Zeitschriftenartikel zum Thema „Flavin hydroquinone dependent Enzymes“
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Perry, Lynda L., und 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, Nr. 21 (24.08.2007): 7563–72. http://dx.doi.org/10.1128/jb.01849-06.
Der volle Inhalt der QuelleMihasan, Marius, Calin-Bogdan Chiribau, Thorsten Friedrich, Vlad Artenie und 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, Nr. 8 (09.02.2007): 2479–85. http://dx.doi.org/10.1128/aem.02668-06.
Der volle Inhalt der QuelleHyster, Todd K. „Radical Biocatalysis: Using Non-Natural Single Electron Transfer Mechanisms to Access New Enzymatic Functions“. Synlett 31, Nr. 03 (07.05.2019): 248–54. http://dx.doi.org/10.1055/s-0037-1611818.
Der volle Inhalt der QuelleWojcieszyńska, Danuta, Katarzyna Hupert-Kocurek und Urszula Guzik. „Flavin-Dependent Enzymes in Cancer Prevention“. International Journal of Molecular Sciences 13, Nr. 12 (07.12.2012): 16751–68. http://dx.doi.org/10.3390/ijms131216751.
Der volle Inhalt der QuelleHilvert, Donald, und E. T. Kaisert. „Semisynthetic Enzymes: Design of Flavin-Dependent Oxidoreductases“. Biotechnology and Genetic Engineering Reviews 5, Nr. 1 (September 1987): 297–318. http://dx.doi.org/10.1080/02648725.1987.10647841.
Der volle Inhalt der QuelleMenon, Binuraj R. K., Jonathan Latham, Mark S. Dunstan, Eileen Brandenburger, Ulrike Klemstein, David Leys, Chinnan Karthikeyan, Michael F. Greaney, Sarah A. Shepherd und Jason Micklefield. „Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes“. Organic & Biomolecular Chemistry 14, Nr. 39 (2016): 9354–61. http://dx.doi.org/10.1039/c6ob01861k.
Der volle Inhalt der QuelleMügge, Carolin, Thomas Heine, Alvaro Gomez Baraibar, Willem J. H. van Berkel, Caroline E. Paul und Dirk Tischler. „Flavin-dependent N-hydroxylating enzymes: distribution and application“. Applied Microbiology and Biotechnology 104, Nr. 15 (05.06.2020): 6481–99. http://dx.doi.org/10.1007/s00253-020-10705-w.
Der volle Inhalt der QuelleMoon, Shin und Choe. „Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius“. Crystals 9, Nr. 11 (23.10.2019): 548. http://dx.doi.org/10.3390/cryst9110548.
Der volle Inhalt der QuelleShepherd, Sarah A., Chinnan Karthikeyan, Jonathan Latham, Anna-Winona Struck, Mark L. Thompson, Binuraj R. K. Menon, Matthew Q. Styles, Colin Levy, David Leys und Jason Micklefield. „Extending the biocatalytic scope of regiocomplementary flavin-dependent halogenase enzymes“. Chemical Science 6, Nr. 6 (2015): 3454–60. http://dx.doi.org/10.1039/c5sc00913h.
Der volle Inhalt der QuelleSaleem-Batcha, Raspudin, Frederick Stull, Jacob N. Sanders, Bradley S. Moore, Bruce A. Palfey, K. N. Houk und Robin Teufel. „Enzymatic control of dioxygen binding and functionalization of the flavin cofactor“. Proceedings of the National Academy of Sciences 115, Nr. 19 (23.04.2018): 4909–14. http://dx.doi.org/10.1073/pnas.1801189115.
Der volle Inhalt der Quellede Gonzalo, Gonzalo, und Andrés R. Alcántara. „Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases“. Catalysts 11, Nr. 5 (08.05.2021): 605. http://dx.doi.org/10.3390/catal11050605.
Der volle Inhalt der QuelleZhang, Jun-Jie, Hong Liu, Yi Xiao, Xian-En Zhang und 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, Nr. 8 (13.02.2009): 2703–10. http://dx.doi.org/10.1128/jb.01566-08.
Der volle Inhalt der QuelleDick, Scott, Laura Marrone, Abraham M. Thariath, Miguel A. Valvano und Thammaiah Viswanatha. „Cofactor- and substrate-binding domains in flavin-dependent N-hydroxylating enzymes“. Trends in Biochemical Sciences 23, Nr. 11 (November 1998): 414. http://dx.doi.org/10.1016/s0968-0004(98)01271-7.
Der volle Inhalt der QuelleWang, Jinyu, und Yajun Liu. „Systematic Theoretical Study on the pH-Dependent Absorption and Fluorescence Spectra of Flavins“. Molecules 28, Nr. 8 (08.04.2023): 3315. http://dx.doi.org/10.3390/molecules28083315.
Der volle Inhalt der QuelleZverinsky, I. V., H. G. Zverinskaya, I. P. Sutsko, P. G. Telegin und A. G. Shlyahtun. „Effects of berberine on the recovery of rat liver xenobiotic-metabolizing enzymes after partial hepatectomy“. Biomeditsinskaya Khimiya 61, Nr. 3 (2015): 381–83. http://dx.doi.org/10.18097/pbmc20156103381.
Der volle Inhalt der QuelleMcLEAN, Kirsty J., Nigel S. SCRUTTON und Andrew W. MUNRO. „Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA“. Biochemical Journal 372, Nr. 2 (01.06.2003): 317–27. http://dx.doi.org/10.1042/bj20021692.
Der volle Inhalt der QuelleHuang, Yan, Randy Xun, Guanjun Chen und Luying Xun. „Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723“. Journal of Bacteriology 190, Nr. 23 (26.09.2008): 7595–600. http://dx.doi.org/10.1128/jb.00489-08.
Der volle Inhalt der QuelleWick, Jonas, Daniel Heine, Gerald Lackner, Mathias Misiek, James Tauber, Hans Jagusch, Christian Hertweck und Dirk Hoffmeister. „A Fivefold Parallelized Biosynthetic Process Secures Chlorination of Armillaria mellea (Honey Mushroom) Toxins“. Applied and Environmental Microbiology 82, Nr. 4 (11.12.2015): 1196–204. http://dx.doi.org/10.1128/aem.03168-15.
Der volle Inhalt der QuelleNeubauer, Pia R., Olga Blifernez-Klassen, Lara Pfaff, Mohamed Ismail, Olaf Kruse und Norbert Sewald. „Two Novel, Flavin-Dependent Halogenases from the Bacterial Consortia of Botryococcus braunii Catalyze Mono- and Dibromination“. Catalysts 11, Nr. 4 (10.04.2021): 485. http://dx.doi.org/10.3390/catal11040485.
Der volle Inhalt der QuelleAndorfer, Mary C., und Jared C. Lewis. „Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis“. Annual Review of Biochemistry 87, Nr. 1 (20.06.2018): 159–85. http://dx.doi.org/10.1146/annurev-biochem-062917-012042.
Der volle Inhalt der QuelleHeine, Thomas, Willem van Berkel, George Gassner, Karl-Heinz van Pée und Dirk Tischler. „Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities“. Biology 7, Nr. 3 (02.08.2018): 42. http://dx.doi.org/10.3390/biology7030042.
Der volle Inhalt der QuellePozzi, Cecilia, Ludovica Lopresti, Giusy Tassone und Stefano Mangani. „Targeting Methyltransferases in Human Pathogenic Bacteria: Insights into Thymidylate Synthase (TS) and Flavin-Dependent TS (FDTS)“. Molecules 24, Nr. 8 (25.04.2019): 1638. http://dx.doi.org/10.3390/molecules24081638.
Der volle Inhalt der QuelleBiegasiewicz, 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 und Todd K. Hyster. „Photoexcitation of flavoenzymes enables a stereoselective radical cyclization“. Science 364, Nr. 6446 (20.06.2019): 1166–69. http://dx.doi.org/10.1126/science.aaw1143.
Der volle Inhalt der QuelleFejzagić, Alexander Veljko, Jan Gebauer, Nikolai Huwa und Thomas Classen. „Halogenating Enzymes for Active Agent Synthesis: First Steps Are Done and Many Have to Follow“. Molecules 24, Nr. 21 (05.11.2019): 4008. http://dx.doi.org/10.3390/molecules24214008.
Der volle Inhalt der QuellePimviriyakul, Panu, Panida Surawatanawong und Pimchai Chaiyen. „Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonation“. Chemical Science 9, Nr. 38 (2018): 7468–82. http://dx.doi.org/10.1039/c8sc01482e.
Der volle Inhalt der QuelleWilletts, Andrew. „The Isoenzymic Diketocamphane Monooxygenases of Pseudomonas putida ATCC 17453—An Episodic History and Still Mysterious after 60 Years“. Microorganisms 9, Nr. 12 (15.12.2021): 2593. http://dx.doi.org/10.3390/microorganisms9122593.
Der volle Inhalt der QuelleUng, Kien Lam, Chloé Poussineau, Julie Couston, Husam M. A. B. Alsarraf und Mickaël Blaise. „Crystal structure of MAB_4123, a putative flavin-dependent monooxygenase from Mycobacterium abscessus“. Acta Crystallographica Section F Structural Biology Communications 79, Nr. 5 (01.05.2023): 128–36. http://dx.doi.org/10.1107/s2053230x2300345x.
Der volle Inhalt der QuellePimviriyakul, Panu, und Pimchai Chaiyen. „A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin–dependent enzymes“. Journal of Biological Chemistry 293, Nr. 48 (03.10.2018): 18525–39. http://dx.doi.org/10.1074/jbc.ra118.005538.
Der volle Inhalt der QuelleShah, Mihir V., James Antoney, Suk Woo Kang, Andrew C. Warden, Carol J. Hartley, Hadi Nazem-Bokaee, Colin J. Jackson und Colin Scott. „Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis“. Catalysts 9, Nr. 10 (20.10.2019): 868. http://dx.doi.org/10.3390/catal9100868.
Der volle Inhalt der QuelleCapeillère-Blandin, C., M. J. Barber und 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, Nr. 3 (15.09.1986): 745–56. http://dx.doi.org/10.1042/bj2380745.
Der volle Inhalt der QuelleFerreira, Maria Isabel M., Toshiya Iida, Syed A. Hasan, Kaoru Nakamura, Marco W. Fraaije, Dick B. Janssen und Toshiaki Kudo. „Analysis of Two Gene Clusters Involved in the Degradation of 4-Fluorophenol by Arthrobacter sp. Strain IF1“. Applied and Environmental Microbiology 75, Nr. 24 (16.10.2009): 7767–73. http://dx.doi.org/10.1128/aem.00171-09.
Der volle Inhalt der QuelleDeng, Yaming, Quan Zhou, Yuzhou Wu, Xi Chen und Fangrui Zhong. „Properties and Mechanisms of Flavin-Dependent Monooxygenases and Their Applications in Natural Product Synthesis“. International Journal of Molecular Sciences 23, Nr. 5 (27.02.2022): 2622. http://dx.doi.org/10.3390/ijms23052622.
Der volle Inhalt der QuelleChanda, Kakoli, Atifa Begum Mozumder, Ringhoilal Chorei, Ridip Kumar Gogoi und 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, Nr. 10 (22.09.2021): 785. http://dx.doi.org/10.3390/jof7100785.
Der volle Inhalt der QuelleManenda, Mahder S., Marie-Ève Picard, Liping Zhang, Normand Cyr, Xiaojun Zhu, Julie Barma, John M. Pascal, Manon Couture, Changsheng Zhang und 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, Nr. 14 (28.02.2020): 4709–22. http://dx.doi.org/10.1074/jbc.ra119.011212.
Der volle Inhalt der QuelleOgawa, Aoba, Gen-ichi Sampei und 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, Nr. 6 (01.06.2019): 450–54. http://dx.doi.org/10.1107/s2053230x19007192.
Der volle Inhalt der QuelleMączka, Wanda, Katarzyna Wińska und Małgorzata Grabarczyk. „Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow“. Catalysts 8, Nr. 12 (05.12.2018): 624. http://dx.doi.org/10.3390/catal8120624.
Der volle Inhalt der QuelleBuss, Maren, Christina Geerds, Thomas Patschkowski, Karsten Niehaus und 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, Nr. 6 (18.05.2018): 345–50. http://dx.doi.org/10.1107/s2053230x18006933.
Der volle Inhalt der QuelleMatsubara, Toshiyuki, Takashi Ohshiro, Yoshihiro Nishina und Yoshikazu Izumi. „Purification, Characterization, and Overexpression of Flavin Reductase Involved in Dibenzothiophene Desulfurization byRhodococcus erythropolis D-1“. Applied and Environmental Microbiology 67, Nr. 3 (01.03.2001): 1179–84. http://dx.doi.org/10.1128/aem.67.3.1179-1184.
Der volle Inhalt der QuelleWilliams, Richard E., Deborah A. Rathbone, Nigel S. Scrutton und Neil C. Bruce. „Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins“. Applied and Environmental Microbiology 70, Nr. 6 (Juni 2004): 3566–74. http://dx.doi.org/10.1128/aem.70.6.3566-3574.2004.
Der volle Inhalt der QuelleMessiha, Hanan L., Thanyaporn Wongnate, Pimchai Chaiyen, Alex R. Jones und 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, Nr. 103 (Februar 2015): 20141155. http://dx.doi.org/10.1098/rsif.2014.1155.
Der volle Inhalt der QuelleKassay, Norbert, Vanda Toldi, József Tőzsér und András Szabó. „Cigarette smoke toxin hydroquinone and misfolding pancreatic lipase variant cooperatively promote endoplasmic reticulum stress and cell death“. PLOS ONE 17, Nr. 6 (15.06.2022): e0269936. http://dx.doi.org/10.1371/journal.pone.0269936.
Der volle Inhalt der QuelleSpohn, 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, Nr. 06 (2009): 1044–50. http://dx.doi.org/10.1160/th09-03-0204.
Der volle Inhalt der QuelleRoberts, Kenneth M., José R. Tormos und Paul F. Fitzpatrick. „Characterization of Unstable Products of Flavin- and Pterin-Dependent Enzymes by Continuous-Flow Mass Spectrometry“. Biochemistry 53, Nr. 16 (18.04.2014): 2672–79. http://dx.doi.org/10.1021/bi500267c.
Der volle Inhalt der QuelleDzeja, Petras P., Peter Bast, Cevher Ozcan, Arturo Valverde, Ekshon L. Holmuhamedov, David G. L. Van Wylen und Andre Terzic. „Targeting nucleotide-requiring enzymes: implications for diazoxide-induced cardioprotection“. American Journal of Physiology-Heart and Circulatory Physiology 284, Nr. 4 (01.04.2003): H1048—H1056. http://dx.doi.org/10.1152/ajpheart.00847.2002.
Der volle Inhalt der QuelleZografos, Alexandros, und Marina Petsi. „Advances in Catalytic Aerobic Oxidations by Activation of Dioxygen-Monooxygenase Enzymes and Biomimetics“. Synthesis 50, Nr. 24 (15.10.2018): 4715–45. http://dx.doi.org/10.1055/s-0037-1610297.
Der volle Inhalt der QuelleGorlatova, Natalia, Marek Tchorzewski, Tatsuo Kurihara, Kenji Soda und Nobuyoshi Esaki. „Purification, Characterization, and Mechanism of a Flavin Mononucleotide-Dependent 2-Nitropropane Dioxygenase fromNeurospora crassa“. Applied and Environmental Microbiology 64, Nr. 3 (01.03.1998): 1029–33. http://dx.doi.org/10.1128/aem.64.3.1029-1033.1998.
Der volle Inhalt der QuelleGao, 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 (23.05.2024): 1198–206. http://dx.doi.org/10.3762/bjoc.20.102.
Der volle Inhalt der QuelleChamizo-Ampudia, Alejandro, Aurora Galvan, Emilio Fernandez und 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, Nr. 10 (29.07.2011): 1270–82. http://dx.doi.org/10.1128/ec.05096-11.
Der volle Inhalt der QuelleYanase, Takumi, Junko Okuda-Shimazaki, Ryutaro Asano, Kazunori Ikebukuro, Koji Sode und 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, Nr. 3 (17.01.2023): 1837. http://dx.doi.org/10.3390/ijms24031837.
Der volle Inhalt der QuelleBuey, Rubén, Ruth Schmitz, Bob Buchanan und Monica Balsera. „Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon“. Antioxidants 7, Nr. 11 (17.11.2018): 166. http://dx.doi.org/10.3390/antiox7110166.
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