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  1 / 15 MEDLINE  
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[PMID]:28640638
[Au] Autor:Robbins JM; Souffrant MG; Hamelberg D; Gadda G; Bommarius AS
[Ad] Endereço:School of Chemical and Biomolecular Engineering, Georgia Institute of Technology , Atlanta, Georgia 30332-0100, United States.
[Ti] Título:Enzyme-Mediated Conversion of Flavin Adenine Dinucleotide (FAD) to 8-Formyl FAD in Formate Oxidase Results in a Modified Cofactor with Enhanced Catalytic Properties.
[So] Source:Biochemistry;56(29):3800-3807, 2017 Jul 25.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Flavins, including flavin adenine dinucleotide (FAD), are fundamental catalytic cofactors that are responsible for the redox functionality of a diverse set of proteins. Alternatively, modified flavin analogues are rarely found in nature as their incorporation typically results in inactivation of flavoproteins, thus leading to the disruption of important cellular pathways. Here, we report that the fungal flavoenzyme formate oxidase (FOX) catalyzes the slow conversion of noncovalently bound FAD to 8-formyl FAD and that this conversion results in a nearly 10-fold increase in formate oxidase activity. Although the presence of an enzyme-bound 8-formyl FMN has been reported previously as a result of site-directed mutagenesis studies of lactate oxidase, FOX is the first reported case of 8-formyl FAD in a wild-type enzyme. Therefore, the formation of the 8-formyl FAD cofactor in formate oxidase was investigated using steady-state kinetics, site-directed mutagenesis, ultraviolet-visible, circular dichroism, and fluorescence spectroscopy, liquid chromatography with mass spectrometry, and computational analysis. Surprisingly, the results from these studies indicate not only that 8-formyl FAD forms spontaneously and results in the active form of FOX but also that its autocatalytic formation is dependent on a nearby arginine residue, R87. Thus, this work describes a new enzyme cofactor and provides insight into the little-understood mechanism of enzyme-mediated 8α-flavin modifications.
[Mh] Termos MeSH primário: Aspergillus oryzae/enzimologia
Coenzimas/química
Flavina-Adenina Dinucleotídeo/química
Proteínas Fúngicas/química
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/química
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Aspergillus oryzae/genética
Dicroísmo Circular
Coenzimas/metabolismo
Mononucleotídeo de Flavina/química
Mononucleotídeo de Flavina/metabolismo
Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Cinética
Mutagênese Sítio-Dirigida
Mutação de Sentido Incorreto
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (8-formylflavin mononucleotide); 0 (Coenzymes); 0 (Fungal Proteins); 146-14-5 (Flavin-Adenine Dinucleotide); 7N464URE7E (Flavin Mononucleotide); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00335


  2 / 15 MEDLINE  
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[PMID]:26884484
[Au] Autor:Takagi D; Ifuku K; Ikeda K; Inoue KI; Park P; Tamoi M; Inoue H; Sakamoto K; Saito R; Miyake C
[Ad] Endereço:Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science (D.T., K.-i.I., K.I.I., P.P., H.I., K.S., R.S., C.M.), and Center for Support to Research and Education Activities (P.P.), Kobe University, Nada, Kobe 657-8501, Japan;Division of Integ
[Ti] Título:Suppression of Chloroplastic Alkenal/One Oxidoreductase Represses the Carbon Catabolic Pathway in Arabidopsis Leaves during Night.
[So] Source:Plant Physiol;170(4):2024-39, 2016 04.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lipid-derived reactive carbonyl species (RCS) possess electrophilic moieties and cause oxidative stress by reacting with cellular components. Arabidopsis (Arabidopsis thaliana) has a chloroplast-localized alkenal/one oxidoreductase (AtAOR) for the detoxification of lipid-derived RCS, especially α,ß-unsaturated carbonyls. In this study, we aimed to evaluate the physiological importance of AtAOR and analyzed AtAOR (aor) mutants, including a transfer DNA knockout, aor (T-DNA), and RNA interference knockdown, aor (RNAi), lines. We found that both aor mutants showed smaller plant sizes than wild-type plants when they were grown under day/night cycle conditions. To elucidate the cause of the aor mutant phenotype, we analyzed the photosynthetic rate and the respiration rate by gas-exchange analysis. Subsequently, we found that both wild-type and aor (RNAi) plants showed similar CO2 assimilation rates; however, the respiration rate was lower in aor (RNAi) than in wild-type plants. Furthermore, we revealed that phosphoenolpyruvate carboxylase activity decreased and starch degradation during the night was suppressed in aor (RNAi). In contrast, the phenotype of aor (RNAi) was rescued when aor (RNAi) plants were grown under constant light conditions. These results indicate that the smaller plant sizes observed in aor mutants grown under day/night cycle conditions were attributable to the decrease in carbon utilization during the night. Here, we propose that the detoxification of lipid-derived RCS by AtAOR in chloroplasts contributes to the protection of dark respiration and supports plant growth during the night.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Carbono/metabolismo
Cloroplastos/enzimologia
Escuridão
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
Oxirredutases/metabolismo
Folhas de Planta/enzimologia
Supressão Genética
[Mh] Termos MeSH secundário: Acroleína/metabolismo
Arabidopsis/genética
Arabidopsis/efeitos da radiação
Proteínas de Arabidopsis/genética
Respiração Celular/efeitos da radiação
Clorofila/metabolismo
Cloroplastos/efeitos da radiação
DNA Bacteriano/genética
Regulação da Expressão Gênica de Plantas/efeitos da radiação
Luz
Mutação/genética
Nitrogênio/metabolismo
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Fenótipo
Fotossíntese
Extratos Vegetais/metabolismo
Folhas de Planta/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Amido/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (DNA, Bacterial); 0 (Plant Extracts); 0 (T-DNA); 1406-65-1 (Chlorophyll); 7440-44-0 (Carbon); 7864XYD3JJ (Acrolein); 9005-25-8 (Starch); EC 1.- (Oxidoreductases); EC 1.2.- (AOR protein, Arabidopsis); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors); N762921K75 (Nitrogen)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160218
[St] Status:MEDLINE
[do] DOI:10.1104/pp.15.01572


  3 / 15 MEDLINE  
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[PMID]:26222439
[Au] Autor:Giménez-Dejoz J; Kolár MH; Ruiz FX; Crespo I; Cousido-Siah A; Podjarny A; Barski OA; Fanfrlík J; Parés X; Farrés J; Porté S
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Faculty of Biosciences, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain.
[Ti] Título:Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase.
[So] Source:PLoS One;10(7):e0134506, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human aldo-keto reductase 1B15 (AKR1B15) is a newly discovered enzyme which shares 92% amino acid sequence identity with AKR1B10. While AKR1B10 is a well characterized enzyme with high retinaldehyde reductase activity, involved in the development of several cancer types, the enzymatic activity and physiological role of AKR1B15 are still poorly known. Here, the purified recombinant enzyme has been subjected to substrate specificity characterization, kinetic analysis and inhibitor screening, combined with structural modeling. AKR1B15 is active towards a variety of carbonyl substrates, including retinoids, with lower kcat and Km values than AKR1B10. In contrast to AKR1B10, which strongly prefers all-trans-retinaldehyde, AKR1B15 exhibits superior catalytic efficiency with 9-cis-retinaldehyde, the best substrate found for this enzyme. With ketone and dicarbonyl substrates, AKR1B15 also shows higher catalytic activity than AKR1B10. Several typical AKR inhibitors do not significantly affect AKR1B15 activity. Amino acid substitutions clustered in loops A and C result in a smaller, more hydrophobic and more rigid active site in AKR1B15 compared with the AKR1B10 pocket, consistent with distinct substrate specificity and narrower inhibitor selectivity for AKR1B15.
[Mh] Termos MeSH primário: Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
Retinaldeído/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/antagonistas & inibidores
Aldeído Redutase/genética
Aldeído Redutase/metabolismo
Sequência de Aminoácidos
Substituição de Aminoácidos
Domínio Catalítico/genética
Inibidores Enzimáticos/farmacologia
Seres Humanos
Cinética
Modelos Moleculares
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/antagonistas & inibidores
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Conformação Proteica
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia Estrutural de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Recombinant Proteins); 514-85-2 (9-cis-retinal); EC 1.1.1.- (AKR1B10 protein, human); EC 1.1.1.- (AKR1B15 protein, human); EC 1.1.1.21 (Aldehyde Reductase); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors); RR725D715M (Retinaldehyde)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150730
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0134506


  4 / 15 MEDLINE  
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[PMID]:25577493
[Au] Autor:Weber S; Salabei JK; Möller G; Kremmer E; Bhatnagar A; Adamski J; Barski OA
[Ad] Endereço:From the Helmholtz Zentrum Muenchen, German Research Center for Environmental Health, Institute of Experimental Genetics, Genome Analysis Center, 85764 Neuherberg, Germany.
[Ti] Título:Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto reductase with activity toward steroids and 3-keto-acyl-CoA conjugates.
[So] Source:J Biol Chem;290(10):6531-45, 2015 Mar 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aldo-keto reductases (AKRs) comprise a superfamily of proteins involved in the reduction and oxidation of biogenic and xenobiotic carbonyls. In humans, at least 15 AKR superfamily members have been identified so far. One of these is a newly identified gene locus, AKR1B15, which clusters on chromosome 7 with the other human AKR1B subfamily members (i.e. AKR1B1 and AKR1B10). We show that alternative splicing of the AKR1B15 gene transcript gives rise to two protein isoforms with different N termini: AKR1B15.1 is a 316-amino acid protein with 91% amino acid identity to AKR1B10; AKR1B15.2 has a prolonged N terminus and consists of 344 amino acid residues. The two gene products differ in their expression level, subcellular localization, and activity. In contrast with other AKR enzymes, which are mostly cytosolic, AKR1B15.1 co-localizes with the mitochondria. Kinetic studies show that AKR1B15.1 is predominantly a reductive enzyme that catalyzes the reduction of androgens and estrogens with high positional selectivity (17ß-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoA conjugates and exhibits strong cofactor selectivity toward NADP(H). In accordance with its substrate spectrum, the enzyme is expressed at the highest levels in steroid-sensitive tissues, namely placenta, testis, and adipose tissue. Placental and adipose expression could be reproduced in the BeWo and SGBS cell lines, respectively. In contrast, AKR1B15.2 localizes to the cytosol and displays no enzymatic activity with the substrates tested. Collectively, these results demonstrate the existence of a novel catalytically active AKR, which is associated with mitochondria and expressed mainly in steroid-sensitive tissues.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Processamento Alternativo/genética
Mitocôndrias/enzimologia
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
Esteroides/metabolismo
[Mh] Termos MeSH secundário: Acil Coenzima A/genética
Tecido Adiposo/metabolismo
Sequência de Aminoácidos
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Cinética
Mitocôndrias/metabolismo
Oxirredução
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Protein Isoforms); 0 (Steroids); EC 1.1.1.- (AKR1B15 protein, human); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150112
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.610121


  5 / 15 MEDLINE  
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[PMID]:25538260
[Au] Autor:Shen Y; Ma J; Yan R; Ling H; Li X; Yang W; Gao J; Huang C; Bu Y; Cao Y; He Y; Wan L; Zu X; Liu J; Huang MC; Stenson WF; Liao DF; Cao D
[Ad] Endereço:Department of Medical Microbiology, Immunology and Cell Biology, Simmons Cancer Institute, Southern Illinois University School of Medicine, Springfield, Illinois.
[Ti] Título:Impaired self-renewal and increased colitis and dysplastic lesions in colonic mucosa of AKR1B8-deficient mice.
[So] Source:Clin Cancer Res;21(6):1466-76, 2015 Mar 15.
[Is] ISSN:1078-0432
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Ulcerative colitis and colitis-associated colorectal cancer (CAC) is a serious health issue, but etiopathological factors remain unclear. Aldo-keto reductase 1B10 (AKR1B10) is specifically expressed in the colonic epithelium, but downregulated in colorectal cancer. This study was aimed to investigate the etiopathogenic role of AKR1B10 in ulcerative colitis and CAC. EXPERIMENTAL DESIGN: Ulcerative colitis and CAC biopsies (paraffin-embedded sections) and frozen tissues were collected to examine AKR1B10 expression. Aldo-keto reductase 1B8 (the ortholog of human AKR1B10) knockout (AKR1B8(-/-)) mice were produced to estimate its role in the susceptibility and severity of chronic colitis and associated dysplastic lesions, induced by dextran sulfate sodium (DSS) at a low dose (2%). Genome-wide exome sequencing was used to profile DNA damage in DSS-induced colitis and tumors. RESULTS: AKR1B10 expression was markedly diminished in over 90% of ulcerative colitis and CAC tissues. AKR1B8 deficiency led to reduced lipid synthesis from butyrate and diminished proliferation of colonic epithelial cells. The DSS-treated AKR1B8(-/-) mice demonstrated impaired injury repair of colonic epithelium and more severe bleeding, inflammation, and ulceration. These AKR1B8(-/-) mice had more severe oxidative stress and DNA damage, and dysplasias were more frequent and at a higher grade in the AKR1B8(-/-) mice than in wild-type mice. Palpable masses were seen in the AKR1B8(-/-) mice only, not in wild-type. CONCLUSIONS: AKR1B8 is a critical protein in the proliferation and injury repair of the colonic epithelium and in the pathogenesis of ulcerative colitis and CAC, being a new etiopathogenic factor of these diseases.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/genética
Colite Ulcerativa/patologia
Colo/patologia
Mucosa Intestinal/patologia
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/biossíntese
Oxirredutases do Álcool/metabolismo
Animais
Sequência de Bases
Proliferação Celular
Transformação Celular Neoplásica/genética
Colite Ulcerativa/induzido quimicamente
Neoplasias Colorretais/patologia
Dano ao DNA/genética
Sulfato de Dextrana
Modelos Animais de Doenças
Células Epiteliais/metabolismo
Seres Humanos
Inflamação/genética
Inflamação/imunologia
Inflamação/patologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Estresse Oxidativo/genética
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/biossíntese
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Espécies Reativas de Oxigênio/metabolismo
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (AKR1B8 protein, mouse); 0 (Reactive Oxygen Species); 9042-14-2 (Dextran Sulfate); EC 1.1.- (Alcohol Oxidoreductases); EC 1.2.- (Akr1b10 protein, mouse); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141225
[St] Status:MEDLINE
[do] DOI:10.1158/1078-0432.CCR-14-2072


  6 / 15 MEDLINE  
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[PMID]:24753388
[Au] Autor:Palmberger D; Ashjaei K; Strell S; Hoffmann-Sommergruber K; Grabherr R
[Ad] Endereço:Vienna Institute of BioTechnology - VIBT, University of Natural Resources and Life Sciences, Vienna, Austria.
[Ti] Título:Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy.
[So] Source:Biotechnol J;9(9):1206-14, 2014 Sep.
[Is] ISSN:1860-7314
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The baculovirus/insect cell system has proven to be a very powerful tool for the expression of several therapeutics. Nevertheless, these products sometimes suffer from reduced biological activity and unwanted side effects. Several studies have demonstrated that glycosylation can greatly influence the structure, function, half-life, antigenicity and immunogenicity of various glycoproteins. Yet, the glycosylation pattern of insect cell-derived products is not favorable for many applications. Especially, the presence of core α1,3-linked fucose bears the risk of causing immediate hypersensitivity reactions in patients with allergy. In this study, we evaluated the impact of fucose residues on the allergenic potential of an insect cell-expressed vaccine candidate. In order to block the GDP-L-fucose de novo synthesis pathway, we integrated the Pseudomonas aeruginosa GDP-6-deoxy-D-lyxo-4-hexulose reductase (RMD) gene into a baculovirus backbone. This virus was then used for the expression of soluble influenza A virus hemagglutinin (HA). Expression studies showed that the co-expression of RMD did not influence the overall level of recombinant protein secretion. We confirmed the result of our strategy by analyzing PNGase A-released N-glycans using MALDI-TOF-MS. In order to evaluate the biological impact of defucosylation of influenza HA we tested the binding activity of IgE derived from the sera of patients with allergy to the purified antigen. The non-fucosylated HA showed a 10-fold decrease in IgE binding levels as compared to wildtype variants.
[Mh] Termos MeSH primário: Anticorpos/imunologia
Fucose/metabolismo
Glicoproteínas/imunologia
Hipersensibilidade/imunologia
Soros Imunes/imunologia
Imunoglobulina E/imunologia
Insetos/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos/metabolismo
Antígenos/imunologia
Antígenos/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Baculoviridae/genética
Baculoviridae/metabolismo
Fucose/imunologia
Glicoproteínas/metabolismo
Glicosilação
Hemaglutininas/genética
Hemaglutininas/metabolismo
Seres Humanos
Hipersensibilidade/metabolismo
Imunoglobulina E/metabolismo
Vírus da Influenza A/metabolismo
Vacinas contra Influenza/imunologia
Vacinas contra Influenza/metabolismo
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
Pseudomonas aeruginosa/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/metabolismo
Células Sf9
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies); 0 (Antigens); 0 (Bacterial Proteins); 0 (Glycoproteins); 0 (Hemagglutinins); 0 (Immune Sera); 0 (Influenza Vaccines); 0 (Recombinant Proteins); 28RYY2IV3F (Fucose); 37341-29-0 (Immunoglobulin E); EC 1.2.- (GDP-6-deoxy-D-lyxo-4-hexulose reductase); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140423
[St] Status:MEDLINE
[do] DOI:10.1002/biot.201400061


  7 / 15 MEDLINE  
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[PMID]:24192347
[Au] Autor:Hu XQ; Guo PC; Ma JD; Li WF
[Ad] Endereço:College of Life and Environment Science, Huangshan University, Huangshan, Anhui 245041, People's Republic of China.
[Ti] Título:Structures of Saccharomyces cerevisiae D-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition.
[So] Source:Acta Crystallogr Sect F Struct Biol Cryst Commun;69(Pt 11):1190-5, 2013 Nov.
[Is] ISSN:1744-3091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic α,ß-dicarbonyl compounds using NADPH as a cofactor at physiological pH levels. Here, crystal structures of Ara1 in apo and NADPH-complexed forms are presented at 2.10 and 2.00 Šresolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (α/ß)8-barrel structure and has a highly conserved cofactor-binding pocket. Structural comparison revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. Moreover, the crystal structures combined with computational simulation defined an open substrate-binding site to accommodate various substrates that possess a dicarbonyl group.
[Mh] Termos MeSH primário: NADP/metabolismo
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/química
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Desidrogenase do Álcool de Açúcar/química
Desidrogenase do Álcool de Açúcar/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Biocatálise
Cristalografia por Raios X
Modelos Moleculares
Dados de Sequência Molecular
Multimerização Proteica
Alinhamento de Sequência
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ara1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 53-59-8 (NADP); EC 1.1.- (Sugar Alcohol Dehydrogenases); EC 1.1.1.116 (D-arabinose dehydrogenase); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131107
[St] Status:MEDLINE
[do] DOI:10.1107/S1744309113026857


  8 / 15 MEDLINE  
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[PMID]:24025706
[Au] Autor:Smerdová L; Neca J; Svobodová J; Topinka J; Schmuczerová J; Kozubík A; Machala M; Vondrácek J
[Ad] Endereço:Department of Cytokinetics, Institute of Biophysics AS CR, 61265 Brno, Czech Republic.
[Ti] Título:Inflammatory mediators accelerate metabolism of benzo[a]pyrene in rat alveolar type II cells: the role of enhanced cytochrome P450 1B1 expression.
[So] Source:Toxicology;314(1):30-8, 2013 Dec 06.
[Is] ISSN:1879-3185
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Long-term deregulated inflammation represents one of the key factors contributing to lung cancer etiology. Previously, we have observed that tumor necrosis factor-α (TNF-α), a major pro-inflammatory cytokine, enhances genotoxicity of benzo[a]pyrene (B[a]P), a highly carcinogenic polycyclic aromatic hydrocarbon, in rat lung epithelial RLE-6TN cells, a model of alveolar type II cells. Therefore, we analyzed B[a]P metabolism in RLE-6TN cells under inflammatory conditions, simulated using either recombinant TNF-α, or a mixture of inflammatory mediators derived from activated alveolar macrophage cell line. Inflammatory conditions significantly accelerated BaP metabolism, as evidenced by decreased levels of both parent B[a]P and its metabolites. TNF-α altered production of the metabolites associated with dihydrodiol-epoxide and radical cation pathways of B[a]P metabolism, especially B[a]P-dihydrodiols, and B[a]P-diones. We then evaluated the role of cytochrome P450 1B1 (CYP1B1), which is strongly up-regulated in cells treated with B[a]P under inflammatory conditions, in the observed effects. The siRNA-mediated CYP1B1 knock-down increased levels of B[a]P and reduced formation of stable DNA adducts, thus confirming the essential role of CYP1B1 in B[a]P metabolism under inflammatory conditions. TNF-α also reduced expression of aldo-keto reductase 1C14, which may compete with CYP1B1 for B[a]P-7,8-dihydrodiol and divert it from the formation of ultimate B[a]P dihydrodiol epoxide. Together, the present data suggests that the CYP1B1-catalyzed metabolism of polycyclic aromatic hydrocarbons might contribute to their enhanced bioactivation and genotoxic effects under inflammatory conditions.
[Mh] Termos MeSH primário: Hidrocarboneto de Aril Hidroxilases/biossíntese
Benzo(a)pireno/metabolismo
Mediadores da Inflamação/farmacologia
Alvéolos Pulmonares/metabolismo
[Mh] Termos MeSH secundário: Subfamília B de Transportador de Cassetes de Ligação de ATP/biossíntese
Subfamília B de Transportador de Cassetes de Ligação de ATP/genética
Animais
Hidrocarboneto de Aril Hidroxilases/genética
Western Blotting
Linhagem Celular
Meios de Cultivo Condicionados
Citocromo P-450 CYP1B1
Citocinas/metabolismo
Adutos de DNA
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/biossíntese
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Alvéolos Pulmonares/citologia
Alvéolos Pulmonares/efeitos dos fármacos
RNA Interferente Pequeno
Ratos
Reação em Cadeia da Polimerase em Tempo Real
Espectrometria de Massas em Tandem
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ATP Binding Cassette Transporter, Sub-Family B); 0 (Culture Media, Conditioned); 0 (Cytokines); 0 (DNA Adducts); 0 (Inflammation Mediators); 0 (RNA, Small Interfering); 0 (multidrug resistance protein 3); 3417WMA06D (Benzo(a)pyrene); EC 1.14.14.1 (Aryl Hydrocarbon Hydroxylases); EC 1.14.14.1 (Cyp1b1 protein, rat); EC 1.14.14.1 (Cytochrome P-450 CYP1B1); EC 1.2.- (AKR1C15 protein, rat); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130913
[St] Status:MEDLINE


  9 / 15 MEDLINE  
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[PMID]:22575657
[Au] Autor:Yamauchi Y; Hasegawa A; Mizutani M; Sugimoto Y
[Ad] Endereço:Graduate School of Agricultural Science, Kobe University, Kobe, Hyogo, Japan. yamauchi@kobe-u.ac.jp
[Ti] Título:Chloroplastic NADPH-dependent alkenal/one oxidoreductase contributes to the detoxification of reactive carbonyls produced under oxidative stress.
[So] Source:FEBS Lett;586(8):1208-13, 2012 Apr 24.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lipid peroxide-derived reactive carbonyls (RCs) can cause serious damage to plant functions. A chloroplastic NADPH-dependent alkenal/one oxidoreductase (AOR) detoxifies RCs, but its physiological significance remains unknown. In this study, we investigated the biological impacts of AOR using an AOR-knock out Arabidopsis line (aor). Methyl viologen treatment, mainly to enhance photosystem (PS) I-originated reactive oxygen species (ROS) production, caused more severe damage to aor than wild type (Col-0). In contrast, the high light treatment used to enhance PSII-originated ROS production resulted in no difference in PSII damage between Col-0 and aor. In conclusion, AOR can contribute to detoxify stromal RCs produced under oxidative stress.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Cloroplastos/metabolismo
Estresse Oxidativo
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/genética
Arabidopsis/enzimologia
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Cloroplastos/enzimologia
Técnicas de Inativação de Genes
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Complexo de Proteína do Fotossistema I/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Photosystem I Protein Complex); 0 (Reactive Oxygen Species); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (leukotriene B4 12-hydroxydehydrogenase); EC 1.2.- (AOR protein, Arabidopsis); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1207
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120512
[St] Status:MEDLINE
[do] DOI:10.1016/j.febslet.2012.03.013


  10 / 15 MEDLINE  
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[PMID]:21276782
[Au] Autor:Salabei JK; Li XP; Petrash JM; Bhatnagar A; Barski OA
[Ad] Endereço:Diabetes and Obesity Center, School of Medicine, University of Louisville, Louisville, KY 40202, United States.
[Ti] Título:Functional expression of novel human and murine AKR1B genes.
[So] Source:Chem Biol Interact;191(1-3):177-84, 2011 May 30.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The Aldo Keto Reductases (AKRs) are a superfamily of enzymes that catalyze the reduction of biogenic and xenobiotic aldehydes and ketones. AKR1B family has 2 known members in humans and 3 in rodents. Two novel gene loci, hereafter referred to as AKR1B15 in human and Akr1b16 in mouse have been predicted to exist within the AKR1B clusters. AKR1B15 displays 91% and 67% sequence identity with human genes AKR1B10 and AKR1B1, respectively while Akr1b16 shares 82-84% identity with murine Akr1b8 and Akr1b7. We tested the hypothesis that AKR1B15 and Akr1b16 genes are expressed as functional proteins in human and murine tissues, respectively. Using whole tissue mRNA, we were able to clone the full-length open reading frames for AKR1B15 from human eye and testes, and Akr1b16 from murine spleen, demonstrating that these genes are transcriptionally active. The corresponding cDNAs were cloned into pET28a and pIRES-hrGFP-1α vectors for bacterial and mammalian expression, respectively. Both genes were expressed as 36kDa proteins found in the insoluble fraction of bacterial cell lysate. These proteins, expressed in bacteria showed no enzymatic activity. However, lysates from COS-7 cells transfected with AKR1B15 showed a 4.8-fold (with p-nitrobenzaldehyde) and 3.3-fold (with dl-glyceraldehyde) increase in enzyme activity compared with untransfected COS-7 cells. The Akr1b16 transcript was shown to be ubiquitously expressed in murine tissues. Highest levels of transcript were found in heart, spleen, and lung. From these observations we conclude that the predicted AKR1B15 and 1b16 genes are expressed in several murine and human tissues. Further studies are required to elucidate their physiological roles.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bactérias/citologia
Células COS
Cercopithecus aethiops
Clonagem Molecular
Loci Gênicos/genética
Genoma Humano/genética
Seres Humanos
Camundongos
Dados de Sequência Molecular
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/química
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (RNA, Messenger); EC 1.1.1.- (AKR1B15 protein, human); EC 1.2.- (Akr1b10 protein, mouse); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors)
[Em] Mês de entrada:1108
[Cu] Atualização por classe:161122
[Lr] Data última revisão:
161122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110201
[St] Status:MEDLINE
[do] DOI:10.1016/j.cbi.2011.01.020



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