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[PMID]:28734978
[Au] Autor:Kranz-Finger S; Mahmoud O; Ricklefs E; Ditz N; Bakkes PJ; Urlacher VB
[Ad] Endereço:Institute of Biochemistry, Heinrich-Heine University Düsseldorf, Universitätsstr. 1, 40225 Düsseldorf, Germany; Cluster of Excellence on Plant Sciences, Heinrich-Heine University Düsseldorf, Universitätsstr. 1, 40225 Düsseldorf, Germany.
[Ti] Título:Insights into the functional properties of the marneral oxidase CYP71A16 from Arabidopsis thaliana.
[So] Source:Biochim Biophys Acta;1866(1):2-10, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The Arabidopsis thaliana gene encoding CYP71A16 is part of the gene cluster for the biosynthesis and modification of the triterpenoid marneral. Previous investigations of A. thaliana have revealed that CYP71A16 catalyzes marneral oxidation, while it also can accept marnerol as substrate. The aim of the present study was to investigate functional properties of CYP71A16 in vitro. For this purpose, heterologous expression of a N-terminally modified version of CYP71A16 was established in Escherichia coli, which yielded up to 50mgL recombinant enzyme. The enzyme was purified and activity was reconstituted in vitro with different redox partners. A heterologous bacterial redox partner system consisting of the flavodoxin YkuN from Bacillus subtilis and the flavodoxin reductase Fpr from E. coli clearly outperformed the cytochrome P450 reductase ATR2 from A. thaliana in supporting the CYP71A16-mediated hydroxylation of marnerol. Substrate binding experiments with CYP71A16 revealed a dissociation constant K of 225µM for marnerol. CYP71A16 catalyzed the hydroxylation of marnerol to 23-hydroxymarnerol with a K of 142µM and a k of 3.9min . Furthermore, GC/MS analysis revealed an as of yet unidentified overoxidation product of this in vitro reaction. 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: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Bacillus subtilis/enzimologia
Sistema Enzimático do Citocromo P-450/metabolismo
Proteínas de Escherichia coli/metabolismo
Ferredoxina-NADP Redutase/metabolismo
Flavodoxina/metabolismo
Triterpenos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/química
Proteínas de Arabidopsis/genética
Bacillus subtilis/química
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Clonagem Molecular
Sistema Enzimático do Citocromo P-450/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Ferredoxina-NADP Redutase/genética
Flavodoxina/genética
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Hidroxilação
Cinética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ATR2 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Escherichia coli Proteins); 0 (Flavodoxin); 0 (Recombinant Proteins); 0 (Triterpenes); 0 (marneral); 117385-73-6 (fpr protein, E coli); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.- (CYP71A16 protein, Arabidopsis); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[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:170724
[St] Status:MEDLINE


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[PMID]:29221464
[Au] Autor:Vorphal MA; Bruna C; Wandersleben T; Dagnino-Leone J; Lobos-González F; Uribe E; Martínez-Oyanedel J; Bunster M
[Ad] Endereço:Laboratorio de Biofísica Molecular, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Barrio Universitario S/N, Casilla 160_C, Concepción, Chile.
[Ti] Título:Molecular and functional characterization of ferredoxin NADP(H) oxidoreductase from Gracilaria chilensis and its complex with ferredoxin.
[So] Source:Biol Res;50(1):39, 2017 Dec 08.
[Is] ISSN:0717-6287
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUD: Ferredoxin NADP(H) oxidoreductases (EC 1.18.1.2) (FNR) are flavoenzymes present in photosynthetic organisms; they are relevant for the production of reduced donors to redox reactions, i.e. in photosynthesis, the reduction of NADP to NADPH using the electrons provided by Ferredoxin (Fd), a small FeS soluble protein acceptor of electrons from PSI in chloroplasts. In rhodophyta no information about this system has been reported, this work is a contribution to the molecular and functional characterization of FNR from Gracilaria chilensis, also providing a structural analysis of the complex FNR/Fd. METHODS: The biochemical and kinetic characterization of FNR was performed from the enzyme purified from phycobilisomes enriched fractions. The sequence of the gene that codifies for the enzyme, was obtained using primers designed by comparison with sequences of Synechocystis and EST from Gracilaria. 5'RACE was used to confirm the absence of a CpcD domain in FNRPBS of Gracilaria chilensis. A three dimensional model for FNR and Fd, was built by comparative modeling and a model for the complex FNR: Fd by docking. RESULTS: The kinetic analysis shows K of 12.5 M and a k of 86 s , data consistent with the parameters determined for the enzyme purified from a soluble extract. The sequence for FNR was obtained and translated to a protein of 33646 Da. A FAD and a NADP+ binding domain were clearly identified by sequence analysis as well as a chloroplast signal sequence. Phycobilisome binding domain, present in some cyanobacteria was absent. Transcriptome analysis of Gch revealed the presence of two Fd; FdL and FdS , sharing the motif CX5CX2CX29X. The analysis indicated that the most probable partner for FNR is FdS. CONCLUSION: The interaction model produced, was consistent with functional properties reported for FNR in plants leaves, and opens the possibilities for research in other rhodophyta of commercial interest.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/química
Ferredoxinas/metabolismo
Gracilaria/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Eletroforese em Gel de Poliacrilamida
Ferredoxina-NADP Redutase/genética
Ferredoxina-NADP Redutase/farmacocinética
Gracilaria/química
Oxirredução
Fotossíntese/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ferredoxins); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171210
[St] Status:MEDLINE
[do] DOI:10.1186/s40659-017-0144-5


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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


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[PMID]:28965846
[Au] Autor:Paul A; Drecourt A; Petit F; Deguine DD; Vasnier C; Oufadem M; Masson C; Bonnet C; Masmoudi S; Mosnier I; Mahieu L; Bouccara D; Kaplan J; Challe G; Domange C; Mochel F; Sterkers O; Gerber S; Nitschke P; Bole-Feysot C; Jonard L; Gherbi S; Mercati O; Ben Aissa I; Lyonnet S; Rötig A; Delahodde A; Marlin S
[Ad] Endereço:UMR 1163, Université Paris Descartes, Sorbonne Paris Cité, Institut IMAGINE, 24 Boulevard du Montparnasse, 75015 Paris, France.
[Ti] Título:FDXR Mutations Cause Sensorial Neuropathies and Expand the Spectrum of Mitochondrial Fe-S-Synthesis Diseases.
[So] Source:Am J Hum Genet;101(4):630-637, 2017 Oct 05.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hearing loss and visual impairment in childhood have mostly genetic origins, some of them being related to sensorial neuronal defects. Here, we report on eight subjects from four independent families affected by auditory neuropathy and optic atrophy. Whole-exome sequencing revealed biallelic mutations in FDXR in affected subjects of each family. FDXR encodes the mitochondrial ferredoxin reductase, the sole human ferredoxin reductase implicated in the biosynthesis of iron-sulfur clusters (ISCs) and in heme formation. ISC proteins are involved in enzymatic catalysis, gene expression, and DNA replication and repair. We observed deregulated iron homeostasis in FDXR mutant fibroblasts and indirect evidence of mitochondrial iron overload. Functional complementation in a yeast strain in which ARH1, the human FDXR ortholog, was deleted established the pathogenicity of these mutations. These data highlight the wide clinical heterogeneity of mitochondrial disorders related to ISC synthesis.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/genética
Perda Auditiva Central/genética
Proteínas com Ferro-Enxofre/metabolismo
Ferro/metabolismo
Doenças Mitocondriais/genética
Mutação
Atrofia Óptica/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Sequência de Aminoácidos
Pré-Escolar
Feminino
Ferredoxina-NADP Redutase/química
Ferredoxina-NADP Redutase/metabolismo
Teste de Complementação Genética
Perda Auditiva Central/enzimologia
Perda Auditiva Central/patologia
Seres Humanos
Proteínas com Ferro-Enxofre/genética
Masculino
Mitocôndrias/enzimologia
Mitocôndrias/genética
Mitocôndrias/patologia
Doenças Mitocondriais/enzimologia
Doenças Mitocondriais/patologia
Atrofia Óptica/enzimologia
Atrofia Óptica/patologia
Linhagem
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Alinhamento de Sequência
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Saccharomyces cerevisiae Proteins); E1UOL152H7 (Iron); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171003
[St] Status:MEDLINE


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[PMID]:28783258
[Au] Autor:Kean KM; Carpenter RA; Pandini V; Zanetti G; Hall AR; Faber R; Aliverti A; Karplus PA
[Ad] Endereço:Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA.
[Ti] Título:High-resolution studies of hydride transfer in the ferredoxin:NADP reductase superfamily.
[So] Source:FEBS J;284(19):3302-3319, 2017 Oct.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ferredoxin: NADP reductase (FNR) is an FAD-containing enzyme best known for catalysing the transfer of electrons from ferredoxin (Fd) to NADP to make NADPH during photosynthesis. It is also the prototype for a broad enzyme superfamily, including the NADPH oxidases (NOXs) that all catalyse similar FAD-enabled electron transfers between NAD(P)H and one-electron carriers. Here, we define further mechanistic details of the NAD(P)H ⇌ FAD hydride-transfer step of the reaction based on spectroscopic studies and high-resolution (~ 1.5 Å) crystallographic views of the nicotinamide-flavin interaction in crystals of corn root FNR Tyr316Ser and Tyr316Ala variants soaked with either nicotinamide, NADP , or NADPH. The spectra obtained from FNR crystal complexes match those seen in solution and the complexes reveal active site packing interactions and patterns of covalent distortion of the FAD that imply significant active site compression that would favour catalysis. Furthermore, anisotropic B-factors show that the mobility of the C4 atom of the nicotinamide in the FNR:NADP complex has a directionality matching that expected for boat-like excursions of the nicotinamide ring thought to enhance hydride transfer. Arguments are made for the relevance of this binding mode to catalysis, and specific consideration is given to how the results extrapolate to provide insight to structure-function relations for the membrane-bound NOX enzymes for which little structural information has been available. DATABASES: Structural data are available in the PDB database under the accession numbers 3LO8 (wild-type), 5VW4 [Y316S:nicotinamide (P3 21)], 5VW9 [Y316S:nicotinamide (P3 21)], 5VW3 [Y316S:NADP (P3 21)], 5VW8 [Y316S:NADP (P3 21)], 5VW2 [Y316S:NADPH (P3 21)], 5VW5 [Y316A:nicotinamide (P3 21)], 5VW6 [Y316A:NADP (P3 21)], 5VW7 [Y316A:NADPH (P3 21)], 5VWA [Y316F (P3 21)], and 5VWB [Y316F:NADP (P3 21)]. Enzyme Commission number: ferredoxin:NADP reductase - E C1.18.1.2.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/química
Flavina-Adenina Dinucleotídeo/química
NADPH Oxidases/química
NADP/química
NAD/química
Proteínas de Plantas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Biocatálise
Domínio Catalítico
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Ferredoxina-NADP Redutase/genética
Ferredoxina-NADP Redutase/metabolismo
Flavina-Adenina Dinucleotídeo/metabolismo
Expressão Gênica
Seres Humanos
Cinética
Modelos Moleculares
NAD/metabolismo
NADP/metabolismo
NADPH Oxidases/genética
NADPH Oxidases/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Raízes de Plantas/química
Raízes de Plantas/enzimologia
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Zea mays/química
Zea mays/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Recombinant Proteins); 0U46U6E8UK (NAD); 146-14-5 (Flavin-Adenine Dinucleotide); 53-59-8 (NADP); EC 1.18.1.2 (Ferredoxin-NADP Reductase); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14190


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[PMID]:28778621
[Au] Autor:Hassan FM; Khattab AA; Abo El Fotoh WMM; Zidan RS
[Ad] Endereço:Pediatric department, Faculty of Medicine, Menoufia University Hospitals, Egypt.
[Ti] Título:A66G and C524T polymorphisms of methionine synthase reductase gene are linked to the development of acyanotic congenital heart diseases in Egyptian children.
[So] Source:Gene;629:59-63, 2017 Sep 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Methionine synthase reductase (MTRR) is one of the main regulatory enzymes in the homocysteine/folate pathway. Genes involved in this pathway may play an important role in the development of congenital heart diseases (CHDs). C524T and A66G polymorphisms of MTRR gene may play an imperative role in the development of acyanotic CHDs. This study carried out on 200 children equally divided into 2 groups: group I: 100 children with acyanotic CHDs; and group II: 100 healthy children served as controls. PCR-RFLP method carried out to amplify the A66G and C524T polymorphisms of MTRR gene digested with Xho1and NdeI enzymes. A significant difference(P=0.015) in genotype frequencies of C524T polymorphism between cases and controls, where CC, CT, and TT were 14.0%, 40.0% and 46.0% in patients compared to 38.0,36.0% and 26.0% in controls. Again, a significant difference (P=0.010) in genotype frequencies of A66G polymorphism between the two groups as AA, AG and GG were 26.0%, 32.0% and42.0% in patients compared to 48.0, 36.0% and 16.0% in controls. Also, MTRR A66G and C524T polymorphisms were associated with a higher CHD risk in the homozygote comparison of wild and mutant genotypes and also in heterozygote and mutant comparison. So A66G and C524T polymorphisms of MTRR gene are associated with increased risk of acyanotic CHDs.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/genética
Cardiopatias Congênitas/genética
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Egito
Feminino
Predisposição Genética para Doença
Seres Humanos
Masculino
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.18.1.- (methionine synthase reductase); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE


  7 / 1232 MEDLINE  
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[PMID]:28726667
[Au] Autor:Vasylyev D; Chernobay L; Vasylieva O; Oliinyk M; Vashuk M
[Ad] Endereço:1Kharkiv Medical Academy of Postgraduate Study; 2Kharkiv National Medical University, Ukraine.
[Ti] Título:CLINICAL AND GENETIC PECULIARITIES OF VASCULAR MANIFESTATIONS OF ANTIPHOSPHOLIPID SYNDROME (CASE REPORT).
[So] Source:Georgian Med News;(267):114-119, 2017 Jun.
[Is] ISSN:1512-0112
[Cp] País de publicação:Georgia (Republic)
[La] Idioma:eng
[Ab] Resumo:Pathogenetic mechanisms of the development of antiphospholipid syndrome (APS) are considered in the article, which is the basis for the development of clinical manifestations and laboratory markers of APS. The modern literature data are analyzed, according to which the presence of antiphospholipid antibodies is a hypercoagulable background, and the formation of thrombi occurs under the influence of other allowing procoagulation factors. The classification of the main types of hereditary thrombophilia is given, which is the primary disorder, against the background of which an autoimmune thrombosis APS develops. A clinical observation of a young age patient is given, whose heterozygous carriage of mutations in the genes responsible for blood coagulation (F7, PAI-1 and ITGB3-ß-integrin), as well as homozygous carriage of a mutation in the MTRR gene associated with a violation of homocysteine methylation, APS was developed, which led to the processes of thrombosis. Timely diagnosis and individually developed pathogenetic therapy allow avoiding life-threatening complications of APS and improving the patients' quality of life. A conclusion about the need for APS and hereditary thrombophilias' examination to all patients of young age with unprovoked thrombosis of deep veins of lower extremities and PE was made.
[Mh] Termos MeSH primário: Síndrome Antifosfolipídica/genética
Fator VII/genética
Ferredoxina-NADP Redutase/genética
Integrina beta3/genética
Inibidor 1 de Ativador de Plasminogênio/genética
[Mh] Termos MeSH secundário: Adulto
Síndrome Antifosfolipídica/fisiopatologia
Heterozigoto
Homozigoto
Seres Humanos
Masculino
Mutação
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ITGB3 protein, human); 0 (Integrin beta3); 0 (Plasminogen Activator Inhibitor 1); 0 (SERPINE1 protein, human); 9001-25-6 (Factor VII); EC 1.18.1.- (methionine synthase reductase); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE


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[PMID]:28705933
[Au] Autor:Nguyen DMN; Schut GJ; Zadvornyy OA; Tokmina-Lukaszewska M; Poudel S; Lipscomb GL; Adams LA; Dinsmore JT; Nixon WJ; Boyd ES; Bothner B; Peters JW; Adams MWW
[Ad] Endereço:From the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
[Ti] Título:Two functionally distinct NADP -dependent ferredoxin oxidoreductases maintain the primary redox balance of .
[So] Source:J Biol Chem;292(35):14603-14616, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Electron bifurcation has recently gained acceptance as the third mechanism of energy conservation in which energy is conserved through the coupling of exergonic and endergonic reactions. A structure-based mechanism of bifurcation has been elucidated recently for the flavin-based enzyme NADH-dependent ferredoxin NADP oxidoreductase I (NfnI) from the hyperthermophillic archaeon NfnI is thought to be involved in maintaining the cellular redox balance, producing NADPH for biosynthesis by recycling the two other primary redox carriers, NADH and ferredoxin. The genome encodes an NfnI paralog termed NfnII, and the two are differentially expressed, depending on the growth conditions. In this study, we show that deletion of the genes encoding either NfnI or NfnII affects the cellular concentrations of NAD(P)H and particularly NADPH. This results in a moderate to severe growth phenotype in deletion mutants, demonstrating a key role for each enzyme in maintaining redox homeostasis. Despite their similarity in primary sequence and cofactor content, crystallographic, kinetic, and mass spectrometry analyses reveal that there are fundamental structural differences between the two enzymes, and NfnII does not catalyze the NfnI bifurcating reaction. Instead, it exhibits non-bifurcating ferredoxin NADP oxidoreductase-type activity. NfnII is therefore proposed to be a bifunctional enzyme and also to catalyze a bifurcating reaction, although its third substrate, in addition to ferredoxin and NADP(H), is as yet unknown.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Ferredoxina-NADP Redutase/metabolismo
Ferredoxinas/metabolismo
Regulação da Expressão Gênica em Archaea
Modelos Moleculares
NADP/metabolismo
Pyrococcus furiosus/enzimologia
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/genética
Proteínas Arqueais/isolamento & purificação
Biocatálise
Coenzimas/química
Coenzimas/metabolismo
Cristalografia por Raios X
Ferredoxina-NADP Redutase/química
Ferredoxina-NADP Redutase/genética
Ferredoxina-NADP Redutase/isolamento & purificação
Ferredoxinas/química
Deleção de Genes
Homeostase
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/isolamento & purificação
Isoenzimas/metabolismo
NAD/química
NAD/metabolismo
NADP/química
Organismos Geneticamente Modificados
Oxirredução
Filogenia
Multimerização Proteica
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/isolamento & purificação
Subunidades Proteicas/metabolismo
Pyrococcus furiosus/genética
Pyrococcus furiosus/crescimento & desenvolvimento
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Coenzymes); 0 (Ferredoxins); 0 (Isoenzymes); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins); 0U46U6E8UK (NAD); 53-59-8 (NADP); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.794172


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[PMID]:28537809
[Au] Autor:Aksoy-Sagirli P; Erdenay A; Kaytan-Saglam E; Kizir A
[Ad] Endereço:1 Department of Biochemistry, Faculty of Pharmacy, Istanbul University , Istanbul, Turkey .
[Ti] Título:Association of Three Single Nucleotide Polymorphisms in MTR and MTRR Genes with Lung Cancer in a Turkish Population.
[So] Source:Genet Test Mol Biomarkers;21(7):428-432, 2017 Jul.
[Is] ISSN:1945-0257
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIMS: Folate metabolism plays a critical role in DNA methylation and synthesis. Polymorphisms in folate metabolism may affect enzyme activities and thereby affect the cancer risk. Methionine synthase (MTR) and methionine synthase reductase (MTRR) are critical enzymes for the folate cycle. In this study, possible associations between genetic variabilities in MTR and MTRR and susceptibility to lung cancer (LC) were investigated in a Turkish population. METHODS: A case-control study with 193 LC cases and 199 noncancerous controls was conducted. DNA was extracted from leukocytes using the high pure polymerase chain reaction (PCR) template preparation kit. The MTR 2756 A>G (rs1805087), MTRR 524 C > T (rs1532268), and MTRR 66 A>G (rs1801394) genotypes were determined using PCR-restriction fragment length polymorphism (PCR-RFLP) assays. The genotype and haplotype analyses of these polymorphisms were performed using SPSS 21 and Haploview 4.2, respectively. RESULTS: An association between the MTRR A66G polymorphism and LC (p = 0.042) was found. In addition, this allele was observed more frequently in smokers compared to nonsmokers (p = 0.030). In contrast, the distribution of the MTR 2756 A>G and the MTRR 524 C > T allele frequencies were similar in the subject cases and controls. CONCLUSIONS: In conclusion, the present study suggests an association between the MTRR 66 A>G gene polymorphisms and LC risk in a Turkish population.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/genética
Neoplasias Pulmonares/genética
[Mh] Termos MeSH secundário: 5-Metiltetra-Hidrofolato-Homocisteína S-Metiltransferase/genética
5-Metiltetra-Hidrofolato-Homocisteína S-Metiltransferase/metabolismo
Idoso
Alelos
Estudos de Casos e Controles
Feminino
Ferredoxina-NADP Redutase/metabolismo
Ácido Fólico
Frequência do Gene
Estudos de Associação Genética/métodos
Predisposição Genética para Doença/genética
Variação Genética
Genótipo
Haplótipos/genética
Seres Humanos
Masculino
Meia-Idade
Polimorfismo de Nucleotídeo Único/genética
Fatores de Risco
Turquia/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
935E97BOY8 (Folic Acid); EC 1.18.1.- (methionine synthase reductase); EC 1.18.1.2 (Ferredoxin-NADP Reductase); EC 2.1.1.13 (5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase); EC 2.1.1.13. (MTR protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170525
[St] Status:MEDLINE
[do] DOI:10.1089/gtmb.2017.0062


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[PMID]:28493936
[Au] Autor:Durda K; Kaklewski K; Gupta S; Szydlowski M; Baszuk P; Jaworska-Bieniek K; Sukiennicki G; Kaczmarek K; Waloszczyk P; Narod S; Lubinski J; Jakubowska A
[Ad] Endereço:Departmentof Genetics and Pathology, International Hereditary Cancer Center, Pomeranian Medical University, Polabska 4, Szczecin, Poland.
[Ti] Título:Serum folate concentration and the incidence of lung cancer.
[So] Source:PLoS One;12(5):e0177441, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Lung cancer is a leading cause of cancer-related mortality globally. Folate helps to maintain DNA integrity and to regulate gene expression. Serum folate levels may affect the risk of several cancers, including lung cancer. In this study we evaluated the association between serum folate concentration and variations in genes involved in folate metabolism with lung cancer incidence in Poland. METHODS: The study included 366 lung cancer patients and 366 control subjects. We measured serum folate concentration and genotyped six variants in MTHFR, MTR and MTRR genes. The odds ratios of being diagnosed with lung cancer were calculated using conditional univariable and multivariable logistic regression with respect to folate level and genotypes. RESULTS: The mean serum folate level was lower in lung cancer cases than in control group (20.07 nmol/l vs. 22.52 nmol/l, p = 0.002). The odds ratio for lung cancer declined with increasing serum content of the folate. The folate concentration of >25.71 nmol/l (IVth quartile) in comparison to <15.92 nmol/l (Ist quartile) was associated with an odds ratio of 0.61 (95%CI 0.40-0.95, p = 0.03). The analysis of variations in MTHFR, MTR and MTRR genes did not reveal any significant difference between lung cancer cases and controls in univariable and multivariable analyses. CONCLUSION: In this case-control study, lower serum folate concentrations were associated with a higher risk of lung cancer diagnosis. Although previous findings have been somewhat mixed, our results add to the evidence that circulating folate levels may be an indicator of lung cancer risk.
[Mh] Termos MeSH primário: Ácido Fólico/sangue
Neoplasias Pulmonares/sangue
Neoplasias Pulmonares/genética
[Mh] Termos MeSH secundário: 5-Metiltetra-Hidrofolato-Homocisteína S-Metiltransferase/genética
Adulto
Idoso
Idoso de 80 Anos ou mais
Estudos de Casos e Controles
Feminino
Ferredoxina-NADP Redutase/genética
Genótipo
Seres Humanos
Incidência
Modelos Logísticos
Neoplasias Pulmonares/epidemiologia
Metilenotetra-Hidrofolato Redutase (NADPH2)/genética
Meia-Idade
Razão de Chances
Polimorfismo de Nucleotídeo Único/genética
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
935E97BOY8 (Folic Acid); EC 1.18.1.- (methionine synthase reductase); EC 1.18.1.2 (Ferredoxin-NADP Reductase); EC 1.5.1.20 (MTHFR protein, human); EC 1.5.1.20 (Methylenetetrahydrofolate Reductase (NADPH2)); EC 2.1.1.13 (5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase); EC 2.1.1.13. (MTR protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177441



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