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[PMID]:29185343
[Au] Autor:Saihara K; Kamikubo R; Ikemoto K; Uchida K; Akagawa M
[Ad] Endereço:Department of Biological Chemistry, Division of Applied Life Science, Graduate School of Life and Environmental Sciences, Osaka Prefecture University , Sakai 599-8531, Japan.
[Ti] Título:Pyrroloquinoline Quinone, a Redox-Active o-Quinone, Stimulates Mitochondrial Biogenesis by Activating the SIRT1/PGC-1α Signaling Pathway.
[So] Source:Biochemistry;56(50):6615-6625, 2017 Dec 19.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pyrroloquinoline quinone (PQQ), a redox-active o-quinone found in various foods and mammalian tissues, has received an increasing amount of attention because of a number of health benefits that can be attributed to its ability to enhance mitochondrial biogenesis. However, its underlying molecular mechanism remains incompletely understood. We have now established that the exposure of mouse NIH/3T3 fibroblasts to a physiologically relevant concentration of PQQ significantly stimulates mitochondrial biogenesis. The exposure of NIH/3T3 cells to 10-100 nM PQQ for 48 h resulted in increased levels of Mitotracker staining, mitochondrial DNA content, and mitochondrially encoded cytochrome c oxidase subunit 1 (MTCO1) protein. Moreover, we observed that PQQ treatment induces deacetylation of the peroxisome proliferator-activated receptor-γ-coactivator 1α (PGC-1α) and facilitates its nuclear translocation and target gene expression but does not affect its protein levels, implying increased activity of the NAD -dependent protein deacetylase sirtuin 1 (SIRT1). Indeed, treatment with a SIRT1 selective inhibitor, EX-527, hampered the ability of PQQ to stimulate PGC-1α-mediated mitochondrial biogenesis. We also found that the PQQ treatment caused a concentration-dependent increase in the cellular NAD levels, but not the total NAD and NADH levels. Our results suggest that PQQ-inducible mitochondrial biogenesis can be attributed to activation of the SIRT1/PGC-1α signaling pathway by enhancing cellular NAD formation.
[Mh] Termos MeSH primário: Cofator PQQ/metabolismo
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo
Sirtuína 1/metabolismo
[Mh] Termos MeSH secundário: Animais
Benzoquinonas/química
Benzoquinonas/metabolismo
Fibroblastos
Células Hep G2
Seres Humanos
Camundongos
Mitocôndrias/metabolismo
Mitocôndrias/fisiologia
Células NIH 3T3
Biogênese de Organelas
Oxirredução
Cofator PQQ/química
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética
Transdução de Sinais/efeitos dos fármacos
Sirtuína 1/genética
Transativadores/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoquinones); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (Trans-Activators); 0 (Transcription Factors); 3T006GV98U (quinone); 72909-34-3 (PQQ Cofactor); EC 3.5.1.- (SIRT1 protein, human); EC 3.5.1.- (Sirt1 protein, mouse); EC 3.5.1.- (Sirtuin 1)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b01185


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[PMID]:28448745
[Au] Autor:Wei P; Si Z; Lu Y; Yu Q; Huang L; Xu Z
[Ad] Endereço:a School of Biological and Chemical Engineering, Zhejiang University of Science & Technology , Hangzhou , P. R. China.
[Ti] Título:Medium optimization for pyrroloquinoline quinone (PQQ) production by Methylobacillus sp. zju323 using response surface methodology and artificial neural network-genetic algorithm.
[So] Source:Prep Biochem Biotechnol;47(7):709-719, 2017 Aug 09.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Methylobacillus sp. zju323 was adopted to improve the biosynthesis of pyrroloquinoline quinone (PQQ) by systematic optimization of the fermentation medium. The Plackett-Burman design was implemented to screen for the key medium components for the PQQ production. CoCl · 6H O, ρ-amino benzoic acid, and MgSO · 7H O were found capable of enhancing the PQQ production most significantly. A five-level three-factor central composite design was used to investigate the direct and interactive effects of these variables. Both response surface methodology (RSM) and artificial neural network-genetic algorithm (ANN-GA) were used to predict the PQQ production and to optimize the medium composition. The results showed that the medium optimized by ANN-GA was better than that by RSM in maximizing PQQ production and the experimental PQQ concentration in the ANN-GA-optimized medium was improved by 44.3% compared with that in the unoptimized medium. Further study showed that this ANN-GA-optimized medium was also effective in improving PQQ production by fed-batch mode, reaching the highest PQQ accumulation of 232.0 mg/L, which was about 47.6% increase relative to that in the original medium. The present work provided an optimized medium and developed a fed-batch strategy which might be potentially applicable in industrial PQQ production.
[Mh] Termos MeSH primário: Microbiologia Industrial/métodos
Methylobacillus/metabolismo
Cofator PQQ/metabolismo
[Mh] Termos MeSH secundário: Algoritmos
Meios de Cultura/metabolismo
Fermentação
Redes Neurais (Computação)
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 72909-34-3 (PQQ Cofactor)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1315596


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[PMID]:28481092
[Au] Autor:Evans RL; Latham JA; Xia Y; Klinman JP; Wilmot CM
[Ad] Endereço:Department of Biochemistry, Molecular Biology, and Biophysics and Biotechnology Institute, University of Minnesota, Twin Cities , St. Paul, Minnesota 55108, United States.
[Ti] Título:Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.
[So] Source:Biochemistry;56(21):2735-2746, 2017 May 30.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is initiated when the precursor peptide, PqqA, is recognized and bound by the RiPP precursor peptide recognition element (RRE), PqqD, for presentation to the first enzyme in the pathway, PqqE. Unlike other RiPP-producing, postribosomal peptide synthesis (PRPS) pathways in which the RRE is a component domain of the first enzyme, PqqD is predominantly a separate scaffolding protein that forms a ternary complex with the precursor peptide and first tailoring enzyme. As PqqD is a stable, independent RRE, this makes the PQQ pathway an ideal PRPS model system for probing RRE interactions using nuclear magnetic resonance (NMR). Herein, we present both the solution NMR structure of Methylobacterium extorquens PqqD and results of H- N HSQC binding experiments that identify the PqqD residues involved in binding the precursor peptide, PqqA, and the enzyme, PqqE. The reported structural model for an independent RRE, along with the mapped binding surfaces, will inform future efforts both to understand and to manipulate PRPS pathways.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Methylobacterium extorquens/enzimologia
Chaperonas Moleculares/metabolismo
Ressonância Magnética Nuclear Biomolecular
Oxirredutases/metabolismo
Cofator PQQ/biossíntese
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Sítios de Ligação
Methylobacterium extorquens/metabolismo
Modelos Moleculares
Chaperonas Moleculares/química
Oxirredutases/química
Cofator PQQ/química
Cofator PQQ/metabolismo
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Molecular Chaperones); 0 (PqqD protein, Methylobacterium extorquens); 72909-34-3 (PQQ Cofactor); EC 1.- (Oxidoreductases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00247


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[PMID]:28407913
[Au] Autor:Ma K; Cui JZ; Ye JB; Hu XM; Ma GL; Yang XP
[Ad] Endereço:School of Food and Biological Engineering, Henan Provincial Collaborative Innovation Center for Food Production and Safety, Zhengzhou University of Light Industry, Dongfeng Road, Zhengzhou 450002, People's Republic of China.
[Ti] Título:Pyrroloquinoline quinone from Gluconobacter oxydans fermentation broth enhances superoxide anion-scavenging capacity of Cu/Zn-SOD.
[So] Source:Food Chem;230:291-294, 2017 Sep 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A bioassay-guided fractionation of extract from Gluconobacter oxydans fermentation broth afforded Compound 1, which was identified as pyrroloquinoline quinone (PQQ) by spectroscopic methods. PQQ has been shown to enhance the superoxide anion-scavenging capacity significantly for Cu/Zn-SOD. To illustrate the mechanism, the interaction between PQQ and Cu/Zn-SOD was investigated. The multiple binding sites involving hydrogen bonds and van der Waals force between PQQ and Cu/Zn-SOD were revealed by isothermal titration calorimetry. The α-helix content was increased in the Cu/Zn-SOD structure with the addition of PQQ into the solution through ultraviolet (UV) spectroscopy. These results indicated that PQQ could change the conformation of Cu/Zn-SOD through interaction, which could enhance its superoxide anion-scavenging capacity. Therefore, PQQ is a potential natural antioxidant.
[Mh] Termos MeSH primário: Gluconobacter oxydans/química
Cofator PQQ/química
Superóxido Dismutase/química
Superóxidos/química
Zinco/química
[Mh] Termos MeSH secundário: Animais
Fermentação
Espécies Reativas de Oxigênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 11062-77-4 (Superoxides); 72909-34-3 (PQQ Cofactor); EC 1.15.1.1 (Superoxide Dismutase); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE


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[PMID]:28344084
[Au] Autor:Vemuluri VR; Shaw S; Autenrieth C; Ghosh R
[Ad] Endereço:Department of Bioenergetics, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart, Pfaffenwaldring 57, D-70569 Stuttgart, Germany; Microbial Culture Collection, National Centre for Cell Science, Pune, Maharashtra 411021, India.
[Ti] Título:A rapid procedure for the in situ assay of periplasmic, PQQ-dependent methanol dehydrogenase in intact single bacterial colonies.
[So] Source:J Microbiol Methods;137:46-49, 2017 Jun.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mechanistic details of methanol oxidation catalyzed by the periplasmically-located pyrroloquinoline quinone-dependent methanol dehydrogenase of methylotrophs can be elucidated using site-directed mutants. Here, we present an in situ colony assay of methanol dehydrogenase, which allows robotic screening of large populations of intact small colonies, and regrowth of colonies for subsequent analysis.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/análise
Bactérias/enzimologia
Técnicas Microbiológicas/métodos
Periplasma/metabolismo
[Mh] Termos MeSH secundário: Bactérias/crescimento & desenvolvimento
Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Programas de Rastreamento
Metanol/metabolismo
Mutagênese Sítio-Dirigida
Oxirredução
Cofator PQQ/metabolismo
Periplasma/microbiologia
Quinonas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Quinones); 72909-34-3 (PQQ Cofactor); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.2.8 (alcohol dehydrogenase (acceptor)); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE


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[PMID]:28007783
[Au] Autor:Jonscher KR; Stewart MS; Alfonso-Garcia A; DeFelice BC; Wang XX; Luo Y; Levi M; Heerwagen MJ; Janssen RC; de la Houssaye BA; Wiitala E; Florey G; Jonscher RL; Potma EO; Fiehn O; Friedman JE
[Ad] Endereço:Department of Anesthesiology, University of Colorado Anschutz Medical Campus, Aurora, Colorado, USA; karen.jonscher@ucdenver.edu.
[Ti] Título:Early PQQ supplementation has persistent long-term protective effects on developmental programming of hepatic lipotoxicity and inflammation in obese mice.
[So] Source:FASEB J;31(4):1434-1448, 2017 Apr.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nonalcoholic fatty liver disease (NAFLD) is widespread in adults and children. Early exposure to maternal obesity or Western-style diet (WD) increases steatosis and oxidative stress in fetal liver and is associated with lifetime disease risk in the offspring. Pyrroloquinoline quinone (PQQ) is a natural antioxidant found in soil, enriched in human breast milk, and essential for development in mammals. We investigated whether a supplemental dose of PQQ, provided prenatally in a mouse model of diet-induced obesity during pregnancy, could protect obese offspring from progression of NAFLD. PQQ treatment given pre- and postnatally in WD-fed offspring had no effect on weight gain but increased metabolic flexibility while reducing body fat and liver lipids, compared with untreated obese offspring. Indices of NAFLD, including hepatic ceramide levels, oxidative stress, and expression of proinflammatory genes ( , , , and ), were decreased in WD PQQ-fed mice, concomitant with increased expression of fatty acid oxidation genes and decreased expression. Notably, these changes persisted even after PQQ withdrawal at weaning. Our results suggest that supplementation with PQQ, particularly during pregnancy and lactation, protects offspring from WD-induced developmental programming of hepatic lipotoxicity and may help slow the advancing epidemic of NAFLD in the next generation.-Jonscher, K. R., Stewart, M. S., Alfonso-Garcia, A., DeFelice, B. C., Wang, X. X., Luo, Y., Levi, M., Heerwagen, M. J. R., Janssen, R. C., de la Houssaye, B. A., Wiitala, E., Florey, G., Jonscher, R. L., Potma, E. O., Fiehn, O. Friedman, J. E. Early PQQ supplementation has persistent long-term protective effects on developmental programming of hepatic lipotoxicity and inflammation in obese mice.
[Mh] Termos MeSH primário: Antioxidantes/uso terapêutico
Hepatopatia Gordurosa não Alcoólica/prevenção & controle
Obesidade/complicações
Cofator PQQ/uso terapêutico
Efeitos Tardios da Exposição Pré-Natal/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Antioxidantes/administração & dosagem
Antioxidantes/farmacologia
Ceramidas/metabolismo
Ciclo-Oxigenase 2/genética
Ciclo-Oxigenase 2/metabolismo
Dieta Hiperlipídica/efeitos adversos
Suplementos Nutricionais
Feminino
Interleucina-6/genética
Interleucina-6/metabolismo
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Proteína 3 que Contém Domínio de Pirina da Família NLR/genética
Proteína 3 que Contém Domínio de Pirina da Família NLR/metabolismo
Óxido Nítrico Sintase Tipo II/genética
Óxido Nítrico Sintase Tipo II/metabolismo
Hepatopatia Gordurosa não Alcoólica/tratamento farmacológico
Hepatopatia Gordurosa não Alcoólica/etiologia
Obesidade/tratamento farmacológico
Obesidade/etiologia
Estresse Oxidativo
PPAR gama/metabolismo
Cofator PQQ/administração & dosagem
Cofator PQQ/farmacologia
Gravidez
Efeitos Tardios da Exposição Pré-Natal/tratamento farmacológico
Efeitos Tardios da Exposição Pré-Natal/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Ceramides); 0 (Interleukin-6); 0 (NLR Family, Pyrin Domain-Containing 3 Protein); 0 (Nlrp3 protein, mouse); 0 (PPAR gamma); 0 (interleukin-6, mouse); 72909-34-3 (PQQ Cofactor); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.14.13.39 (Nos2 protein, mouse); EC 1.14.99.- (Ptgs2 protein, mouse); EC 1.14.99.1 (Cyclooxygenase 2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161224
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600906R


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[PMID]:27156055
[Au] Autor:Han S; Du T; Jiang H; Wang X
[Ad] Endereço:State Key Lab of Bioelectronics (Chien-Shiung Wu Laboratory), Southeast University, No. 2 Sipailou, Nanjing 210096, China.
[Ti] Título:Synergistic effect of pyrroloquinoline quinone and graphene nano-interface for facile fabrication of sensitive NADH biosensor.
[So] Source:Biosens Bioelectron;89(Pt 1):422-429, 2017 Mar 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A self-assembly composite of graphene-pyrroloquinoline quinone (PQQ) was fabricated and modified on glassy carbon electrode (GCE) for sensitive detection of nicotinamide adenine dinucleotide (NADH). Chitosan (CTS) was applied to disperse graphene to form a stable robust film on GCE. A synergistic effect between PQQ and graphene was observed during the electrocatalytic oxidation of NADH, with about 260mV reduction in the oxidation potential and 2.5-fold increase in the oxidation current compared with those on the bare GCE. The electrochemical sensors based on the modified electrodes allowed the detection of NADH with a good linear dependence from 0.32 to 220µM with a high sensitivity of 0.421µAµM cm and a low detection limit of 0.16µM (S/N=3). It could also eliminate the interference of electroactive substances like ascorbic acid (AA), uric acid, and dopamine and its derivatives. The outstanding performances of graphene-PQQ/CTS composite capable of improving the electrical conductivity and accelerating the electron transport suggested its promising applications for design of different graphene based composites used in electrochemical sensing and energy fields.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Técnicas Eletroquímicas/métodos
Grafite/química
NAD/sangue
Nanoestruturas/química
Cofator PQQ/química
[Mh] Termos MeSH secundário: Impedância Elétrica
Eletrodos
Seres Humanos
Limite de Detecção
Modelos Moleculares
Nanoestruturas/ultraestrutura
Oxirredução
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0U46U6E8UK (NAD); 72909-34-3 (PQQ Cofactor); 7782-42-5 (Graphite)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160509
[St] Status:MEDLINE


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[PMID]:26661224
[Au] Autor:Martino Adami PV; Quijano C; Magnani N; Galeano P; Evelson P; Cassina A; Do Carmo S; Leal MC; Castaño EM; Cuello AC; Morelli L
[Ad] Endereço:Laboratory of Amyloidosis and Neurodegeneration, Fundación Instituto Leloir-IIBBA-CONICET, Buenos Aires, Argentina.
[Ti] Título:Synaptosomal bioenergetic defects are associated with cognitive impairment in a transgenic rat model of early Alzheimer's disease.
[So] Source:J Cereb Blood Flow Metab;37(1):69-84, 2017 Jan.
[Is] ISSN:1559-7016
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Synaptic bioenergetic deficiencies may be associated with early Alzheimer's disease (AD). To explore this concept, we assessed pre-synaptic mitochondrial function in hemizygous (+/-)TgMcGill-R-Thy1-APP rats. The low burden of Aß and the wide array of behavioral and cognitive impairments described in 6-month-old hemizygous TgMcGill-R-Thy1-APP rats (Tg(+/-)) support their use to investigate synaptic bioenergetics deficiencies described in subjects with early Alzheimer's disease (AD). In this report, we show that pre-synaptic mitochondria from Tg(+/-) rats evidence a decreased respiratory control ratio and spare respiratory capacity associated with deficits in complex I enzymatic activity. Cognitive impairments were prevented and bioenergetic deficits partially reversed when Tg(+/-) rats were fed a nutritionally complete diet from weaning to 6-month-old supplemented with pyrroloquinoline quinone, a mitochondrial biogenesis stimulator with antioxidant and neuroprotective effects. These results provide evidence that, as described in AD brain and not proven in Tg mice models with AD-like phenotype, the mitochondrial bioenergetic capacity of synaptosomes is not conserved in the Tg(+/-) rats. This animal model may be suitable for understanding the basic biochemical mechanisms involved in early AD.
[Mh] Termos MeSH primário: Doença de Alzheimer/etiologia
Disfunção Cognitiva/etiologia
Metabolismo Energético
Sinaptossomos/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/dietoterapia
Doença de Alzheimer/metabolismo
Doença de Alzheimer/patologia
Animais
Disfunção Cognitiva/metabolismo
Dietoterapia
Modelos Animais de Doenças
Complexo I de Transporte de Elétrons/metabolismo
Mitocôndrias/metabolismo
Cofator PQQ/uso terapêutico
Ratos
Ratos Transgênicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
72909-34-3 (PQQ Cofactor); EC 1.6.5.3 (Electron Transport Complex I)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE


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[PMID]:27638737
[Au] Autor:Evans RL; Latham JA; Klinman JP; Wilmot CM; Xia Y
[Ad] Endereço:Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Twin Cities, Saint Paul, MN, 55108, USA.
[Ti] Título:(1)H, (13)C, and (15)N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA.
[So] Source:Biomol NMR Assign;10(2):385-9, 2016 Oct.
[Is] ISSN:1874-270X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is a dehydrogenase cofactor synthesized by, but not exclusively used by, certain prokaryotes. RiPPs represent a rapidly expanding and diverse class of natural products-many of which have therapeutic potential-and the biosynthetic pathways for these are gaining attention. Five gene products from the pqq operon (PqqA, PqqB, PqqC, PqqD, and PqqE) are essential for PQQ biosynthesis. The substrate is the peptide PqqA, which is presented to the radical SAM enzyme PqqE by the small protein PqqD. PqqA is unstructured in solution, and only binds to PqqE when in complex with PqqD. PqqD is a member of a growing family of RiPP chaperone proteins (or domains in most cases) that present their associated peptide substrates to the initial RiPP biosynthesis enzymes. An X-ray crystal structure exists for dimeric Xanthomonas campestris PqqD (PDB ID: 3G2B), but PqqD is now known to act as a monomer under physiological conditions. In this study, the PqqD truncation from naturally fused Methylobacterium extorquens (Mex) PqqCD was overexpressed in Escherichia coli and MexPqqA was chemically synthesized. Solution NMR (1)H-,(15)N-HSQC chemical shift studies have identified the PqqD residues involved in binding PqqA, and (1)H, (13)C, and (15)N peak assignments for PqqD alone and for PqqD bound to PqqA are reported herein.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Methylobacterium extorquens
Ressonância Magnética Nuclear Biomolecular
Cofator PQQ/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 72909-34-3 (PQQ Cofactor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160918
[St] Status:MEDLINE
[do] DOI:10.1007/s12104-016-9705-8


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[PMID]:27592307
[Au] Autor:Kim HW; Wang JY; Lee JY; Park AK; Park H; Jeon SJ
[Ad] Endereço:Division of Life Sciences, Korea Polar Research Institute (KOPRI), Korea University of Science and Technology, 26 Songdomirae-ro, Incheon, 21990, Republic of Korea; Department of Polar Sciences, Korea University of Science and Technology, 26 Songdomirae-ro, Incheon, 21990, Republic of Korea.
[Ti] Título:Biochemical and structural characterization of quinoprotein aldose sugar dehydrogenase from Thermus thermophilus HJ6: Mutational analysis of Tyr156 in the substrate-binding site.
[So] Source:Arch Biochem Biophys;608:20-6, 2016 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The gene encoding a quinoprotein aldose sugar dehydrogenase (ASD) from Thermus thermophilus HJ6 (Tt_ASD) was cloned and sequenced; it comprised 1059 nucleotides encoding a protein containing 352 amino acids that had a predicted molecular mass of 38.9 kDa. The deduced amino acid sequence showed 42.9% and 33.9% identities to the ASD proteins from Pyrobaculum aerophilum and Escherichia coli, respectively. The biochemical properties of Tt_ASD were characterized. The optimum pH for the oxidation of glucose was 7.0-7.5 and the optimum temperature was 70 °C. The half-life of heat inactivation for the apoenzyme was about 25 min at 85 °C. The enzyme was highly thermostable, and the activity of the pyrroloquinoline quinone-bound holoenzyme was not lost after incubation at 85 °C for 100 min. Tt_ASD could oxidize various sugars, including hexoses, pentoses, disaccharides, and polysaccharides, in addition to alcohols. Structural analysis suggested that Tyr156 would be the substrate-binding residue. Two mutants, Y156A and Y156K, had impaired activities and affinities for all substrates and completely lost their activities for alcohols. This structural and mutational analysis of Tt_ASD demonstrates the crucial role of Tyr156 in determining substrate specificity.
[Mh] Termos MeSH primário: Aspartato-Semialdeído Desidrogenase/química
Proteínas de Bactérias/química
Análise Mutacional de DNA
Thermus thermophilus/genética
[Mh] Termos MeSH secundário: Aspartato-Semialdeído Desidrogenase/genética
Proteínas de Bactérias/genética
Sítios de Ligação
Proteínas de Escherichia coli/genética
Concentração de Íons de Hidrogênio
Cinética
Conformação Molecular
Mutação
Fases de Leitura Aberta
Cofator PQQ/química
Cofator PQQ/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Especificidade por Substrato
Temperatura Ambiente
Thermus thermophilus/enzimologia
Tirosina/química
Tirosina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Recombinant Proteins); 42HK56048U (Tyrosine); 72909-34-3 (PQQ Cofactor); EC 1.2.1.11 (Asd protein, E coli); EC 1.2.1.11 (Aspartate-Semialdehyde Dehydrogenase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160905
[St] Status:MEDLINE



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