Artykuły w czasopismach na temat „Flavin hydroquinone dependent Enzymes”
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Perry, Lynda L., i 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.
Pełny tekst źródłaMihasan, Marius, Calin-Bogdan Chiribau, Thorsten Friedrich, Vlad Artenie i 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 (9.02.2007): 2479–85. http://dx.doi.org/10.1128/aem.02668-06.
Pełny tekst źródłaHyster, Todd K. "Radical Biocatalysis: Using Non-Natural Single Electron Transfer Mechanisms to Access New Enzymatic Functions". Synlett 31, nr 03 (7.05.2019): 248–54. http://dx.doi.org/10.1055/s-0037-1611818.
Pełny tekst źródłaWojcieszyńska, Danuta, Katarzyna Hupert-Kocurek i Urszula Guzik. "Flavin-Dependent Enzymes in Cancer Prevention". International Journal of Molecular Sciences 13, nr 12 (7.12.2012): 16751–68. http://dx.doi.org/10.3390/ijms131216751.
Pełny tekst źródłaHilvert, Donald, i E. T. Kaisert. "Semisynthetic Enzymes: Design of Flavin-Dependent Oxidoreductases". Biotechnology and Genetic Engineering Reviews 5, nr 1 (wrzesień 1987): 297–318. http://dx.doi.org/10.1080/02648725.1987.10647841.
Pełny tekst źródłaMenon, Binuraj R. K., Jonathan Latham, Mark S. Dunstan, Eileen Brandenburger, Ulrike Klemstein, David Leys, Chinnan Karthikeyan, Michael F. Greaney, Sarah A. Shepherd i 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.
Pełny tekst źródłaMügge, Carolin, Thomas Heine, Alvaro Gomez Baraibar, Willem J. H. van Berkel, Caroline E. Paul i Dirk Tischler. "Flavin-dependent N-hydroxylating enzymes: distribution and application". Applied Microbiology and Biotechnology 104, nr 15 (5.06.2020): 6481–99. http://dx.doi.org/10.1007/s00253-020-10705-w.
Pełny tekst źródłaMoon, Shin i 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.
Pełny tekst źródłaShepherd, Sarah A., Chinnan Karthikeyan, Jonathan Latham, Anna-Winona Struck, Mark L. Thompson, Binuraj R. K. Menon, Matthew Q. Styles, Colin Levy, David Leys i 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.
Pełny tekst źródłaSaleem-Batcha, Raspudin, Frederick Stull, Jacob N. Sanders, Bradley S. Moore, Bruce A. Palfey, K. N. Houk i 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.
Pełny tekst źródłade Gonzalo, Gonzalo, i Andrés R. Alcántara. "Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases". Catalysts 11, nr 5 (8.05.2021): 605. http://dx.doi.org/10.3390/catal11050605.
Pełny tekst źródłaZhang, Jun-Jie, Hong Liu, Yi Xiao, Xian-En Zhang i 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.
Pełny tekst źródłaDick, Scott, Laura Marrone, Abraham M. Thariath, Miguel A. Valvano i Thammaiah Viswanatha. "Cofactor- and substrate-binding domains in flavin-dependent N-hydroxylating enzymes". Trends in Biochemical Sciences 23, nr 11 (listopad 1998): 414. http://dx.doi.org/10.1016/s0968-0004(98)01271-7.
Pełny tekst źródłaWang, Jinyu, i Yajun Liu. "Systematic Theoretical Study on the pH-Dependent Absorption and Fluorescence Spectra of Flavins". Molecules 28, nr 8 (8.04.2023): 3315. http://dx.doi.org/10.3390/molecules28083315.
Pełny tekst źródłaZverinsky, I. V., H. G. Zverinskaya, I. P. Sutsko, P. G. Telegin i 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.
Pełny tekst źródłaMcLEAN, Kirsty J., Nigel S. SCRUTTON i Andrew W. MUNRO. "Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA". Biochemical Journal 372, nr 2 (1.06.2003): 317–27. http://dx.doi.org/10.1042/bj20021692.
Pełny tekst źródłaHuang, Yan, Randy Xun, Guanjun Chen i 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.
Pełny tekst źródłaWick, Jonas, Daniel Heine, Gerald Lackner, Mathias Misiek, James Tauber, Hans Jagusch, Christian Hertweck i 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.
Pełny tekst źródłaNeubauer, Pia R., Olga Blifernez-Klassen, Lara Pfaff, Mohamed Ismail, Olaf Kruse i 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.
Pełny tekst źródłaAndorfer, Mary C., i 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.
Pełny tekst źródłaHeine, Thomas, Willem van Berkel, George Gassner, Karl-Heinz van Pée i Dirk Tischler. "Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities". Biology 7, nr 3 (2.08.2018): 42. http://dx.doi.org/10.3390/biology7030042.
Pełny tekst źródłaPozzi, Cecilia, Ludovica Lopresti, Giusy Tassone i 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.
Pełny tekst źródłaBiegasiewicz, 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 i 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.
Pełny tekst źródłaFejzagić, Alexander Veljko, Jan Gebauer, Nikolai Huwa i Thomas Classen. "Halogenating Enzymes for Active Agent Synthesis: First Steps Are Done and Many Have to Follow". Molecules 24, nr 21 (5.11.2019): 4008. http://dx.doi.org/10.3390/molecules24214008.
Pełny tekst źródłaPimviriyakul, Panu, Panida Surawatanawong i 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.
Pełny tekst źródłaWilletts, 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.
Pełny tekst źródłaUng, Kien Lam, Chloé Poussineau, Julie Couston, Husam M. A. B. Alsarraf i 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 (1.05.2023): 128–36. http://dx.doi.org/10.1107/s2053230x2300345x.
Pełny tekst źródłaPimviriyakul, Panu, i Pimchai Chaiyen. "A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin–dependent enzymes". Journal of Biological Chemistry 293, nr 48 (3.10.2018): 18525–39. http://dx.doi.org/10.1074/jbc.ra118.005538.
Pełny tekst źródłaShah, Mihir V., James Antoney, Suk Woo Kang, Andrew C. Warden, Carol J. Hartley, Hadi Nazem-Bokaee, Colin J. Jackson i 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.
Pełny tekst źródłaCapeillère-Blandin, C., M. J. Barber i 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.
Pełny tekst źródłaFerreira, Maria Isabel M., Toshiya Iida, Syed A. Hasan, Kaoru Nakamura, Marco W. Fraaije, Dick B. Janssen i 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.
Pełny tekst źródłaDeng, Yaming, Quan Zhou, Yuzhou Wu, Xi Chen i 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.
Pełny tekst źródłaChanda, Kakoli, Atifa Begum Mozumder, Ringhoilal Chorei, Ridip Kumar Gogoi i 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.
Pełny tekst źródłaManenda, Mahder S., Marie-Ève Picard, Liping Zhang, Normand Cyr, Xiaojun Zhu, Julie Barma, John M. Pascal, Manon Couture, Changsheng Zhang i 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.
Pełny tekst źródłaOgawa, Aoba, Gen-ichi Sampei i 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 (1.06.2019): 450–54. http://dx.doi.org/10.1107/s2053230x19007192.
Pełny tekst źródłaMączka, Wanda, Katarzyna Wińska i Małgorzata Grabarczyk. "Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow". Catalysts 8, nr 12 (5.12.2018): 624. http://dx.doi.org/10.3390/catal8120624.
Pełny tekst źródłaBuss, Maren, Christina Geerds, Thomas Patschkowski, Karsten Niehaus i 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.
Pełny tekst źródłaMatsubara, Toshiyuki, Takashi Ohshiro, Yoshihiro Nishina i Yoshikazu Izumi. "Purification, Characterization, and Overexpression of Flavin Reductase Involved in Dibenzothiophene Desulfurization byRhodococcus erythropolis D-1". Applied and Environmental Microbiology 67, nr 3 (1.03.2001): 1179–84. http://dx.doi.org/10.1128/aem.67.3.1179-1184.
Pełny tekst źródłaWilliams, Richard E., Deborah A. Rathbone, Nigel S. Scrutton i Neil C. Bruce. "Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins". Applied and Environmental Microbiology 70, nr 6 (czerwiec 2004): 3566–74. http://dx.doi.org/10.1128/aem.70.6.3566-3574.2004.
Pełny tekst źródłaMessiha, Hanan L., Thanyaporn Wongnate, Pimchai Chaiyen, Alex R. Jones i 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 (luty 2015): 20141155. http://dx.doi.org/10.1098/rsif.2014.1155.
Pełny tekst źródłaKassay, Norbert, Vanda Toldi, József Tőzsér i 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.
Pełny tekst źródłaSpohn, Gabriele, Andre Kleinridders, F. Thomas Wunderlich, Matthias Watzka, Frank Zaucke, Katrin Blum-bach, Christof Geisen i in. "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.
Pełny tekst źródłaRoberts, Kenneth M., José R. Tormos i 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.
Pełny tekst źródłaDzeja, Petras P., Peter Bast, Cevher Ozcan, Arturo Valverde, Ekshon L. Holmuhamedov, David G. L. Van Wylen i Andre Terzic. "Targeting nucleotide-requiring enzymes: implications for diazoxide-induced cardioprotection". American Journal of Physiology-Heart and Circulatory Physiology 284, nr 4 (1.04.2003): H1048—H1056. http://dx.doi.org/10.1152/ajpheart.00847.2002.
Pełny tekst źródłaZografos, Alexandros, i 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.
Pełny tekst źródłaGorlatova, Natalia, Marek Tchorzewski, Tatsuo Kurihara, Kenji Soda i Nobuyoshi Esaki. "Purification, Characterization, and Mechanism of a Flavin Mononucleotide-Dependent 2-Nitropropane Dioxygenase fromNeurospora crassa". Applied and Environmental Microbiology 64, nr 3 (1.03.1998): 1029–33. http://dx.doi.org/10.1128/aem.64.3.1029-1033.1998.
Pełny tekst źródłaGao, Jinmin, Liyuan Li, Shijie Shen, Guomin Ai, Bin Wang, Fang Guo, Tongjian Yang i in. "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.
Pełny tekst źródłaChamizo-Ampudia, Alejandro, Aurora Galvan, Emilio Fernandez i 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.
Pełny tekst źródłaYanase, Takumi, Junko Okuda-Shimazaki, Ryutaro Asano, Kazunori Ikebukuro, Koji Sode i 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.
Pełny tekst źródłaBuey, Rubén, Ruth Schmitz, Bob Buchanan i 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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