDLINE  
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[PMID]:21777627
[Au] Autor:Gadkar VJ; Filion M
[Ad] Endereço:Department of Biology, Université de Moncton, 18 Antonine-Maillet, Moncton, NB, Canada E1A 3E9.
[Ti] Título:A novel method to perform genomic walks using a combination of single strand DNA circularization and rolling circle amplification.
[So] Source:J Microbiol Methods;87(1):38-43, 2011 Oct.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Characterization of regions flanking a known sequence within a genome, known as genome walking, is a cornerstone technique in modern genetic analysis. In the present work we have developed a new PCR-dependent, directional genome walking protocol based on the unique circularization property of a novel DNA ligase, CircLigase. In the first step, PCR based primer extension is performed using a phosphorylated primer, designed to extend from the boundary of the known sequence, into the flanking region. This linear amplification results in the generation of single-stranded (ss) DNA, which is then circularized using CircLigase. Using the hyperbranching activity of Phi29 DNA polymerase, the circular ssDNA is then linearized by rolling circle amplification, resulting in copious amounts of double stranded concatameric DNA. Nested primers are used to amplify the flanking sequence using inverse PCR. The products are resolved on an agarose gel and the bands whose mobility change due to the nested location of the primer combination used are identified, extracted, and cloned into a plasmid vector for sequencing. Empirical proof for this concept was generated on two antimicrobial biosynthetic genes in Pseudomonas sp. LBUM300. Using the hcnB and phlD genes as starting points, ca 1 kb of flanking sequences were successfully isolated. The use of locus specific primers ensured both directionality and specificity of the walks, alleviating the generation of spurious amplicons, typically observed in randomly primed walking protocols. The presented genome walking protocol could be applied to any microbial genome and requires only 100-150 bp of prior sequence information. The proposed methodology does not entail laborious testing of restriction enzymes or adaptor ligation. This is the first report of a successful application of the novel ligase enzyme, CircLigase for genomic walking purposes.
[Mh] Termos MeSH primário: DNA Circular/química
DNA de Cadeia Simples/química
Genoma Bacteriano
Técnicas de Amplificação de Ácido Nucleico
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Sequência de Bases
DNA Ligases/química
Dados de Sequência Molecular
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/genética
Pseudomonas/genética
Análise de Sequência de DNA/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Circular); 0 (DNA, Single-Stranded); 0 (PhlD protein, Pseudomonas); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); EC 1.4.99.5 (glycine dehydrogenase (cyanide-forming)); EC 6.5.1.- (DNA Ligases)
[Em] Mês de entrada:1112
[Cu] Atualização por classe:110906
[Lr] Data última revisão:
110906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110723
[St] Status:MEDLINE
[do] DOI:10.1016/j.mimet.2011.07.003


  6 / 29 MEDLINE  
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[PMID]:21373760
[Au] Autor:Olivieri A; Rico D; Khiari Z; Henehan G; O'Sullivan J; Tipton K
[Ad] Endereço:School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland. oliviera@tcd.ie
[Ti] Título:From caffeine to fish waste: amine compounds present in food and drugs and their interactions with primary amine oxidase.
[So] Source:J Neural Transm (Vienna);118(7):1079-89, 2011 Jul.
[Is] ISSN:1435-1463
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Tissue bound primary amine oxidase (PrAO) and its circulating plasma-soluble form are involved, through their catalytic activity, in important cellular roles, including the adhesion of lymphocytes to endothelial cells during various inflammatory conditions, the regulation of cell growth and maturation, extracellular matrix deposition and maturation and glucose transport. PrAO catalyses the oxidative deamination of several xenobiotics and has been linked to vascular toxicity, due to the generation of cytotoxic aldehydes. In this study, a series of amines and aldehydes contained in food and drugs were tested via a high-throughput assay as potential substrates or inhibitors of bovine plasma PrAO. Although none of the compounds analyzed were found to be substrates for the enzyme, a series of molecules, including caffeine, the antidiabetics phenformin and tolbutamide and the antimicrobial pentamidine, were identified as PrAO inhibitors. Although the inhibition observed was in the millimolar and micromolar range, these data show that further work will be necessary to elucidate whether the interaction of ingested biogenic or xenobiotic amines with PrAO might adversely affect its biological roles.
[Mh] Termos MeSH primário: Aminas/efeitos adversos
Inibidores Enzimáticos/efeitos adversos
Alimentos/efeitos adversos
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/antagonistas & inibidores
[Mh] Termos MeSH secundário: Aminas/metabolismo
Animais
Cafeína/efeitos adversos
Cafeína/metabolismo
Bovinos
Avaliação Pré-Clínica de Medicamentos/métodos
Ensaios Enzimáticos/métodos
Inibidores Enzimáticos/metabolismo
Produtos Pesqueiros/efeitos adversos
Peixes
Seres Humanos
Hipoglicemiantes/efeitos adversos
Hipoglicemiantes/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/metabolismo
Fenformin/efeitos adversos
Fenformin/metabolismo
Xenobióticos/efeitos adversos
Xenobióticos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amines); 0 (Enzyme Inhibitors); 0 (Hypoglycemic Agents); 0 (Xenobiotics); 3G6A5W338E (Caffeine); DD5K7529CE (Phenformin); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110305
[St] Status:MEDLINE
[do] DOI:10.1007/s00702-011-0611-z


  7 / 29 MEDLINE  
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[PMID]:20306300
[Au] Autor:Kim YM; Kim EC; Kim Y
[Ad] Endereço:Department of Biochemistry, School of Medicine, Wonkwang University, Iksan, Jeonbuk, 570-749, Korea.
[Ti] Título:The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin.
[So] Source:Mol Biol Rep;38(1):145-9, 2011 Jan.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The lysyl oxidase-like 2 (LOXL2) protein is a human paralogue of lysyl oxidase (LOX) that functions as an amine oxidase for formation of lysine-derived cross-links found in collagen and elastin. In addition to the C-terminal domains characteristic to the LOX family members, LOXL2 contains four scavenger receptor cysteine-rich (SRCR) domains in the N-terminus. In order to assess the amine oxidase activity of LOXL2, we expressed a series of recombinant LOXL2 proteins with deletions in the SRCR domains, using an Escherichia coli expression system. All of the purified recombinant LOXL2 proteins, with or without the SRCR domains in the N-terminus, showed significant amine oxidase activity toward several different types of collagen and elastin in in vitro amine oxidase assays, indicating deletion of the SRCR domains does not interfere with amine oxidase activity of LOXL2. Further, amine oxidase activity of LOXL2 was not susceptible to inhibition by ß-aminopropionitrile, an irreversible inhibitor of LOX, suggesting a different enzymatic mechanism between these two paralogues.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/metabolismo
Colágeno/metabolismo
Elastina/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/metabolismo
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/química
Aminopropionitrilo/farmacologia
Animais
Bovinos
Escherichia coli
Seres Humanos
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/química
Estrutura Terciária de Proteína
Proteínas Recombinantes/isolamento & purificação
Especificidade por Substrato/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Recombinant Proteins); 151-18-8 (Aminopropionitrile); 9007-34-5 (Collagen); 9007-58-3 (Elastin); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); EC 1.4.3.- (LOXL2 protein, human)
[Em] Mês de entrada:1103
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100323
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-010-0088-0


  8 / 29 MEDLINE  
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[PMID]:20530901
[Au] Autor:Liu YH; Wu WC; Lu YL; Lai YJ; Hou WC
[Ad] Endereço:Division of Gastroenterology, Shin Kong Wu Ho-Su Memorial Hospital, Taipei, Taiwan.
[Ti] Título:Antioxidant and amine oxidase inhibitory activities of hydroxyurea.
[So] Source:Biosci Biotechnol Biochem;74(6):1256-60, 2010.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hydroxyurea (HU, NH(2)CONHOH), or hydroxycarbamide, is a hydroxamic acid derivative used as a drug for anti-neoplasm and sickle-cell disease. In this study, HU was found to have antioxidant activities against 2,2-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl radicals and dose-dependent inhibitory activities against monoamine oxidase (MAO)-A, MAO-B, and semicarbazide-sensitive amine oxidase (SSAO) as compared to controls of clorgyline, deprenyl, and semicarbazide respectively. HU showed mixed-type, competitive-type, and competitive-type inhibition, respectively, with respect to substrates of MAO-A, MAO-B, and SSAO with apparent inhibition constants (Ki) of 19.46, 5.38, and 1.84 microM.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Depuradores de Radicais Livres/farmacologia
Hidroxiureia/farmacologia
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Compostos de Bifenilo/química
Bovinos
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Depuradores de Radicais Livres/química
Radical Hidroxila/química
Hidroxiureia/química
Cinética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/metabolismo
Picratos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biphenyl Compounds); 0 (Enzyme Inhibitors); 0 (Free Radical Scavengers); 0 (Picrates); 3352-57-6 (Hydroxyl Radical); DFD3H4VGDH (1,1-diphenyl-2-picrylhydrazyl); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); X6Q56QN5QC (Hydroxyurea)
[Em] Mês de entrada:1010
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100610
[St] Status:MEDLINE


  9 / 29 MEDLINE  
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[PMID]:19624733
[Au] Autor:Forneris F; Battaglioli E; Mattevi A; Binda C
[Ad] Endereço:Dipartimento di Genetica e Microbiologia, Università di Pavia, Italy.
[Ti] Título:New roles of flavoproteins in molecular cell biology: histone demethylase LSD1 and chromatin.
[So] Source:FEBS J;276(16):4304-12, 2009 Aug.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lysine-specific demethylase 1 (LSD1) is an enzyme that removes methyl groups from mono- and dimethylated Lys4 of histone H3, a post-translational modification associated with gene activation. Human LSD1 was the first histone demethylase to be discovered and this enzymatic activity is conserved among eukaryotes. LSD1 has been identified in a number of chromatin-remodeling complexes that control gene transcription and its demethylase activity has also been linked to pathological processes including tumorigenesis. The 852-residue sequence of LSD1 comprises an amine oxidase domain which identifies a family of enzymes that catalyze the FAD-dependent oxidation of amine substrates ranging from amino acids to aromatic neurotransmitters. Among these proteins, LSD1 is peculiar in that it acts on a protein substrate in the nuclear environment of chromatin-remodeling complexes. This functional divergence occurred during evolution from the eubacteria to eukaryotes by acquisition of additional domains such as the SWIRM domain. The N-terminal part of LSD1, predicted to be disordered, contains linear motifs that might represent functional sites responsible for the association of this enzyme with a variety of transcriptional protein complexes. LSD1 shares structural features with other flavin amine oxidases, including the overall fold of the amine oxidase domain region and details in the active site that are relevant for amine substrate oxidation.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Flavoproteínas/fisiologia
Regulação da Expressão Gênica
Oxirredutases N-Desmetilantes/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias
Proteínas Fúngicas
Histona Desmetilases
Seres Humanos
Metilação
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2
Proteínas de Plantas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Chromatin); 0 (Flavoproteins); 0 (Fungal Proteins); 0 (Plant Proteins); EC 1.14.11.- (Histone Demethylases); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); EC 1.5.- (KDM1A protein, human); EC 1.5.- (Oxidoreductases, N-Demethylating)
[Em] Mês de entrada:0909
[Cu] Atualização por classe:111027
[Lr] Data última revisão:
111027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090724
[St] Status:MEDLINE
[do] DOI:10.1111/j.1742-4658.2009.07142.x


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[PMID]:19210678
[Au] Autor:Svercel M; Christen D; Moënne-Loccoz Y; Duffy B; Défago G
[Ad] Endereço:Plant Pathology, Institute of Integrative Biology, Zürich, Switzerland.
[Ti] Título:Effect of long-term vineyard monoculture on rhizosphere populations of pseudomonads carrying the antimicrobial biosynthetic genes phlD and/or hcnAB.
[So] Source:FEMS Microbiol Ecol;68(1):25-36, 2009 Apr.
[Is] ISSN:1574-6941
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The impact of repeated culture of perennial plants (i.e. in long-term monoculture) on the ecology of plant-beneficial bacteria is unknown. Here, the influence of extremely long-term monocultures of grapevine (up to 1603 years) on rhizosphere populations of fluorescent pseudomonads carrying the biosynthetic genes phlD for 2,4-diacetylphloroglucinol and/or hcnAB for hydrogen cyanide was determined. Soils from long-term and adjacent short-term monoculture vineyards (or brushland) in four regions of Switzerland were baited with grapevine or tobacco plantlets, and rhizosphere pseudomonads were studied by most probable number (MPN)-PCR. Higher numbers and percentages of phlD(+) and of hcnAB(+) rhizosphere pseudomonads were detected on using soil from long-term vineyards. On focusing on phlD, restriction fragment length polymorphism profiling of the last phlD-positive MPN wells revealed seven phlD alleles (three exclusively on tobacco, thereof two new ones). Higher numbers of phlD alleles coincided with a lower prevalence of the allele displayed by the well-studied biocontrol strain Pseudomonas fluorescens F113. The prevalence of this allele was 35% for tobacco in long-term monoculture soils vs. >60% in the other three cases. We conclude that soils from long-term grapevine monocultures represent an untapped resource for isolating novel biocontrol Pseudomonas strains when tobacco is used as bait.
[Mh] Termos MeSH primário: Agricultura/métodos
Pseudomonas/isolamento & purificação
Microbiologia do Solo
Vitis/microbiologia
[Mh] Termos MeSH secundário: Antibiose
Proteínas de Bactérias/genética
Biodiversidade
Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/genética
Polimorfismo de Fragmento de Restrição
Pseudomonas/genética
Suíça
Tabaco/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (PhlD protein, Pseudomonas); EC 1.4.- (Oxidoreductases Acting on CH-NH2 Group Donors); EC 1.4.99.5 (glycine dehydrogenase (cyanide-forming))
[Em] Mês de entrada:0903
[Cu] Atualização por classe:090317
[Lr] Data última revisão:
090317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090213
[St] Status:MEDLINE
[do] DOI:10.1111/j.1574-6941.2009.00649.x



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