Base de dados : MEDLINE
Pesquisa : B03.510.024.049.537 [Categoria DeCS]
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  1 / 133 MEDLINE  
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[PMID]:27238429
[Au] Autor:Matsumoto M; Hayashi K; Suetake H; Yamamoto A; Araki K
[Ad] Endereço:The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-8580, Japan.
[Ti] Título:Identification and functional characterization of multiple interleukin 12 in amberjack (Seriola dumerili).
[So] Source:Fish Shellfish Immunol;55:281-92, 2016 Aug.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Interleukin (IL) -12 is a heterodimeric cytokine mainly produced by monocytes, macrophages, and dendritic cells in mammals. IL-12p70 composed of IL-12p35 and IL-12p40, is known to play a crucial role in promoting cell-mediated immunity (CMI) through Th1 differentiation and IFN-γ production. Although two types of IL-12p35 (p35a, p35b) and three types of IL-12p40 (p40a, p40b and p40c) have been identified in several fish species, the knowledge on functional characteristics of teleost IL-12 is still limited. In the present study, we cloned two types of IL-12p35 and three types of IL-12p40 genes in amberjack and yellowtail, and analyzed their expressions in response to stimulation with Nocardia seriolae in amberjack. As a result, four types of IL-12 (IL-12p35a, p35b, p40a and p40b) and IFN-γ mRNA were increased by live-N. seriolae stimulation but not by formalin-killed N. seriolae, suggesting that four types of IL-12 (p35, p35b, p40a and p40c) participate in promoting CMI. Subsequently, we produced six types of recombinant IL-12p70 (rIL12p70) protein in insect cells. Head kidney leukocytes were cultured with formalin-killed N. seriolae and six types of rIL-12p70 to elucidate the role of amberjack IL-12p70 in induction of CMI. After stimulation, IFN-γ expression was elevated whereas IL-10 expression was suppressed in Head kidney leukocytes stimulated with four types of rIL-12 (p40a/p35a, p40c/p35a, p40a/p35b, p40a/p35b). On the other hand, two types of rIL-12 (p40b/p35a, p40b/p35b) only elicited down regulation of IL-10 expression. These results indicate that all amberjack IL-12p70 isoforms are involved in Th1 -differentiation and promotion of CMI with different manners. Fish IL-12 has a potential for the promising vaccine adjuvant.
[Mh] Termos MeSH primário: Infecções por Actinomycetales/veterinária
Vacinas Bacterianas/imunologia
Doenças dos Peixes/terapia
Proteínas de Peixes/genética
Interleucina-12/genética
Nocardiaceae/imunologia
Perciformes
[Mh] Termos MeSH secundário: Infecções por Actinomycetales/microbiologia
Infecções por Actinomycetales/terapia
Sequência de Aminoácidos
Animais
Doenças dos Peixes/microbiologia
Proteínas de Peixes/química
Proteínas de Peixes/metabolismo
Interleucina-12/química
Interleucina-12/metabolismo
Subunidade p35 da Interleucina-12/genética
Subunidade p35 da Interleucina-12/metabolismo
Subunidade p40 da Interleucina-12/genética
Subunidade p40 da Interleucina-12/metabolismo
Filogenia
Alinhamento de Sequência/veterinária
Vacinas Atenuadas/imunologia
Vacinas de Produtos Inativados/imunologia
Vacinas Sintéticas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Vaccines); 0 (Fish Proteins); 0 (Interleukin-12 Subunit p35); 0 (Interleukin-12 Subunit p40); 0 (Vaccines, Attenuated); 0 (Vaccines, Inactivated); 0 (Vaccines, Synthetic); 187348-17-0 (Interleukin-12)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170217
[Lr] Data última revisão:
170217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160531
[St] Status:MEDLINE


  2 / 133 MEDLINE  
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[PMID]:26792212
[Au] Autor:Cribbs SK; Uppal K; Li S; Jones DP; Huang L; Tipton L; Fitch A; Greenblatt RM; Kingsley L; Guidot DM; Ghedin E; Morris A
[Ad] Endereço:Pulmonary Medicine, Department of Veterans Affairs Medical Center, 1670 Clairmont Rd, Mailstop 151p, Decatur, 30033, GA, USA. skomaku@emory.edu.
[Ti] Título:Correlation of the lung microbiota with metabolic profiles in bronchoalveolar lavage fluid in HIV infection.
[So] Source:Microbiome;4:3, 2016 Jan 20.
[Is] ISSN:2049-2618
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: While 16S ribosomal RNA (rRNA) sequencing has been used to characterize the lung's bacterial microbiota in human immunodeficiency virus (HIV)-infected individuals, taxonomic studies provide limited information on bacterial function and impact on the host. Metabolic profiles can provide functional information on host-microbe interactions in the lungs. We investigated the relationship between the respiratory microbiota and metabolic profiles in the bronchoalveolar lavage fluid of HIV-infected and HIV-uninfected outpatients. RESULTS: Targeted sequencing of the 16S rRNA gene was used to analyze the bacterial community structure and liquid chromatography-high-resolution mass spectrometry was used to detect features in bronchoalveolar lavage fluid. Global integration of all metabolic features with microbial species was done using sparse partial least squares regression. Thirty-nine HIV-infected subjects and 20 HIV-uninfected controls without acute respiratory symptoms were enrolled. Twelve mass-to-charge ratio (m/z) features from C18 analysis were significantly different between HIV-infected individuals and controls (false discovery rate (FDR) = 0.2); another 79 features were identified by network analysis. Further metabolite analysis demonstrated that four features were significantly overrepresented in the bronchoalveolar lavage (BAL) fluid of HIV-infected individuals compared to HIV-uninfected, including cystine, two complex carbohydrates, and 3,5-dibromo-L-tyrosine. There were 231 m/z features significantly associated with peripheral blood CD4 cell counts identified using sparse partial least squares regression (sPLS) at a variable importance on projection (VIP) threshold of 2. Twenty-five percent of these 91 m/z features were associated with various microbial species. Bacteria from families Caulobacteraceae, Staphylococcaceae, Nocardioidaceae, and genus Streptococcus were associated with the greatest number of features. Glycerophospholipid and lineolate pathways correlated with these bacteria. CONCLUSIONS: In bronchoalveolar lavage fluid, specific metabolic profiles correlated with bacterial organisms known to play a role in the pathogenesis of pneumonia in HIV-infected individuals. These findings suggest that microbial communities and their interactions with the host may have functional metabolic impact in the lung.
[Mh] Termos MeSH primário: Infecções por HIV/metabolismo
Infecções por HIV/microbiologia
Pulmão/metabolismo
Metaboloma
Microbiota/genética
RNA Ribossômico 16S/genética
[Mh] Termos MeSH secundário: Adulto
Líquido da Lavagem Broncoalveolar/microbiologia
Estudos de Casos e Controles
Caulobacteraceae/classificação
Caulobacteraceae/genética
Caulobacteraceae/metabolismo
Cromatografia Líquida
Cistina/metabolismo
Feminino
Glicerofosfolipídeos/metabolismo
HIV/crescimento & desenvolvimento
Infecções por HIV/virologia
Interações Hospedeiro-Patógeno
Seres Humanos
Análise dos Mínimos Quadrados
Pulmão/microbiologia
Masculino
Espectrometria de Massas
Nocardiaceae/classificação
Nocardiaceae/genética
Nocardiaceae/metabolismo
RNA Ribossômico 16S/metabolismo
Análise de Sequência de RNA
Staphylococcaceae/classificação
Staphylococcaceae/genética
Staphylococcaceae/metabolismo
Streptococcus/classificação
Streptococcus/genética
Streptococcus/metabolismo
Tirosina/análogos & derivados
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Glycerophospholipids); 0 (RNA, Ribosomal, 16S); 42HK56048U (Tyrosine); 48TCX9A1VT (Cystine); 537-24-6 (3,5-dibromotyrosine)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160122
[St] Status:MEDLINE
[do] DOI:10.1186/s40168-016-0147-4


  3 / 133 MEDLINE  
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[PMID]:25146761
[Au] Autor:Pietra F
[Ad] Endereço:Accademia Lucchese di Scienze, Lettere e Arti, Classe di Scienze, Palazzo Ducale, Lucca I-55100, (phone/fax: +39-0583-417336). francesco.pietra@accademialucchese.it.
[Ti] Título:Binding pockets and pathways for dioxygen through the KijD3 N-oxygenase in complex with flavin mononucleotide cofactor and a 3-aminoglucose substrate: predictions from molecular dynamics simulations.
[So] Source:Chem Biodivers;11(8):1151-62, 2014 Aug.
[Is] ISSN:1612-1880
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:In this work, two protein systems, Kij3D-FMN-AKM-O2 and Kij3D-FMN-O2 , made of KijD3 N-oxygenase, flavin mononucleotide (FMN) cofactor, dTDP-3-amino-2,3,6-trideoxy-4-keto-3-methyl-D-glucose (AKM) substrate, and dioxygen (O2), have been assembled by adding a molecule of O2, and removing (or not) AKM, to crystal data for the Kij3D-FMN-AKM complex. Egress of AKM and O2 from these systems was then investigated by applying a tiny external random force, in turn, to their center of mass in the course of molecular dynamics in explicit H2 O. It turned out that the wide AKM channel, even when emptied, does not constitute the main route for O2 egress. Other routes appear to be also viable, while various binding pockets (BPs) outside the active center are prone to trap O2. By reversing the reasoning, these can also be considered as routes for uptake of O2 by the protein, before or after AKM uptake, while BPs may serve as reservoirs of O2. This shows that the small molecule O2 is capable of permeating the protein by exploiting all nearby interstices that are created on thermal fluctuations of the protein, rather than having necessarily to look for farther, permanent channels.
[Mh] Termos MeSH primário: Mononucleotídeo de Flavina/química
Oxigênio/metabolismo
Oxigenases/química
Oxigenases/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Mononucleotídeo de Flavina/metabolismo
Modelos Moleculares
Simulação de Dinâmica Molecular
Nocardiaceae/enzimologia
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
7N464URE7E (Flavin Mononucleotide); EC 1.13.- (Oxygenases); S88TT14065 (Oxygen)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140822
[Lr] Data última revisão:
140822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140823
[St] Status:MEDLINE
[do] DOI:10.1002/cbdv.201400081


  4 / 133 MEDLINE  
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[PMID]:22934346
[Au] Autor:Du H; Yu L; Zhang Y
[Ad] Endereço:Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China. dujing5555@gmail.com
[Ti] Título:[Recent advance on the genus nocardioides--a review].
[So] Source:Wei Sheng Wu Xue Bao;52(6):671-8, 2012 Jun 04.
[Is] ISSN:0001-6209
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:The Nocardioides genus was established by Prauser H. in 1976 according to morphological and physiological characteristics, as well as partial chemotaxonomic analyses of 17 nocardio-form actinobacteria isolated from soil, based on which a novel species Nocardioides albus was proposed as the type species. With the development in the technologies of isolation, purification and taxonomy, more and more members of this genus with varied morphological, physiological and biochemical characteristics were increasingly discovered from different sources, while all of them shared the same diagnostic characteristics of the genus. In the past 50 years, some of the members of the genus Nocardioides were ever transferred in or out and then some species description was ever emended. Till date, there were 56 validly described species in this genus. Some members of this genus were used in agriculture and industry. The objective of this review is to summarize the research advances in the genus Nocardioides, such as the changes of the taxonomic position and emendation description of the species as well as the application prospect in industry and agriculture.
[Mh] Termos MeSH primário: Nocardiaceae/classificação
[Mh] Termos MeSH secundário: Nocardiaceae/genética
Filogenia
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Em] Mês de entrada:1211
[Cu] Atualização por classe:120831
[Lr] Data última revisão:
120831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120901
[St] Status:MEDLINE


  5 / 133 MEDLINE  
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[PMID]:20538584
[Au] Autor:Reed T; Lushington GH; Xia Y; Hirakawa H; Travis DM; Mure M; Scott EE; Limburg J
[Ad] Endereço:Department of Chemistry, The University of Kansas, Lawrence, Kansas 66045, USA.
[Ti] Título:Crystal structure of histamine dehydrogenase from Nocardioides simplex.
[So] Source:J Biol Chem;285(33):25782-91, 2010 Aug 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histamine dehydrogenase (HADH) isolated from Nocardioides simplex catalyzes the oxidative deamination of histamine to imidazole acetaldehyde. HADH is highly specific for histamine, and we are interested in understanding the recognition mode of histamine in its active site. We describe the first crystal structure of a recombinant form of HADH (HADH) to 2.7-A resolution. HADH is a homodimer, where each 76-kDa subunit contains an iron-sulfur cluster ([4Fe-4S](2+)) and a 6-S-cysteinyl flavin mononucleotide (6-S-Cys-FMN) as redox cofactors. The overall structure of HADH is very similar to that of trimethylamine dehydrogenase (TMADH) from Methylotrophus methylophilus (bacterium W3A1). However, some distinct differences between the structure of HADH and TMADH have been found. Tyr(60), Trp(264), and Trp(355) provide the framework for the "aromatic bowl" that serves as a trimethylamine-binding site in TMADH is comprised of Gln(65), Trp(267), and Asp(358), respectively, in HADH. The surface Tyr(442) that is essential in transferring electrons to electron-transfer flavoprotein (ETF) in TMADH is not conserved in HADH. We use this structure to propose the binding mode for histamine in the active site of HADH through molecular modeling and to compare the interactions to those observed for other histamine-binding proteins whose structures are known.
[Mh] Termos MeSH primário: Nocardiaceae/enzimologia
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Estrutura Molecular
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.99.- (histamine dehydrogenase)
[Em] Mês de entrada:1008
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100612
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M109.084301


  6 / 133 MEDLINE  
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[PMID]:20334431
[Au] Autor:Bruender NA; Thoden JB; Holden HM
[Ad] Endereço:Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
[Ti] Título:X-ray structure of kijd3, a key enzyme involved in the biosynthesis of D-kijanose.
[So] Source:Biochemistry;49(17):3517-24, 2010 May 04.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:D-kijanose is an unusual nitrosugar found attached to the antibiotic kijanimicin. Ten enzymes are required for its production in Actinomadura kijaniata, a soil-dwelling actinomycete. The focus of this investigation is on the protein encoded by the kijd3 gene and hereafter referred to as KijD3. On the basis of amino acid sequence analyses, KijD3 has been proposed to be an FAD-dependent oxidoreductase, which catalyzes the sixth step in d-kijanose biosynthesis by converting dTDP-3-amino-2,3,6-trideoxy-4-keto-3-methyl-d-glucose into its C-3' nitro derivative. This putative activity, however, has never been demonstrated in vivo or in vitro. Here we report the first structural study of this enzyme. For our investigation, crystals of KijD3 were grown in the presence of dTDP, and the structure was solved to 2.05-A resolution. The enzyme is a tetramer with each subunit folding into three distinct regions: a five alpha-helical bundle, an eight-stranded beta-sheet, and a second five alpha-helical bundle. The dTDP moiety is anchored to the protein via the side chains of Glu 113, Gln 254, and Arg 330. The overall fold of KijD3 places it into the well-characterized fatty acyl-CoA dehydrogenase superfamily. There is a decided cleft in each subunit with the appropriate dimensions to accommodate a dTDP-linked sugar. Strikingly, the loop defined by Phe 383 to Ala 388, which projects into the active site, contains two adjacent cis-peptide bonds, Pro 386 and Tyr 387. Activity assays demonstrate that KijD3 requires FAD for activity and that it produces a hydroxylamino product. The molecular architecture of KijD3 described in this report serves as a paradigm for a new family of enzymes that function on dTDP-linked sugar substrates.
[Mh] Termos MeSH primário: Acil-CoA Desidrogenase/química
Acil-CoA Desidrogenase/metabolismo
Aminoglicosídeos/metabolismo
Flavina-Adenina Dinucleotídeo/metabolismo
Nitrorredutases/química
Nitrorredutases/metabolismo
Nocardiaceae/enzimologia
[Mh] Termos MeSH secundário: Acil-CoA Desidrogenase/genética
Catálise
Domínio Catalítico
Clonagem Molecular
Cristalização
Cristalografia por Raios X
Dimerização
Modelos Moleculares
Nitrorredutases/genética
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Aminoglycosides); 146-14-5 (Flavin-Adenine Dinucleotide); 78798-08-0 (kijanimicin); EC 1.3.8.7 (Acyl-CoA Dehydrogenase); EC 1.7.- (Nitroreductases)
[Em] Mês de entrada:1005
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100326
[St] Status:MEDLINE
[do] DOI:10.1021/bi100318v


  7 / 133 MEDLINE  
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[PMID]:20202801
[Au] Autor:Kiran GS; Thomas TA; Selvin J
[Ad] Endereço:School of Life Sciences, Bharathidasan University, Tiruchirappalli, India.
[Ti] Título:Production of a new glycolipid biosurfactant from marine Nocardiopsis lucentensis MSA04 in solid-state cultivation.
[So] Source:Colloids Surf B Biointerfaces;78(1):8-16, 2010 Jun 15.
[Is] ISSN:1873-4367
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Considering the need of potential biosurfactant producers and economic production processes using industrial waste, the present study aims to develop solid-state culture (SSC) of a marine actinobacterium for biosurfactant production. A potential biosurfactant producer Nocardiopsis lucentensis MSA04 was isolated from the marine sponge Dendrilla nigra. Among the substrates screened, wheat bran increased the production significantly (E(24) 25%) followed by oil seed cake and industrial waste such as tannery pretreated sludge, treated molasses (distillery waste) and pretreated molasses. Enhanced biosurfactant production was achieved under SSC conditions using kerosene as carbon source, beef extract as nitrogen source and wheat bran as substrate. The maximum production of biosurfactant by MSA04 occurred at a C/N ratio of 0.5 envisaging that a higher amount of nitrogen source is required by the strain compared to that of the carbon source. The kerosene and beef extract interactively increase the production and a stable production was attained with the influence of both factors independently. A significant interactive influence of secondary control factors such as copper sulfate and inoculum size was validated in response surface methods-based experiments. The surface active compound produced by MSA04 was characterized as glycolipid with a hydrophobic non-polar hydrocarbon chain (nonanoic acid methyl ester) and hydrophilic sugar, 3-acetyl 2,5 dimethyl furan. In conclusion, the strain N. lucentensis MSA04 was a potential source of glycolipid biosurfactant, could be used for the development of bioremediation processes in the marine environment.
[Mh] Termos MeSH primário: Técnicas de Cultura de Células/métodos
Glicolipídeos/biossíntese
Nocardiaceae/química
Nocardiaceae/citologia
Água do Mar/microbiologia
Tensoativos/metabolismo
[Mh] Termos MeSH secundário: Análise de Variância
Carbono/farmacologia
Genes Bacterianos/genética
Glicolipídeos/química
Glicolipídeos/isolamento & purificação
Hidrocarbonetos/metabolismo
Interações Hidrofóbicas e Hidrofílicas
Querosene
Espectrometria de Massas
Nitrogênio/farmacologia
Nocardiaceae/genética
Nocardiaceae/isolamento & purificação
Filogenia
Propriedades de Superfície/efeitos dos fármacos
Tensoativos/química
Tensoativos/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycolipids); 0 (Hydrocarbons); 0 (Kerosene); 0 (Surface-Active Agents); 7440-44-0 (Carbon); N762921K75 (Nitrogen)
[Em] Mês de entrada:1007
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100306
[St] Status:MEDLINE
[do] DOI:10.1016/j.colsurfb.2010.01.028


  8 / 133 MEDLINE  
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[PMID]:19846434
[Au] Autor:Tsutsumi M; Tsuse N; Fujieda N; Kano K
[Ad] Endereço:Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
[Ti] Título:Site-directed mutation at residues near the catalytic site of histamine dehydrogenase from Nocardioides simplex and its effects on substrate inhibition.
[So] Source:J Biochem;147(2):257-64, 2010 Feb.
[Is] ISSN:1756-2651
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Histamine dehydrogenase from Nocardioides simplex (nHmDH) is a homodimer containing one 6-S-cysteinyl FMN (CFMN) and one [4Fe-4S] cluster per monomer. nHmDH catalyses the oxidative deamination of histamine to ammonia and imidazole acetaldehyde, but histamine inhibits its catalytic activity at high concentrations. We mutated gene-encoded residues (Tyr180, Gly268 and Asp269) near CFMN to understand the biophysical meaning of the substrate inhibition. Three mutants Y180F, G268D/D269C and Y180F/G268D/D269C were expressed by considering the DNA sequence alignment of histamine dehydrogenase from Rhizobium sp. 4-9 (rHmDH), which does not suffer from the substrate inhibition. The Y180F/G268D/D269C mutation to mimic rHmDH successfully suppressed the inhibition, although the catalytic activity decreased. The substrate inhibition was weakened by the Y180F mutation, but G268D/D269C was still susceptible to the inhibition. It was found that it also causes changes in the UV-vis absorption spectra of the substrate-reduced form and the redox potential of the enzymes. The characterization suggests that the thermodynamic preference of the semiquinone form of CFMN in the two-electron-reduced subunit of the enzyme is responsible for the substrate inhibition. However, destabilization of the semiquinone form leads to kinetic hindrance due to the uphill single electron transfer from the fully reduced CFMN to the [4Fe-4S] cluster.
[Mh] Termos MeSH primário: Mutagênese Sítio-Dirigida
Nocardiaceae/enzimologia
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico/genética
Cristalografia por Raios X
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Proteínas com Ferro-Enxofre/metabolismo
Cinética
Dados de Sequência Molecular
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/química
Homologia de Sequência de Aminoácidos
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.99.- (histamine dehydrogenase)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:100203
[Lr] Data última revisão:
100203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091023
[St] Status:MEDLINE
[do] DOI:10.1093/jb/mvp162


  9 / 133 MEDLINE  
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[PMID]:19735135
[Au] Autor:Narayanan R; Stottrup BL; Wang P
[Ad] Endereço:Department of Bioproducts and Biosystems Engineering and Biotechnology Institute, The University of Minnesota, St. Paul, Minnesota 55108, USA.
[Ti] Título:Surface packing characterization of Langmuir monolayer-anchored enzyme.
[So] Source:Langmuir;25(18):10660-5, 2009 Sep 15.
[Is] ISSN:0743-7463
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have synthesized a novel interface-anchoring alcohol dehydrogenase by covalent attachment of a hydrophobic polymer tail to the hydrophilic protein head. Analogous to a protein-based surfactant, this polymer-enzyme conjugate self-assembled at liquid-liquid or liquid-air interfaces to form a membrane similar to other surfactant monolayers. The packing and morphology of the interface-anchored enzymes play an important role in regulating the membrane behaviors including enzyme mobility and interfacial interactions of enzymes with reactant and product molecules. To characterize the surface assembly morphology of the interface-anchored enzymes, Langmuir film balance and fluorescence microscopy techniques were used. The Langmuir isotherm of the interface-anchored enzyme demonstrated a pronounced molecular rearrangement upon compression of the isotherm. This corresponded to changes in membrane morphology and state observed using fluorescence microscopy. The molecular diffusion within the novel interface-anchored enzymes was further evaluated by using a fluorescence recovery after photobleaching technique. We report a diffusion coefficient of 6.7x10(-10) cm2/s. The study represents the first in-depth analysis of surface packing and interfacial mobility of such interface-anchored enzymes.
[Mh] Termos MeSH primário: Álcool Desidrogenase/química
Álcool Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Acetofenonas
Adsorção
Difusão
Recuperação de Fluorescência Após Fotodegradação
Interações Hidrofóbicas e Hidrofílicas
Microscopia de Fluorescência
Nocardiaceae/enzimologia
Polímeros/química
Pressão
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Acetophenones); 0 (Polymers); EC 1.1.1.1 (Alcohol Dehydrogenase); RK493WHV10 (acetophenone)
[Em] Mês de entrada:0912
[Cu] Atualização por classe:121115
[Lr] Data última revisão:
121115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090909
[St] Status:MEDLINE
[do] DOI:10.1021/la901076j


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[PMID]:19154353
[Au] Autor:Ilari A; Fiorillo A; Angelaccio S; Florio R; Chiaraluce R; van der Oost J; Consalvi V
[Ad] Endereço:CNR Institute of Molecular Biology and Pathology, Italy. andrea.ilari@uniroma1.it
[Ti] Título:Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus--structural basis of substrate recognition.
[So] Source:FEBS J;276(4):1048-58, 2009 Feb.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bacterial and archaeal endo-beta-1,3-glucanases that belong to glycoside hydrolase family 16 share a beta-jelly-roll fold, but differ significantly in sequence and in substrate specificity. The crystal structure of the laminarinase (EC 3.2.1.39) from the hyperthermophilic archaeon Pyrococcus furiosus (pfLamA) has been determined at 2.1 A resolution by molecular replacement. The pfLamA structure reveals a kink of six residues (72-77) at the entrance of the catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic Nocardiopsis sp. strain F96 and Bacillus macerans, two proteins displaying an overall fold similar to that of pfLamA, but with different substrate specificity. A deletion mutant of pfLamA, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan 10 times more efficiently than the wild-type protein, indicating the importance of the kink in substrate preference.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Celulases/química
Pyrococcus furiosus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bacillus/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Cálcio/metabolismo
Catálise
Celulases/genética
Celulases/metabolismo
Cristalografia por Raios X
Modelos Moleculares
Dados de Sequência Molecular
Mutação
Nocardiaceae/enzimologia
Conformação Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.2.1.- (Cellulases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:0903
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090122
[St] Status:MEDLINE
[do] DOI:10.1111/j.1742-4658.2008.06848.x



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