Artigos de revistas sobre o tema "Flavin hydroquinone dependent Enzymes"
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Perry, Lynda L., e Gerben J. Zylstra. "Cloning of a Gene Cluster Involved in the Catabolism of p-Nitrophenol by Arthrobacter sp. Strain JS443 and Characterization of the p-Nitrophenol Monooxygenase". Journal of Bacteriology 189, n.º 21 (24 de agosto de 2007): 7563–72. http://dx.doi.org/10.1128/jb.01849-06.
Texto completo da fonteMihasan, Marius, Calin-Bogdan Chiribau, Thorsten Friedrich, Vlad Artenie e Roderich Brandsch. "An NAD(P)H-Nicotine Blue Oxidoreductase Is Part of the Nicotine Regulon and May Protect Arthrobacter nicotinovorans from Oxidative Stress during Nicotine Catabolism". Applied and Environmental Microbiology 73, n.º 8 (9 de fevereiro de 2007): 2479–85. http://dx.doi.org/10.1128/aem.02668-06.
Texto completo da fonteHyster, Todd K. "Radical Biocatalysis: Using Non-Natural Single Electron Transfer Mechanisms to Access New Enzymatic Functions". Synlett 31, n.º 03 (7 de maio de 2019): 248–54. http://dx.doi.org/10.1055/s-0037-1611818.
Texto completo da fonteWojcieszyńska, Danuta, Katarzyna Hupert-Kocurek e Urszula Guzik. "Flavin-Dependent Enzymes in Cancer Prevention". International Journal of Molecular Sciences 13, n.º 12 (7 de dezembro de 2012): 16751–68. http://dx.doi.org/10.3390/ijms131216751.
Texto completo da fonteHilvert, Donald, e E. T. Kaisert. "Semisynthetic Enzymes: Design of Flavin-Dependent Oxidoreductases". Biotechnology and Genetic Engineering Reviews 5, n.º 1 (setembro de 1987): 297–318. http://dx.doi.org/10.1080/02648725.1987.10647841.
Texto completo da fonteMenon, Binuraj R. K., Jonathan Latham, Mark S. Dunstan, Eileen Brandenburger, Ulrike Klemstein, David Leys, Chinnan Karthikeyan, Michael F. Greaney, Sarah A. Shepherd e Jason Micklefield. "Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes". Organic & Biomolecular Chemistry 14, n.º 39 (2016): 9354–61. http://dx.doi.org/10.1039/c6ob01861k.
Texto completo da fonteMügge, Carolin, Thomas Heine, Alvaro Gomez Baraibar, Willem J. H. van Berkel, Caroline E. Paul e Dirk Tischler. "Flavin-dependent N-hydroxylating enzymes: distribution and application". Applied Microbiology and Biotechnology 104, n.º 15 (5 de junho de 2020): 6481–99. http://dx.doi.org/10.1007/s00253-020-10705-w.
Texto completo da fonteMoon, Shin e Choe. "Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius". Crystals 9, n.º 11 (23 de outubro de 2019): 548. http://dx.doi.org/10.3390/cryst9110548.
Texto completo da fonteShepherd, Sarah A., Chinnan Karthikeyan, Jonathan Latham, Anna-Winona Struck, Mark L. Thompson, Binuraj R. K. Menon, Matthew Q. Styles, Colin Levy, David Leys e Jason Micklefield. "Extending the biocatalytic scope of regiocomplementary flavin-dependent halogenase enzymes". Chemical Science 6, n.º 6 (2015): 3454–60. http://dx.doi.org/10.1039/c5sc00913h.
Texto completo da fonteSaleem-Batcha, Raspudin, Frederick Stull, Jacob N. Sanders, Bradley S. Moore, Bruce A. Palfey, K. N. Houk e Robin Teufel. "Enzymatic control of dioxygen binding and functionalization of the flavin cofactor". Proceedings of the National Academy of Sciences 115, n.º 19 (23 de abril de 2018): 4909–14. http://dx.doi.org/10.1073/pnas.1801189115.
Texto completo da fontede Gonzalo, Gonzalo, e Andrés R. Alcántara. "Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases". Catalysts 11, n.º 5 (8 de maio de 2021): 605. http://dx.doi.org/10.3390/catal11050605.
Texto completo da fonteZhang, Jun-Jie, Hong Liu, Yi Xiao, Xian-En Zhang e Ning-Yi Zhou. "Identification and Characterization of Catabolic para-Nitrophenol 4-Monooxygenase and para-Benzoquinone Reductase from Pseudomonas sp. Strain WBC-3". Journal of Bacteriology 191, n.º 8 (13 de fevereiro de 2009): 2703–10. http://dx.doi.org/10.1128/jb.01566-08.
Texto completo da fonteDick, Scott, Laura Marrone, Abraham M. Thariath, Miguel A. Valvano e Thammaiah Viswanatha. "Cofactor- and substrate-binding domains in flavin-dependent N-hydroxylating enzymes". Trends in Biochemical Sciences 23, n.º 11 (novembro de 1998): 414. http://dx.doi.org/10.1016/s0968-0004(98)01271-7.
Texto completo da fonteWang, Jinyu, e Yajun Liu. "Systematic Theoretical Study on the pH-Dependent Absorption and Fluorescence Spectra of Flavins". Molecules 28, n.º 8 (8 de abril de 2023): 3315. http://dx.doi.org/10.3390/molecules28083315.
Texto completo da fonteZverinsky, I. V., H. G. Zverinskaya, I. P. Sutsko, P. G. Telegin e A. G. Shlyahtun. "Effects of berberine on the recovery of rat liver xenobiotic-metabolizing enzymes after partial hepatectomy". Biomeditsinskaya Khimiya 61, n.º 3 (2015): 381–83. http://dx.doi.org/10.18097/pbmc20156103381.
Texto completo da fonteMcLEAN, Kirsty J., Nigel S. SCRUTTON e Andrew W. MUNRO. "Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA". Biochemical Journal 372, n.º 2 (1 de junho de 2003): 317–27. http://dx.doi.org/10.1042/bj20021692.
Texto completo da fonteHuang, Yan, Randy Xun, Guanjun Chen e Luying Xun. "Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723". Journal of Bacteriology 190, n.º 23 (26 de setembro de 2008): 7595–600. http://dx.doi.org/10.1128/jb.00489-08.
Texto completo da fonteWick, Jonas, Daniel Heine, Gerald Lackner, Mathias Misiek, James Tauber, Hans Jagusch, Christian Hertweck e Dirk Hoffmeister. "A Fivefold Parallelized Biosynthetic Process Secures Chlorination of Armillaria mellea (Honey Mushroom) Toxins". Applied and Environmental Microbiology 82, n.º 4 (11 de dezembro de 2015): 1196–204. http://dx.doi.org/10.1128/aem.03168-15.
Texto completo da fonteNeubauer, Pia R., Olga Blifernez-Klassen, Lara Pfaff, Mohamed Ismail, Olaf Kruse e Norbert Sewald. "Two Novel, Flavin-Dependent Halogenases from the Bacterial Consortia of Botryococcus braunii Catalyze Mono- and Dibromination". Catalysts 11, n.º 4 (10 de abril de 2021): 485. http://dx.doi.org/10.3390/catal11040485.
Texto completo da fonteAndorfer, Mary C., e Jared C. Lewis. "Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis". Annual Review of Biochemistry 87, n.º 1 (20 de junho de 2018): 159–85. http://dx.doi.org/10.1146/annurev-biochem-062917-012042.
Texto completo da fonteHeine, Thomas, Willem van Berkel, George Gassner, Karl-Heinz van Pée e Dirk Tischler. "Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities". Biology 7, n.º 3 (2 de agosto de 2018): 42. http://dx.doi.org/10.3390/biology7030042.
Texto completo da fontePozzi, Cecilia, Ludovica Lopresti, Giusy Tassone e Stefano Mangani. "Targeting Methyltransferases in Human Pathogenic Bacteria: Insights into Thymidylate Synthase (TS) and Flavin-Dependent TS (FDTS)". Molecules 24, n.º 8 (25 de abril de 2019): 1638. http://dx.doi.org/10.3390/molecules24081638.
Texto completo da fonteBiegasiewicz, Kyle F., Simon J. Cooper, Xin Gao, Daniel G. Oblinsky, Ji Hye Kim, Samuel E. Garfinkle, Leo A. Joyce, Braddock A. Sandoval, Gregory D. Scholes e Todd K. Hyster. "Photoexcitation of flavoenzymes enables a stereoselective radical cyclization". Science 364, n.º 6446 (20 de junho de 2019): 1166–69. http://dx.doi.org/10.1126/science.aaw1143.
Texto completo da fonteFejzagić, Alexander Veljko, Jan Gebauer, Nikolai Huwa e Thomas Classen. "Halogenating Enzymes for Active Agent Synthesis: First Steps Are Done and Many Have to Follow". Molecules 24, n.º 21 (5 de novembro de 2019): 4008. http://dx.doi.org/10.3390/molecules24214008.
Texto completo da fontePimviriyakul, Panu, Panida Surawatanawong e Pimchai Chaiyen. "Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonation". Chemical Science 9, n.º 38 (2018): 7468–82. http://dx.doi.org/10.1039/c8sc01482e.
Texto completo da fonteWilletts, Andrew. "The Isoenzymic Diketocamphane Monooxygenases of Pseudomonas putida ATCC 17453—An Episodic History and Still Mysterious after 60 Years". Microorganisms 9, n.º 12 (15 de dezembro de 2021): 2593. http://dx.doi.org/10.3390/microorganisms9122593.
Texto completo da fonteUng, Kien Lam, Chloé Poussineau, Julie Couston, Husam M. A. B. Alsarraf e Mickaël Blaise. "Crystal structure of MAB_4123, a putative flavin-dependent monooxygenase from Mycobacterium abscessus". Acta Crystallographica Section F Structural Biology Communications 79, n.º 5 (1 de maio de 2023): 128–36. http://dx.doi.org/10.1107/s2053230x2300345x.
Texto completo da fontePimviriyakul, Panu, e Pimchai Chaiyen. "A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin–dependent enzymes". Journal of Biological Chemistry 293, n.º 48 (3 de outubro de 2018): 18525–39. http://dx.doi.org/10.1074/jbc.ra118.005538.
Texto completo da fonteShah, Mihir V., James Antoney, Suk Woo Kang, Andrew C. Warden, Carol J. Hartley, Hadi Nazem-Bokaee, Colin J. Jackson e Colin Scott. "Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis". Catalysts 9, n.º 10 (20 de outubro de 2019): 868. http://dx.doi.org/10.3390/catal9100868.
Texto completo da fonteCapeillère-Blandin, C., M. J. Barber e R. C. Bray. "Comparison of the processes involved in reduction by the substrate for two homologous flavocytochromes b2 from different species of yeast". Biochemical Journal 238, n.º 3 (15 de setembro de 1986): 745–56. http://dx.doi.org/10.1042/bj2380745.
Texto completo da fonteFerreira, Maria Isabel M., Toshiya Iida, Syed A. Hasan, Kaoru Nakamura, Marco W. Fraaije, Dick B. Janssen e Toshiaki Kudo. "Analysis of Two Gene Clusters Involved in the Degradation of 4-Fluorophenol by Arthrobacter sp. Strain IF1". Applied and Environmental Microbiology 75, n.º 24 (16 de outubro de 2009): 7767–73. http://dx.doi.org/10.1128/aem.00171-09.
Texto completo da fonteDeng, Yaming, Quan Zhou, Yuzhou Wu, Xi Chen e Fangrui Zhong. "Properties and Mechanisms of Flavin-Dependent Monooxygenases and Their Applications in Natural Product Synthesis". International Journal of Molecular Sciences 23, n.º 5 (27 de fevereiro de 2022): 2622. http://dx.doi.org/10.3390/ijms23052622.
Texto completo da fonteChanda, Kakoli, Atifa Begum Mozumder, Ringhoilal Chorei, Ridip Kumar Gogoi e Himanshu Kishore Prasad. "A Lignocellulolytic Colletotrichum sp. OH with Broad-Spectrum Tolerance to Lignocellulosic Pretreatment Compounds and Derivatives and the Efficiency to Produce Hydrogen Peroxide and 5-Hydroxymethylfurfural Tolerant Cellulases". Journal of Fungi 7, n.º 10 (22 de setembro de 2021): 785. http://dx.doi.org/10.3390/jof7100785.
Texto completo da fonteManenda, Mahder S., Marie-Ève Picard, Liping Zhang, Normand Cyr, Xiaojun Zhu, Julie Barma, John M. Pascal, Manon Couture, Changsheng Zhang e Rong Shi. "Structural analyses of the Group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations". Journal of Biological Chemistry 295, n.º 14 (28 de fevereiro de 2020): 4709–22. http://dx.doi.org/10.1074/jbc.ra119.011212.
Texto completo da fonteOgawa, Aoba, Gen-ichi Sampei e Gota Kawai. "Crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C-terminal domain". Acta Crystallographica Section F Structural Biology Communications 75, n.º 6 (1 de junho de 2019): 450–54. http://dx.doi.org/10.1107/s2053230x19007192.
Texto completo da fonteMączka, Wanda, Katarzyna Wińska e Małgorzata Grabarczyk. "Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow". Catalysts 8, n.º 12 (5 de dezembro de 2018): 624. http://dx.doi.org/10.3390/catal8120624.
Texto completo da fonteBuss, Maren, Christina Geerds, Thomas Patschkowski, Karsten Niehaus e Hartmut H. Niemann. "Perfect merohedral twinning combined with noncrystallographic symmetry potentially causes the failure of molecular replacement with low-homology search models for the flavin-dependent halogenase HalX from Xanthomonas campestris". Acta Crystallographica Section F Structural Biology Communications 74, n.º 6 (18 de maio de 2018): 345–50. http://dx.doi.org/10.1107/s2053230x18006933.
Texto completo da fonteMatsubara, Toshiyuki, Takashi Ohshiro, Yoshihiro Nishina e Yoshikazu Izumi. "Purification, Characterization, and Overexpression of Flavin Reductase Involved in Dibenzothiophene Desulfurization byRhodococcus erythropolis D-1". Applied and Environmental Microbiology 67, n.º 3 (1 de março de 2001): 1179–84. http://dx.doi.org/10.1128/aem.67.3.1179-1184.
Texto completo da fonteWilliams, Richard E., Deborah A. Rathbone, Nigel S. Scrutton e Neil C. Bruce. "Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins". Applied and Environmental Microbiology 70, n.º 6 (junho de 2004): 3566–74. http://dx.doi.org/10.1128/aem.70.6.3566-3574.2004.
Texto completo da fonteMessiha, Hanan L., Thanyaporn Wongnate, Pimchai Chaiyen, Alex R. Jones e Nigel S. Scrutton. "Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes". Journal of The Royal Society Interface 12, n.º 103 (fevereiro de 2015): 20141155. http://dx.doi.org/10.1098/rsif.2014.1155.
Texto completo da fonteKassay, Norbert, Vanda Toldi, József Tőzsér e András Szabó. "Cigarette smoke toxin hydroquinone and misfolding pancreatic lipase variant cooperatively promote endoplasmic reticulum stress and cell death". PLOS ONE 17, n.º 6 (15 de junho de 2022): e0269936. http://dx.doi.org/10.1371/journal.pone.0269936.
Texto completo da fonteSpohn, Gabriele, Andre Kleinridders, F. Thomas Wunderlich, Matthias Watzka, Frank Zaucke, Katrin Blum-bach, Christof Geisen et al. "VKORC1 deficiency in mice causes early postnatal lethality due to severe bleeding". Thrombosis and Haemostasis 101, n.º 06 (2009): 1044–50. http://dx.doi.org/10.1160/th09-03-0204.
Texto completo da fonteRoberts, Kenneth M., José R. Tormos e Paul F. Fitzpatrick. "Characterization of Unstable Products of Flavin- and Pterin-Dependent Enzymes by Continuous-Flow Mass Spectrometry". Biochemistry 53, n.º 16 (18 de abril de 2014): 2672–79. http://dx.doi.org/10.1021/bi500267c.
Texto completo da fonteDzeja, Petras P., Peter Bast, Cevher Ozcan, Arturo Valverde, Ekshon L. Holmuhamedov, David G. L. Van Wylen e Andre Terzic. "Targeting nucleotide-requiring enzymes: implications for diazoxide-induced cardioprotection". American Journal of Physiology-Heart and Circulatory Physiology 284, n.º 4 (1 de abril de 2003): H1048—H1056. http://dx.doi.org/10.1152/ajpheart.00847.2002.
Texto completo da fonteZografos, Alexandros, e Marina Petsi. "Advances in Catalytic Aerobic Oxidations by Activation of Dioxygen-Monooxygenase Enzymes and Biomimetics". Synthesis 50, n.º 24 (15 de outubro de 2018): 4715–45. http://dx.doi.org/10.1055/s-0037-1610297.
Texto completo da fonteGorlatova, Natalia, Marek Tchorzewski, Tatsuo Kurihara, Kenji Soda e Nobuyoshi Esaki. "Purification, Characterization, and Mechanism of a Flavin Mononucleotide-Dependent 2-Nitropropane Dioxygenase fromNeurospora crassa". Applied and Environmental Microbiology 64, n.º 3 (1 de março de 1998): 1029–33. http://dx.doi.org/10.1128/aem.64.3.1029-1033.1998.
Texto completo da fonteGao, Jinmin, Liyuan Li, Shijie Shen, Guomin Ai, Bin Wang, Fang Guo, Tongjian Yang et al. "Cofactor-independent C–C bond cleavage reactions catalyzed by the AlpJ family of oxygenases in atypical angucycline biosynthesis". Beilstein Journal of Organic Chemistry 20 (23 de maio de 2024): 1198–206. http://dx.doi.org/10.3762/bjoc.20.102.
Texto completo da fonteChamizo-Ampudia, Alejandro, Aurora Galvan, Emilio Fernandez e Angel Llamas. "The Chlamydomonas reinhardtii Molybdenum Cofactor Enzyme crARC Has a Zn-Dependent Activity and Protein Partners Similar to Those of Its Human Homologue". Eukaryotic Cell 10, n.º 10 (29 de julho de 2011): 1270–82. http://dx.doi.org/10.1128/ec.05096-11.
Texto completo da fonteYanase, Takumi, Junko Okuda-Shimazaki, Ryutaro Asano, Kazunori Ikebukuro, Koji Sode e Wakako Tsugawa. "Development of a Versatile Method to Construct Direct Electron Transfer-Type Enzyme Complexes Employing SpyCatcher/SpyTag System". International Journal of Molecular Sciences 24, n.º 3 (17 de janeiro de 2023): 1837. http://dx.doi.org/10.3390/ijms24031837.
Texto completo da fonteBuey, Rubén, Ruth Schmitz, Bob Buchanan e Monica Balsera. "Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon". Antioxidants 7, n.º 11 (17 de novembro de 2018): 166. http://dx.doi.org/10.3390/antiox7110166.
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