Artículos de revistas sobre el tema "PLP-dependent enzyme"
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Ngo, Ho-Phuong-Thuy, Nuno M. F. S. A. Cerqueira, Jin-Kwang Kim, Myoung-Ki Hong, Pedro Alexandrino Fernandes, Maria João Ramos y Lin-Woo Kang. "PLP undergoes conformational changes during the course of an enzymatic reaction". Acta Crystallographica Section D Biological Crystallography 70, n.º 2 (31 de enero de 2014): 596–606. http://dx.doi.org/10.1107/s1399004713031283.
Texto completoAL Mughram, Mohammed H., Mohini S. Ghatge, Glen E. Kellogg y Martin K. Safo. "Elucidating the Interaction between Pyridoxine 5′-Phosphate Oxidase and Dopa Decarboxylase: Activation of B6-Dependent Enzyme". International Journal of Molecular Sciences 24, n.º 1 (30 de diciembre de 2022): 642. http://dx.doi.org/10.3390/ijms24010642.
Texto completoKawakami, Ryushi, Chinatsu Kinoshita, Tomoki Kawase, Mikio Sato, Junji Hayashi, Haruhiko Sakuraba y Toshihisa Ohshima. "Characterization of a novel moderate-substrate specificity amino acid racemase from the hyperthermophilic archaeon Thermococcus litoralis". Bioscience, Biotechnology, and Biochemistry 85, n.º 7 (4 de mayo de 2021): 1650–57. http://dx.doi.org/10.1093/bbb/zbab078.
Texto completoZou, Lingling, Yang Song, Chengliang Wang, Jiaqi Sun, Leilei Wang, Beijiu Cheng y Jun Fan. "Crystal structure of maize serine racemase with pyridoxal 5′-phosphate". Acta Crystallographica Section F Structural Biology Communications 72, n.º 3 (16 de febrero de 2016): 165–71. http://dx.doi.org/10.1107/s2053230x16000960.
Texto completoRocha, Juliana F., André F. Pina, Sérgio F. Sousa y Nuno M. F. S. A. Cerqueira. "PLP-dependent enzymes as important biocatalysts for the pharmaceutical, chemical and food industries: a structural and mechanistic perspective". Catalysis Science & Technology 9, n.º 18 (2019): 4864–76. http://dx.doi.org/10.1039/c9cy01210a.
Texto completoYoshikane, Yu, Nana Yokochi, Kouhei Ohnishi, Hideyuki Hayashi y Toshiharu Yagi. "Molecular cloning, expression and characterization of pyridoxamine–pyruvate aminotransferase". Biochemical Journal 396, n.º 3 (29 de mayo de 2006): 499–507. http://dx.doi.org/10.1042/bj20060078.
Texto completoWilliamson, P. R., J. M. Kittler, J. W. Thanassi y H. M. Kagan. "Reactivity of a functional carbonyl moiety in bovine aortic lysyl oxidase. Evidence against pyridoxal 5′-phosphate". Biochemical Journal 235, n.º 2 (15 de abril de 1986): 597–605. http://dx.doi.org/10.1042/bj2350597.
Texto completoMOORE, Patrick S., Paola DOMINICI y Carla BORRI VOLTATTORNI. "Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes". Biochemical Journal 315, n.º 1 (1 de abril de 1996): 249–56. http://dx.doi.org/10.1042/bj3150249.
Texto completoKezuka, Yuichiro, Yasuo Yoshida y Takamasa Nonaka. "Structure of hydrogen sulfide-producing enzyme from a periodontal pathogen". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C454. http://dx.doi.org/10.1107/s205327331409545x.
Texto completoGao, Sisi, Huanting Liu, Valérie de Crécy-Lagard, Wen Zhu, Nigel G. J. Richards y James H. Naismith. "PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis". Chemical Communications 55, n.º 96 (2019): 14502–5. http://dx.doi.org/10.1039/c9cc06975e.
Texto completoRaasakka, Arne, Elaheh Mahootchi, Ingeborg Winge, Weisha Luan, Petri Kursula y Jan Haavik. "Structure of the mouse acidic amino acid decarboxylase GADL1". Acta Crystallographica Section F Structural Biology Communications 74, n.º 1 (1 de enero de 2018): 65–73. http://dx.doi.org/10.1107/s2053230x17017848.
Texto completoMizobuchi, Taichi, Risako Nonaka, Motoki Yoshimura, Katsumasa Abe, Shouji Takahashi, Yoshio Kera y Masaru Goto. "Crystal structure of a pyridoxal 5′-phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca broughtonii". Acta Crystallographica Section F Structural Biology Communications 73, n.º 12 (6 de noviembre de 2017): 651–56. http://dx.doi.org/10.1107/s2053230x17015813.
Texto completoDeka, Geeta, Shveta Bisht, H. S. Savithri y M. R. N. Murthy. "Structural studies on the catalytic mechanism of Diaminopropionate ammonia lyase". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C1822. http://dx.doi.org/10.1107/s2053273314081789.
Texto completoBorchert, Andrew J., Jacquelyn M. Walejko, Adrien Le Guennec, Dustin C. Ernst, Arthur S. Edison y Diana M. Downs. "Integrated Metabolomics and Transcriptomics Suggest the Global Metabolic Response to 2-Aminoacrylate Stress in Salmonella enterica". Metabolites 10, n.º 1 (24 de diciembre de 2019): 12. http://dx.doi.org/10.3390/metabo10010012.
Texto completoHan, Qinghong, Mingxu Xu, Li Tang, Xuezhong Tan, Xiuying Tan, Yuying Tan y Robert M. Hoffman. "Homogeneous, Nonradioactive, Enzymatic Assay for Plasma Pyridoxal 5-Phosphate". Clinical Chemistry 48, n.º 9 (1 de septiembre de 2002): 1560–64. http://dx.doi.org/10.1093/clinchem/48.9.1560.
Texto completoJALA, Venkatakrishna Rao, Naropantul APPAJI RAO y Handanahal Subbarao SAVITHRI. "Identification of amino acid residues, essential for maintaining the tetrameric structure of sheep liver cytosolic serine hydroxymethyltransferase, by targeted mutagenesis". Biochemical Journal 369, n.º 3 (1 de febrero de 2003): 469–76. http://dx.doi.org/10.1042/bj20021160.
Texto completoCampanini, Barbara, Stefano Bettati, Martino Luigi di Salvo, Andrea Mozzarelli y Roberto Contestabile. "Asymmetry of the Active Site Loop Conformation between Subunits of Glutamate-1-semialdehyde Aminomutase in Solution". BioMed Research International 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/353270.
Texto completoDeshmukh, Ashish y Balasubramanian Gopal. "Structural insights into the catalytic mechanism of Bacillus subtilis BacF". Acta Crystallographica Section F Structural Biology Communications 76, n.º 3 (1 de marzo de 2020): 145–51. http://dx.doi.org/10.1107/s2053230x20001636.
Texto completoCellini, Barbara, Mariarita Bertoldi, Riccardo Montioli, Alessandro Paiardini y Carla Borri Voltattorni. "Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications". Biochemical Journal 408, n.º 1 (29 de octubre de 2007): 39–50. http://dx.doi.org/10.1042/bj20070637.
Texto completoSteffen-Munsberg, Fabian, Clare Vickers, Hannes Kohls, Henrik Land, Hendrik Mallin, Alberto Nobili, Lilly Skalden et al. "Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications". Biotechnology Advances 33, n.º 5 (septiembre de 2015): 566–604. http://dx.doi.org/10.1016/j.biotechadv.2014.12.012.
Texto completoMukherjee, Mandira, Stuart A. Sievers, Mark T. Brown y Patricia J. Johnson. "Identification and Biochemical Characterization of Serine Hydroxymethyl Transferase in the Hydrogenosome of Trichomonas vaginalis". Eukaryotic Cell 5, n.º 12 (15 de septiembre de 2006): 2072–78. http://dx.doi.org/10.1128/ec.00249-06.
Texto completoIkushiro, Hiroko, Mohammad Mainul Islam, Hiromasa Tojo y Hideyuki Hayashi. "Molecular Characterization of Membrane-Associated Soluble Serine Palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii". Journal of Bacteriology 189, n.º 15 (8 de junio de 2007): 5749–61. http://dx.doi.org/10.1128/jb.00194-07.
Texto completoMirzaei, Mitra y Per Berglund. "Engineering of ωTransaminase for Effective Production of Chiral Amines". Journal of Computational and Theoretical Nanoscience 17, n.º 6 (1 de junio de 2020): 2827–32. http://dx.doi.org/10.1166/jctn.2020.8947.
Texto completoKasaragod, Vikram Babu, Anabel Pacios-Michelena, Natascha Schaefer, Fang Zheng, Nicole Bader, Christian Alzheimer, Carmen Villmann y Hermann Schindelin. "Pyridoxal kinase inhibition by artemisinins down-regulates inhibitory neurotransmission". Proceedings of the National Academy of Sciences 117, n.º 52 (14 de diciembre de 2020): 33235–45. http://dx.doi.org/10.1073/pnas.2008695117.
Texto completoDajnowicz, Steven, Matthew Blakeley, David Keen, Andrey Kovalevsky y Timothy Mueser. "Direct observation of protonation states in a PLP-dependent enzyme by neutron crystallography". Acta Crystallographica Section A Foundations and Advances 73, a1 (26 de mayo de 2017): a26. http://dx.doi.org/10.1107/s0108767317099731.
Texto completoMUHAMMAD, MURTALA, YANGYANG LI, SIYU GONG, YANMIN SHI, JIANSONG JU, BAOHUA ZHAO y DONG LIU. "Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain of Streptococcus iniae". Polish Journal of Microbiology 68, n.º 3 (septiembre de 2019): 331–41. http://dx.doi.org/10.33073/pjm-2019-036.
Texto completoBeattie, Ashley E., Sita D. Gupta, Lenka Frankova, Agne Kazlauskaite, Jeffrey M. Harmon, Teresa M. Dunn y Dominic J. Campopiano. "The Pyridoxal 5′-Phosphate (PLP)-Dependent Enzyme Serine Palmitoyltransferase (SPT): Effects of the Small Subunits and Insights from Bacterial Mimics of Human hLCB2a HSAN1 Mutations". BioMed Research International 2013 (2013): 1–13. http://dx.doi.org/10.1155/2013/194371.
Texto completoAsojo, Oluwatoyin A., Sarah K. Nelson, Sara Mootien, Yashang Lee, Wanderson C. Rezende, Daniel A. Hyman, Monica M. Matsumoto et al. "Structural and biochemical analyses of alanine racemase from the multidrug-resistantClostridium difficilestrain 630". Acta Crystallographica Section D Biological Crystallography 70, n.º 7 (29 de junio de 2014): 1922–33. http://dx.doi.org/10.1107/s1399004714009419.
Texto completoDai, Guang Zhi, Wen Bo Han, Ya Ning Mei, Kuang Xu, Rui Hua Jiao, Hui Ming Ge y Ren Xiang Tan. "Pyridoxal-5′-phosphate–dependent bifunctional enzyme catalyzed biosynthesis of indolizidine alkaloids in fungi". Proceedings of the National Academy of Sciences 117, n.º 2 (27 de diciembre de 2019): 1174–80. http://dx.doi.org/10.1073/pnas.1914777117.
Texto completoChen, Hao-Ping, Chin-Fen Lin, Ya-Jung Lee, San-San Tsay y Shih-Hsiung Wu. "Purification and Properties of Ornithine Racemase from Clostridium sticklandii". Journal of Bacteriology 182, n.º 7 (1 de abril de 2000): 2052–54. http://dx.doi.org/10.1128/jb.182.7.2052-2054.2000.
Texto completoGaskin, Peter J., Harriet J. Adcock, Lorraine D. Buckberry, Paul H. Teesdale-Spittle y P. Nicholas Shawl. "The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes". Human & Experimental Toxicology 14, n.º 5 (mayo de 1995): 422–27. http://dx.doi.org/10.1177/096032719501400506.
Texto completoVozdek, Roman, Aleš Hnízda, Jakub Krijt, Marta Kostrouchová y Viktor Kožich. "Novel structural arrangement of nematode cystathionine β-synthases: characterization of Caenorhabditis elegans CBS-1". Biochemical Journal 443, n.º 2 (27 de marzo de 2012): 535–47. http://dx.doi.org/10.1042/bj20111478.
Texto completoBERTOLDI, Mariarita, Barbara CELLINI, Alessandro PAIARDINI, Martino Di SALVO y Carla BORRIVOLTATTORNI. "Treponema denticola cystalysin exhibits significant alanine racemase activity accompanied by transamination: mechanistic implications1". Biochemical Journal 371, n.º 2 (15 de abril de 2003): 473–83. http://dx.doi.org/10.1042/bj20020875.
Texto completoSato, Dan, Tomoo Shiba, Sae Mizuno, Ayaka Kawamura, Shoko Hanada, Tetsuya Yamada, Mai Shinozaki et al. "The hyperthermophilic cystathionine γ-synthase from the aerobic crenarchaeonSulfolobus tokodaii: expression, purification, crystallization and structural insights". Acta Crystallographica Section F Structural Biology Communications 73, n.º 3 (21 de febrero de 2017): 152–58. http://dx.doi.org/10.1107/s2053230x17002011.
Texto completoYu, Xin-Jun, Chang-Yi Huang, Xiao-Dan Xu, Hong Chen, Miao-Jie Liang, Zhe-Xian Xu, Hui-Xia Xu y Zhao Wang. "Protein Engineering of a Pyridoxal-5′-Phosphate-Dependent l-Aspartate-α-Decarboxylase from Tribolium castaneum for β-Alanine Production". Molecules 25, n.º 6 (12 de marzo de 2020): 1280. http://dx.doi.org/10.3390/molecules25061280.
Texto completoBakunova, Alina K., Alena Yu Nikolaeva, Tatiana V. Rakitina, Tatiana Y. Isaikina, Maria G. Khrenova, Konstantin M. Boyko, Vladimir O. Popov y Ekaterina Yu Bezsudnova. "The Uncommon Active Site of D-Amino Acid Transaminase from Haliscomenobacter hydrossis: Biochemical and Structural Insights into the New Enzyme". Molecules 26, n.º 16 (20 de agosto de 2021): 5053. http://dx.doi.org/10.3390/molecules26165053.
Texto completoSköldberg, Filip, Fredrik Rorsman, Jaakko Perheentupa, Mona Landin-Olsson, Eystein S. Husebye, Jan Gustafsson y Olle Kämpe. "Analysis of Antibody Reactivity against Cysteine Sulfinic Acid Decarboxylase, A Pyridoxal Phosphate-Dependent Enzyme, in Endocrine Autoimmune Disease". Journal of Clinical Endocrinology & Metabolism 89, n.º 4 (1 de abril de 2004): 1636–40. http://dx.doi.org/10.1210/jc.2003-031161.
Texto completoWebster, Scott P., Dominic J. Campopiano, Dmitriy Alexeev, Marina Alexeeva, Rory M. Watt, Lindsay Sawyer y Robert L. Baxter. "Characterisation of 8-amino-7-oxononanoate synthase: A bacterial PLP-dependent, acyl CoA condensing enzyme". Biochemical Society Transactions 26, n.º 3 (1 de agosto de 1998): S268. http://dx.doi.org/10.1042/bst026s268.
Texto completoZhang, Hu, Zhao, Huang, Mei y Mei. "Parallel Strategy Increases the Thermostability and Activity of Glutamate Decarboxylase". Molecules 25, n.º 3 (6 de febrero de 2020): 690. http://dx.doi.org/10.3390/molecules25030690.
Texto completoBörner, Tim, Carl Grey y Patrick Adlercreutz. "Generic HPLC platform for automated enzyme reaction monitoring: Advancing the assay toolbox for transaminases and other PLP-dependent enzymes". Biotechnology Journal 11, n.º 8 (10 de junio de 2016): 1025–36. http://dx.doi.org/10.1002/biot.201500587.
Texto completoHasegawa, Takema, Diana Hapsari y Hitoshi Iwahashi. "RNase H-dependent amplification improves the accuracy of rolling circle amplification combined with loop-mediated isothermal amplification (RCA-LAMP)". PeerJ 9 (30 de julio de 2021): e11851. http://dx.doi.org/10.7717/peerj.11851.
Texto completoGraham, David E., Stephanie M. Taylor, Rachel Z. Wolf y Seema C. Namboori. "Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase". Biochemical Journal 424, n.º 3 (10 de diciembre de 2009): 467–78. http://dx.doi.org/10.1042/bj20090999.
Texto completoHo, Thien-Hoang, Kim-Hung Huynh, Diem Quynh Nguyen, Hyunjae Park, Kyoungho Jung, Bookyo Sur, Yeh-Jin Ahn, Sun-Shin Cha y Lin-Woo Kang. "Catalytic Intermediate Crystal Structures of Cysteine Desulfurase from the Archaeon Thermococcus onnurineus NA1". Archaea 2017 (2017): 1–11. http://dx.doi.org/10.1155/2017/5395293.
Texto completoDrake, Eric J. y Andrew M. Gulick. "1.2 Å resolution crystal structure of the periplasmic aminotransferase PvdN fromPseudomonas aeruginosa". Acta Crystallographica Section F Structural Biology Communications 72, n.º 5 (22 de abril de 2016): 403–8. http://dx.doi.org/10.1107/s2053230x16006257.
Texto completoBERTOLDI, Mariarita y Carla BORRI VOLTATTORNI. "Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions". Biochemical Journal 352, n.º 2 (24 de noviembre de 2000): 533–38. http://dx.doi.org/10.1042/bj3520533.
Texto completoFujino, A., T. Ose, M. Yao, M. Honma y I. Tanaka. "Catalytic activity analysis of PLP dependent enzyme PH0054 from hyperthermophilic archaebacteria P.horikoshii OT3 by X-ray crystallography". Seibutsu Butsuri 41, supplement (2001): S100. http://dx.doi.org/10.2142/biophys.41.s100_4.
Texto completoLambrecht, Jennifer A., Jeffrey M. Flynn y Diana M. Downs. "Conserved YjgF Protein Family Deaminates Reactive Enamine/Imine Intermediates of Pyridoxal 5′-Phosphate (PLP)-dependent Enzyme Reactions". Journal of Biological Chemistry 287, n.º 5 (17 de noviembre de 2011): 3454–61. http://dx.doi.org/10.1074/jbc.m111.304477.
Texto completoMurphy, Cormac D., David O'Hagan y Christoph Schaffrath. "Identification of a PLP-Dependent Threonine Transaldolase: A Novel Enzyme Involved in 4-Fluorothreonine Biosynthesis inStreptomyces cattleya". Angewandte Chemie 113, n.º 23 (3 de diciembre de 2001): 4611–13. http://dx.doi.org/10.1002/1521-3757(20011203)113:23<4611::aid-ange4611>3.0.co;2-u.
Texto completoNguyen, Diem-Quynh, Ho-Phuong-Thuy Ngo, Yeh-Jin Ahn, Sang Hee Lee y Lin-Woo Kang. "Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine β-lyase fromAcinetobacter baumanniiOXA-23". Acta Crystallographica Section F Structural Biology Communications 70, n.º 10 (25 de septiembre de 2014): 1368–71. http://dx.doi.org/10.1107/s2053230x14017981.
Texto completoMarienhagen, Jan, Nicole Kennerknecht, Hermann Sahm y Lothar Eggeling. "Functional Analysis of All Aminotransferase Proteins Inferred from the Genome Sequence of Corynebacterium glutamicum". Journal of Bacteriology 187, n.º 22 (15 de noviembre de 2005): 7639–46. http://dx.doi.org/10.1128/jb.187.22.7639-7646.2005.
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