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  1 / 19040 MEDLINE  
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[PMID]:28465173
[Au] Autor:Xue J; Balamurugan S; Li DW; Liu YH; Zeng H; Wang L; Yang WD; Liu JS; Li HY
[Ad] Endereço:Key Laboratory of Eutrophication and Red Tide Prevention of Guangdong Higher Education Institutes, College of Life Science and Technology, Jinan University, Guangzhou 510632, China.
[Ti] Título:Glucose-6-phosphate dehydrogenase as a target for highly efficient fatty acid biosynthesis in microalgae by enhancing NADPH supply.
[So] Source:Metab Eng;41:212-221, 2017 05.
[Is] ISSN:1096-7184
[Cp] País de publicação:Belgium
[La] Idioma:eng
[Ab] Resumo:Oleaginous microalgae have great prospects in the fields of feed, nutrition, biofuel, etc. However, biomass and lipid productivity in microalgae remain a major economic and technological bottleneck. Here we present a novel regulatory target, glucose-6-phosphate dehydrogenase (G6PD) from the pentose phosphate pathway (PPP), in boosting microalgal lipid accumulation. G6PD, involved in the formation of NADPH demanded in fatty acid biosynthesis as reducing power, was characterized in oleaginous microalga Phaeodactylum tricornutum. In G6PD overexpressing microalgae, transcript abundance of G6PD increased by 4.4-fold, and G6PD enzyme activity increased by more than 3.1-fold with enhanced NADPH production. Consequently, the lipid content increased by 2.7-fold and reached up to 55.7% of dry weight, while cell growth was not apparently affected. The fatty acid composition exhibited significant changes, including a remarkable increase in monounsaturated fatty acids C16:1 and C18:1 concomitant with a decrease in polyunsaturated fatty acids C20:5 and C22:6. G6PD was localized to the chloroplast and its overexpression stimulated an increase in the number and size of oil bodies. Proteomic and metabolomic analyzes revealed that G6PD play a key role in regulating pentose phosphate pathway and subsequently upregulating NADPH consuming pathways such as fatty acid synthesis, thus eventually leading to lipid accumulation. Our findings show the critical role of G6PD in microalgal lipid accumulation by enhancing NADPH supply and demonstrate that G6PD is a promising target for metabolic engineering.
[Mh] Termos MeSH primário: Proteínas de Cloroplastos
Diatomáceas
Ácidos Graxos Insaturados
Glucosefosfato Desidrogenase
Microalgas
NADP
[Mh] Termos MeSH secundário: Proteínas de Cloroplastos/genética
Proteínas de Cloroplastos/metabolismo
Diatomáceas/enzimologia
Diatomáceas/metabolismo
Ácidos Graxos Insaturados/biossíntese
Ácidos Graxos Insaturados/genética
Glucose-6-Fosfato/genética
Glucose-6-Fosfato/metabolismo
Glucosefosfato Desidrogenase/genética
Glucosefosfato Desidrogenase/metabolismo
Microalgas/enzimologia
Microalgas/genética
NADP/genética
NADP/metabolismo
Via de Pentose Fosfato/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chloroplast Proteins); 0 (Fatty Acids, Unsaturated); 53-59-8 (NADP); 56-73-5 (Glucose-6-Phosphate); EC 1.1.1.49 (Glucosephosphate Dehydrogenase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  2 / 19040 MEDLINE  
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[PMID]:28461575
[Au] Autor:Phuc NM; Wu Z; O Y; Lee JH; Oh S; Song GY; Liu KH
[Ad] Endereço:BK21 Plus KNU Multi-Omics-Based Creative Drug Research Team, College of Pharmacy and Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu, Korea (N.M.P., Z.W., K.-H.L.); College of Pharmacy, Chungnam National University, Daejeon, Korea (Y.O., J.-H.L., G.-Y.S.); and Dep
[Ti] Título:LKY-047: First Selective Inhibitor of Cytochrome P450 2J2.
[So] Source:Drug Metab Dispos;45(7):765-769, 2017 Jul.
[Is] ISSN:1521-009X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Highly selective cytochrome P450 CYP2J2 (CYP2J2) inhibitors suitable for reaction phenotyping are currently not available. (7 )-(+)-(4-Nitro-phenyl)-acrylic acid, 8,8-dimethyl-2-oxo-6,7-dihydro- -pyrano[3,2-g]chromen-7-yl-ester (LKY-047), a decursin derivative, was synthesized, and its inhibitor potencies toward CYP2J2 as well as other cytochrome P450 (P450) enzymes in human liver microsomes (HLM) were evaluated. LKY-047 was demonstrated to be a strong competitive inhibitor of CYP2J2-mediated astemizole -demethylase and terfenadine hydroxylase activity, with values of 0.96 and 2.61 M, respectively. It also acted as an uncompetitive inhibitor of CYP2J2-mediated ebastine hydroxylation with a value of 3.61 M. Preincubation of LKY-047 with HLMs and NADPH did not alter inhibition potency, indicating that it is not a mechanism-based inhibitor. LKY-047 was found to be a selective CYP2J2 inhibitor with no inhibitory effect on other human P450s, such as CYPs 1A2, 2A6, 2B6, 2C8, 2C9, 2C19, 2D6, 2E1, and 3A (IC > 50 M). These in vitro data support the use of LKY-047 as a selective CYP2J2 inhibitor with potential application in the identification of P450 isoforms responsible for drug metabolism in reaction phenotyping assays.
[Mh] Termos MeSH primário: Inibidores das Enzimas do Citocromo P-450/farmacologia
Sistema Enzimático do Citocromo P-450/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
Hidroxilação/efeitos dos fármacos
Inativação Metabólica/efeitos dos fármacos
Microssomos Hepáticos/efeitos dos fármacos
Microssomos Hepáticos/metabolismo
NADP/metabolismo
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome P-450 Enzyme Inhibitors); 0 (Protein Isoforms); 53-59-8 (NADP); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.14.14.1 (arachidonate epoxygenase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1124/dmd.117.075036


  3 / 19040 MEDLINE  
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[PMID]:29199984
[Au] Autor:Law A; Stergioulis A; Halavaty AS; Minasov G; Anderson WF; Kuhn ML
[Ad] Endereço:Department of Chemistry and Biochemistry, San Francisco State University, USA.
[Ti] Título:Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD).
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 12):644-650, 2017 Dec 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacillus anthracis is the causative agent of the deadly disease Anthrax. Its use in bioterrorism and its ability to re-emerge have brought renewed interest in this organism. B. anthracis is a Gram-positive bacterium that adds L-rhamnose to its cell-wall polysaccharides using the activated donor dTDP-ß-L-rhamnose. The enzymes involved in the biosynthesis of the activated donor are absent in humans, which make them ideal targets for therapeutic development to combat pathogens. Here, the 2.65 Šresolution crystal structure of the fourth enzyme in the dTDP-ß-L-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro-ß-L-rhamnose reductase (RfbD), is presented in complex with NADP . This enzyme catalyzes the reduction of dTDP-4-dehydro-ß-L-rhamnose to dTDP-ß-L-rhamnose. Although the protein was co-crystallized in the presence of Mg , the protein lacks the conserved residues that coordinate Mg .
[Mh] Termos MeSH primário: Bacillus anthracis/enzimologia
Proteínas de Bactérias/química
Desidrogenases de Carboidrato/química
Desidrogenases de Carboidrato/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Desidrogenases de Carboidrato/genética
Cristalografia por Raios X
Magnésio/metabolismo
Modelos Moleculares
NADP/química
NADP/metabolismo
Açúcares de Nucleosídeo Difosfato/metabolismo
Conformação Proteica
Multimerização Proteica
Homologia Estrutural de Proteína
Especificidade por Substrato
Nucleotídeos de Timina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Nucleoside Diphosphate Sugars); 0 (Thymine Nucleotides); 2147-59-3 (thymidine diphosphate rhamnose); 53-59-8 (NADP); EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.1.133 (dTDP-4-dehydrorhamnose reductase); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17015746


  4 / 19040 MEDLINE  
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[PMID]:28470513
[Au] Autor:Präbst K; Engelhardt H; Ringgeler S; Hübner H
[Ad] Endereço:Institute of Bioprocess Engineering, Friedrich-Alexander University Erlangen-Nürnberg, Paul-Gordan-Str. 3, 91052, Erlangen, Germany. konstantin.praebst@fau.de.
[Ti] Título:Basic Colorimetric Proliferation Assays: MTT, WST, and Resazurin.
[So] Source:Methods Mol Biol;1601:1-17, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This chapter describes selected assays for the evaluation of cellular viability and proliferation of cell cultures. The underlying principle of these assays is the measurement of a biochemical marker to evaluate the cell's metabolic activity. The formation of the omnipresent reducing agents NADH and NADPH is used as a marker for metabolic activity in the following assays. Using NADH and NADPH as electron sources, specific dyes are biochemically reduced which results in a color change that can be determined with basic photometrical methods. The assays selected for this chapter include MTT, WST, and resazurin. They are applicable for adherent or suspended cell lines, easy to perform, and comparably economical. Detailed protocols and notes for easier handling and avoiding pitfalls are enclosed to each assay.
[Mh] Termos MeSH primário: Contagem de Células/métodos
Proliferação Celular
Sobrevivência Celular
Colorimetria/métodos
Indicadores e Reagentes/química
Oxazinas/química
Sais de Tetrazólio/química
Tiazóis/química
Xantenos/química
[Mh] Termos MeSH secundário: Bioensaio
Calibragem
Células HeLa
Seres Humanos
NAD/análise
NADP/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-(2-methoxy-4-nitrophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H tetrazolium monosodium salt); 0 (Indicators and Reagents); 0 (Oxazines); 0 (Tetrazolium Salts); 0 (Thiazoles); 0 (Xanthenes); 0U46U6E8UK (NAD); 1FN9YD6968 (resazurin); 53-59-8 (NADP); EUY85H477I (thiazolyl blue)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6960-9_1


  5 / 19040 MEDLINE  
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[PMID]:28821467
[Au] Autor:Kim J; Lee PG; Jung EO; Kim BG
[Ad] Endereço:Department of Chemical and Biological Engineering, Seoul National University, Seoul, 08826, Republic of Korea.
[Ti] Título:In vitro characterization of CYP102G4 from Streptomyces cattleya: A self-sufficient P450 naturally producing indigo.
[So] Source:Biochim Biophys Acta;1866(1):60-67, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Self-sufficient CYP102As possess outstanding hydroxylating activity to fatty acids such as myristic acid. Other CYP102 subfamily members share substrate specificity of CYP102As, but, occasionally, unusual characteristics of its own subfamily have been found. In this study, only one self-sufficient cytochrome P450 from Streptomyces cattleya was renamed from CYP102A_scat to CYP102G4, purified and characterized. UV-Vis spectrometry pattern, FAD/FMN analysis, and protein sequence comparison among CYP102s have shown that CYP102 from Streptomyces cattleya belongs to CYP102G subfamily. It showed hydroxylation activity toward fatty acids generating ω-1, ω-2, and ω-3-hydroxyfatty acids, which is similar to the general substrate specificity of CYP102 family. Unexpectedly, however, expression of CYP102G4 showed indigo production in LB medium batch flask culture, and high catalytic activity (k /K ) for indole was measured as 6.14±0.10min mM . Besides indole, CYP102G4 was able to hydroxylate aromatic compounds such as flavone, benzophenone, and chloroindoles. Homology model has shown such ability to accept aromatic compounds is due to its bigger active site cavity. Unlike other CYP102s, CYP102G4 did not have biased cofactor dependency, which was possibly determined by difference in NAD(P)H binding residues (Ala984, Val990, and Tyr1064) compared to CYP102A1 (Arg966, Lys972 and Trp1046). Overall, a self-sufficient CYP within CYP102G subfamily was characterized using purified enzymes, which appears to possess unique properties such as an only prokaryotic CYP naturally producing indigo.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Sistema Enzimático do Citocromo P-450/metabolismo
Ácidos Graxos/metabolismo
Índigo Carmim/metabolismo
NADPH-Ferri-Hemoproteína Redutase/metabolismo
Streptomyces/enzimologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Benzofenonas/metabolismo
Domínio Catalítico
Clonagem Molecular
Sistema Enzimático do Citocromo P-450/química
Sistema Enzimático do Citocromo P-450/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Ácidos Graxos/química
Flavonas/metabolismo
Expressão Gênica
Hidroxilação
Indóis/metabolismo
Cinética
Modelos Moleculares
NADP/química
NADP/metabolismo
NADPH-Ferri-Hemoproteína Redutase/química
NADPH-Ferri-Hemoproteína Redutase/genética
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Streptomyces/genética
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 (Bacterial Proteins); 0 (Benzophenones); 0 (Fatty Acids); 0 (Flavones); 0 (Indoles); 0 (Recombinant Proteins); 53-59-8 (NADP); 701M4TTV9O (benzophenone); 8724FJW4M5 (indole); 9035-51-2 (Cytochrome P-450 Enzyme System); D3741U8K7L (Indigo Carmine); EC 1.6.2.4 (NADPH-Ferrihemoprotein Reductase); EC 1.6.2.4 (flavocytochrome P450 BM3 monoxygenases); S2V45N7G3B (flavone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE


  6 / 19040 MEDLINE  
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[PMID]:28739446
[Au] Autor:Panneerselvam S; Shehzad A; Mueller-Dieckmann J; Wilmanns M; Bocola M; Davari MD; Schwaneberg U
[Ad] Endereço:HASYLAB, DESY, Notkestrasse 85, 22603 Hamburg, Germany.
[Ti] Título:Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.
[So] Source:Biochim Biophys Acta;1866(1):134-140, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:P450 BM3 is a multi-domain heme-containing soluble bacterial monooxygenase. P450 BM3 and variants are known to oxidize structurally diverse substrates. Crystal structures of individual domains of P450 BM3 are available. However, the spatial organization of the full-length protein is unknown. In this study, crystal structures of the P450 BM3 M7 heme domain variant with and without cobalt (III) sepulchrate are reported. Cobalt (III) sepulchrate acts as an electron shuttle in an alternative cofactor system employing zinc dust as the electron source. The crystal structure shows a binding site for the mediator cobalt (III) sepulchrate at the entrance of the substrate access channel. The mediator occupies an unusual position which is far from the active site and distinct from the binding of the natural redox partner (FAD/NADPH binding domain).
[Mh] Termos MeSH primário: Bacillus megaterium/química
Proteínas de Bactérias/química
Cobalto/química
Coenzimas/química
Sistema Enzimático do Citocromo P-450/química
Elétrons
Heme/química
NADPH-Ferri-Hemoproteína Redutase/química
NADP/química
[Mh] Termos MeSH secundário: Bacillus megaterium/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cobalto/metabolismo
Coenzimas/metabolismo
Cristalografia por Raios X
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Heme/metabolismo
Modelos Moleculares
NADP/metabolismo
NADPH-Ferri-Hemoproteína Redutase/genética
NADPH-Ferri-Hemoproteína Redutase/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Zinco/química
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Recombinant Proteins); 3G0H8C9362 (Cobalt); 42VZT0U6YR (Heme); 53-59-8 (NADP); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.6.2.4 (NADPH-Ferrihemoprotein Reductase); EC 1.6.2.4 (flavocytochrome P450 BM3 monoxygenases); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  7 / 19040 MEDLINE  
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[PMID]:28578073
[Au] Autor:Baravalle R; Ciaramella A; Baj F; Di Nardo G; Gilardi G
[Ad] Endereço:Department of Life Sciences and Systems Biology, University of Torino, Via Accademia Albertina 13, Torino, Italy.
[Ti] Título:Identification of endocrine disrupting chemicals acting on human aromatase.
[So] Source:Biochim Biophys Acta;1866(1):88-96, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Human aromatase is the cytochrome P450 catalysing the conversion of androgens into estrogens playing a key role in the endocrine system. Due to this role, it is likely to be a target of the so-called endocrine disrupting chemicals, a series of compounds able to interfere with the hormone system with toxic effects. If on one side the toxicity of some compounds such as bisphenol A is well known, on the other side the toxic concentrations of such compounds as well as the effect of the many other molecules that are in contact with us in everyday life still need a deep investigation. The availability of biological assays able to detect the interaction of chemicals with key molecular targets of the endocrine system represents a possible solution to identify potential endocrine disrupting chemicals. Here the so-called alkali assay previously developed in our laboratory is applied to test the effect of different compounds on the activity of human aromatase. The assay is based on the detection of the alkali product that forms upon strong alkali treatment of the NADP released upon enzyme turnover. Here it is applied on human aromatase and validated using anastrozole and sildenafil as known aromatase inhibitors. Out of the small library of compounds tested, resveratrol and ketoconazole resulted to inhibit aromatase activity, while bisphenol A and nicotine were found to exert an inhibitory effect at relatively high concentrations (100µM), and other molecules such as lindane and four plasticizers did not show any significant effect. These data are confirmed by quantification of the product estrone in the same reaction mixtures through ELISA. Overall, the results show that the alkali assay is suitable to screen for molecules that interfere with aromatase activity. As a consequence it can also be applied to other molecular targets of EDCs that use NAD(P)H for catalysis in a high throughput format for the fast screening of many different compounds as endocrine disrupting chemicals. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Inibidores da Aromatase/química
Aromatase/química
Bioensaio
Disruptores Endócrinos/química
[Mh] Termos MeSH secundário: Aromatase/genética
Inibidores da Aromatase/análise
Compostos Benzidrílicos/análise
Compostos Benzidrílicos/química
Disruptores Endócrinos/análise
Ensaio de Imunoadsorção Enzimática
Estrona/química
Expressão Gênica
Seres Humanos
Cetoconazol/análise
Cetoconazol/química
Ligantes
NADP/química
Nicotina/análise
Nicotina/química
Nitrilos/análise
Nitrilos/química
Fenóis/análise
Fenóis/química
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Citrato de Sildenafila/análise
Citrato de Sildenafila/química
Bibliotecas de Moléculas Pequenas/análise
Bibliotecas de Moléculas Pequenas/química
Estilbenos/análise
Estilbenos/química
Triazóis/análise
Triazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aromatase Inhibitors); 0 (Benzhydryl Compounds); 0 (Endocrine Disruptors); 0 (Ligands); 0 (Nitriles); 0 (Phenols); 0 (Recombinant Proteins); 0 (Small Molecule Libraries); 0 (Stilbenes); 0 (Triazoles); 2DI9HA706A (Estrone); 2Z07MYW1AZ (anastrozole); 53-59-8 (NADP); 6M3C89ZY6R (Nicotine); BW9B0ZE037 (Sildenafil Citrate); EC 1.14.14.1 (Aromatase); EC 1.14.14.1 (CYP19A1 protein, human); MLT3645I99 (bisphenol A); Q369O8926L (resveratrol); R9400W927I (Ketoconazole)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170605
[St] Status:MEDLINE


  8 / 19040 MEDLINE  
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[PMID]:28463500
[Au] Autor:Kobylarz MJ; Heieis GA; Loutet SA; Murphy MEP
[Ad] Endereço:The Department of Microbiology and Immunology, Life Sciences Institute, University of British Columbia , Vancouver, British Columbia V6T 1Z3; Canada.
[Ti] Título:Iron Uptake Oxidoreductase (IruO) Uses a Flavin Adenine Dinucleotide Semiquinone Intermediate for Iron-Siderophore Reduction.
[So] Source:ACS Chem Biol;12(7):1778-1786, 2017 Jul 21.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many pathogenic bacteria including Staphylococcus aureus use iron-chelating siderophores to acquire iron. Iron uptake oxidoreductase (IruO), a flavin adenine dinucleotide (FAD)-containing nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reductase from S. aureus, functions as a reductase for IsdG and IsdI, two paralogous heme degrading enzymes. Also, the gene encoding for IruO was shown to be required for growth of S. aureus on hydroxamate siderophores as a sole iron source. Here, we show that IruO binds the hydroxamate-type siderophores desferrioxamine B and ferrichrome A with low micromolar affinity and in the presence of NADPH, Fe(II) was released. Steady-state kinetics of Fe(II) release provides k /K values in the range of 600 to 7000 M s for these siderophores supporting a role for IruO as a siderophore reductase in iron utilization. Crystal structures of IruO were solved in two distinct conformational states mediated by the formation of an intramolecular disulfide bond. A putative siderophore binding site was identified adjacent to the FAD cofactor. This site is partly occluded in the oxidized IruO structure consistent with this form being less active than reduced IruO. This reduction in activity could have a physiological role to limit iron release under oxidative stress conditions. Visible spectroscopy of anaerobically reduced IruO showed that the reaction proceeds by a single electron transfer mechanism through an FAD semiquinone intermediate. From the data, a model for single electron siderophore reduction by IruO using NADPH is described.
[Mh] Termos MeSH primário: Benzoquinonas/química
Flavina-Adenina Dinucleotídeo/química
Ferro/metabolismo
Oxirredutases/metabolismo
Sideróforos/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Sítios de Ligação
Clonagem Molecular
Cristalografia por Raios X
Cinética
Modelos Moleculares
NADP/química
Oxirredução
Oxirredutases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoquinones); 0 (Siderophores); 146-14-5 (Flavin-Adenine Dinucleotide); 3225-29-4 (semiquinone radicals); 53-59-8 (NADP); E1UOL152H7 (Iron); EC 1.- (Oxidoreductases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00203


  9 / 19040 MEDLINE  
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[PMID]:29177972
[Au] Autor:Hanukoglu I
[Ad] Endereço:Laboratory of Cell Biology, Ariel University, 40700, Ariel, Israel. mbiochem@gmail.com.
[Ti] Título:Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme.
[So] Source:J Mol Evol;85(5-6):205-218, 2017 Dec.
[Is] ISSN:1432-1432
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:FAD and NAD(P) together represent an ideal pair for coupled redox reactions in their capacity to accept two electrons and their redox potentials. Enzymes that bind both NAD(P) and FAD represent large superfamilies that fulfill essential roles in numerous metabolic pathways. Adrenodoxin reductase (AdxR) shares Rossmann fold features with some of these superfamilies but remains in a group of its own in the absence of sequence homology. This article documents the phylogenetic distribution of AdxR by examining whole genome databases for Metazoa, Plantae, Fungi, and Protista, and determines the conserved structural features of AdxR. Scanning these databases showed that most organisms have a single gene coding for an AdxR ortholog. The sequence identity between AdxR orthologs is correlated with the phylogenetic distance among metazoan species. The NADP binding site of all AdxR orthologs showed a modified Rossmann fold motif with a GxGxxA consensus instead of the classical GxGxxG at the edge of the first ßα-fold. To examine the hypothesis that enzyme-coenzyme interfaces represent the conserved regions of AdxR, the residues interfacing FAD and NADP were identified and compared with multiple-sequence alignment results. Most conserved residues were indeed found at sites that surround the interfacing residues between the enzyme and the two coenzymes. In contrast to protein-protein interaction hot-spots that may appear in isolated patches, in AdxR the conserved regions show strict preservation of the overall structure. This structure maintains the precise positioning of the two coenzymes for optimal electron transfer between NADP and FAD without electron leakage to other acceptors.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/química
Ferredoxina-NADP Redutase/genética
Ferredoxina-NADP Redutase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Coenzimas/metabolismo
Sequência Conservada/genética
Transporte de Elétrons
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/genética
Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas Mitocondriais/metabolismo
Modelos Moleculares
NADP/química
NADP/genética
NADP/metabolismo
Filogenia
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Mitochondrial Proteins); 146-14-5 (Flavin-Adenine Dinucleotide); 53-59-8 (NADP); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1007/s00239-017-9821-9


  10 / 19040 MEDLINE  
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[PMID]:28471355
[Au] Autor:Wang R; Wu J; Jin DK; Chen Y; Lv Z; Chen Q; Miao Q; Huo X; Wang F
[Ad] Endereço:Wuxi Biortus Biosciences Co. Ltd, A5, 6 Dongsheng West Road, 214437 Jiangyin, Jiangsu, People's Republic of China.
[Ti] Título:Structure of NADP -bound 7ß-hydroxysteroid dehydrogenase reveals two cofactor-binding modes.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):246-252, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In mammals, bile acids/salts and their glycine and taurine conjugates are effectively recycled through enterohepatic circulation. 7ß-Hydroxysteroid dehydrogenases (7ß-HSDHs; EC 1.1.1.201), including that from the intestinal microbe Collinsella aerofaciens, catalyse the NADPH-dependent reversible oxidation of secondary bile-acid products to avoid potential toxicity. Here, the first structure of NADP bound to dimeric 7ß-HSDH is presented. In one active site, NADP adopts a conventional binding mode similar to that displayed in related enzyme structures. However, in the other active site a unique binding mode is observed in which the orientation of the nicotinamide is different. Since 7ß-HSDH has become an attractive target owing to the wide and important pharmaceutical use of its product ursodeoxycholic acid, this work provides a more detailed template to support rational protein engineering to improve the enzymatic activities of this useful biocatalyst, further improving the yield of ursodeoxycholic acid and its other applications.
[Mh] Termos MeSH primário: Actinobacteria/química
Proteínas de Bactérias/química
Hidroxiesteroide Desidrogenases/química
NADP/química
Ácido Ursodesoxicólico/química
[Mh] Termos MeSH secundário: Actinobacteria/enzimologia
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Hidroxiesteroide Desidrogenases/genética
Hidroxiesteroide Desidrogenases/metabolismo
Modelos Moleculares
NADP/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ácido Ursodesoxicólico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 53-59-8 (NADP); 724L30Y2QR (Ursodeoxycholic Acid); EC 1.1.- (Hydroxysteroid Dehydrogenases); EC 1.1.1.- (7 beta-hydroxysteroid dehydrogenase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17004460



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