Статті в журналах з теми "Diaminopimelate epimerase"
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Miura, Hiromi, Kentaro Hori, Yosuke Sasaki, Yuki Inahashi, Yasufumi Yagisawa, Nobuyuki Fujita, Satoshi Ōmura, and Yōko Takahashi. "Simple analytic method of diaminopimelate epimerase activity." Journal of Bioscience and Bioengineering 116, no. 2 (August 2013): 253–55. http://dx.doi.org/10.1016/j.jbiosc.2013.02.015.
Повний текст джерелаUsha, Veeraraghavan, Lynn G. Dover, David I. Roper, Klaus Fütterer, and Gurdyal S. Besra. "Structure of the diaminopimelate epimerase DapF fromMycobacterium tuberculosis." Acta Crystallographica Section D Biological Crystallography 65, no. 4 (March 19, 2009): 383–87. http://dx.doi.org/10.1107/s0907444909002522.
Повний текст джерелаLam, L. K., L. D. Arnold, T. H. Kalantar, J. G. Kelland, P. M. Lane-Bell, M. M. Palcic, M. A. Pickard, and J. C. Vederas. "Analogs of diaminopimelic acid as inhibitors of meso-diaminopimelate dehydrogenase and LL-diaminopimelate epimerase." Journal of Biological Chemistry 263, no. 24 (August 1988): 11814–19. http://dx.doi.org/10.1016/s0021-9258(18)37858-x.
Повний текст джерелаStenta, Marco, Matteo Calvaresi, Piero Altoè, Domenico Spinelli, Marco Garavelli, Roberta Galeazzi, and Andrea Bottoni. "Catalytic Mechanism of Diaminopimelate Epimerase: A QM/MM Investigation." Journal of Chemical Theory and Computation 5, no. 7 (May 27, 2009): 1915–30. http://dx.doi.org/10.1021/ct900004x.
Повний текст джерелаHor, Lilian, Renwick C. J. Dobson, Matthew T. Downton, John Wagner, Craig A. Hutton, and Matthew A. Perugini. "Dimerization of Bacterial Diaminopimelate Epimerase Is Essential for Catalysis." Journal of Biological Chemistry 288, no. 13 (February 19, 2013): 9238–48. http://dx.doi.org/10.1074/jbc.m113.450148.
Повний текст джерелаBARTLETT, A. T. M., and P. J. WHITE. "Species of Bacillus That Make a Vegetative Peptidoglycan Containing Lysine Lack Diaminopimelate Epimerase but Have Diaminopimelate Dehydrogenase." Microbiology 131, no. 9 (September 1, 1985): 2145–52. http://dx.doi.org/10.1099/00221287-131-9-2145.
Повний текст джерелаHor, Lilian, Renwick C. J. Dobson, Con Dogovski, Craig A. Hutton, and Matthew A. Perugini. "Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase fromEscherichia coli." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 1 (December 25, 2009): 37–40. http://dx.doi.org/10.1107/s1744309109047708.
Повний текст джерелаPillai, B., M. M. Cherney, C. M. Diaper, A. Sutherland, J. S. Blanchard, J. C. Vederas, and M. N. G. James. "Structural insights into stereochemical inversion by diaminopimelate epimerase: An antibacterial drug target." Proceedings of the National Academy of Sciences 103, no. 23 (May 24, 2006): 8668–73. http://dx.doi.org/10.1073/pnas.0602537103.
Повний текст джерелаVederas, John C. "2005 Alfred Bader Award Lecture Diaminopimelate and lysine biosynthesis - An antimicrobial target in bacteria." Canadian Journal of Chemistry 84, no. 10 (October 1, 2006): 1197–207. http://dx.doi.org/10.1139/v06-072.
Повний текст джерелаPark, Jeong Soon, Woo Cheol Lee, Jung Hyun Song, Seung Il Kim, Je Chul Lee, Chaejoon Cheong, and Hye-Yeon Kim. "Purification, crystallization and preliminary X-ray crystallographic analysis of diaminopimelate epimerase fromAcinetobacter baumannii." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 1 (December 20, 2012): 42–44. http://dx.doi.org/10.1107/s1744309112048506.
Повний текст джерелаKoo, Carolyn W., Andrew Sutherland, John C. Vederas, and John S. Blanchard. "Identification of Active Site Cysteine Residues that Function as General Bases: Diaminopimelate Epimerase." Journal of the American Chemical Society 122, no. 25 (June 2000): 6122–23. http://dx.doi.org/10.1021/ja001193t.
Повний текст джерелаPillai, Bindu, Maia Cherney, Christopher M. Diaper, Andrew Sutherland, John S. Blanchard, John C. Vederas, and Michael N. G. James. "Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase." Biochemical and Biophysical Research Communications 363, no. 3 (November 2007): 547–53. http://dx.doi.org/10.1016/j.bbrc.2007.09.012.
Повний текст джерелаBrunetti, L., R. Galeazzi, M. Orena, and A. Bottoni. "Catalytic mechanism of l,l-diaminopimelic acid with diaminopimelate epimerase by molecular docking simulations." Journal of Molecular Graphics and Modelling 26, no. 7 (April 2008): 1082–90. http://dx.doi.org/10.1016/j.jmgm.2007.09.005.
Повний текст джерелаGrassick, Alice, Gerlind Sulzenbacher, Véronique Roig-Zamboni, Valérie Campanacci, Christian Cambillau, and Yves Bourne. "Crystal structure of E. coli yddE protein reveals a striking homology with diaminopimelate epimerase." Proteins: Structure, Function, and Bioinformatics 55, no. 3 (April 1, 2004): 764–67. http://dx.doi.org/10.1002/prot.20025.
Повний текст джерелаHIGGINS, William, Chantal TARDIF, Catherine RICHAUD, Michele A. KRIVANEK, and Alan CARDIN. "Expression of recombinant diaminopimelate epimerase in Escherichia coli. Isolation and inhibition with an irreversible inhibitor." European Journal of Biochemistry 186, no. 1-2 (December 1989): 137–43. http://dx.doi.org/10.1111/j.1432-1033.1989.tb15187.x.
Повний текст джерелаRichaud, C., W. Higgins, D. Mengin-Lecreulx, and P. Stragier. "Molecular cloning, characterization, and chromosomal localization of dapF, the Escherichia coli gene for diaminopimelate epimerase." Journal of Bacteriology 169, no. 4 (1987): 1454–59. http://dx.doi.org/10.1128/jb.169.4.1454-1459.1987.
Повний текст джерелаWeir, A. N. C., C. Bucke, G. Holt, M. D. Lilly, and A. T. Bull. "A high-performance liquid chromatography method for the simultaneous assay of diaminopimelate epimerase and decarboxylase." Analytical Biochemistry 180, no. 2 (August 1989): 298–302. http://dx.doi.org/10.1016/0003-2697(89)90434-x.
Повний текст джерелаMengin-Lecreulx, D., C. Michaud, C. Richaud, D. Blanot, and J. van Heijenoort. "Incorporation of LL-diaminopimelic acid into peptidoglycan of Escherichia coli mutants lacking diaminopimelate epimerase encoded by dapF." Journal of Bacteriology 170, no. 5 (1988): 2031–39. http://dx.doi.org/10.1128/jb.170.5.2031-2039.1988.
Повний текст джерелаGelb, Michael H., Yukang Lin, Michael A. Pickard, Yonghong Song, and John C. Vederas. "Synthesis of 3-fluorodiaminopimelic acid isomers as inhibitors of diaminopimelate epimerase: stereocontrolled enzymatic elimination of hydrogen fluoride." Journal of the American Chemical Society 112, no. 12 (June 1990): 4932–42. http://dx.doi.org/10.1021/ja00168a045.
Повний текст джерелаPillai, Bindu, Vijayalakshmi A. Moorthie, Marco J. van Belkum, Sandra L. Marcus, Maia M. Cherney, Christopher M. Diaper, John C. Vederas, and Michael N. G. James. "Crystal Structure of Diaminopimelate Epimerase from Arabidopsis thaliana, an Amino Acid Racemase Critical for l-Lysine Biosynthesis." Journal of Molecular Biology 385, no. 2 (January 2009): 580–94. http://dx.doi.org/10.1016/j.jmb.2008.10.072.
Повний текст джерелаKumagai, Takanori, Yusuke Koyama, Kosuke Oda, Masafumi Noda, Yasuyuki Matoba, and Masanori Sugiyama. "Molecular Cloning and Heterologous Expression of a Biosynthetic Gene Cluster for the Antitubercular Agent d-Cycloserine Produced by Streptomyces lavendulae." Antimicrobial Agents and Chemotherapy 54, no. 3 (January 19, 2010): 1132–39. http://dx.doi.org/10.1128/aac.01226-09.
Повний текст джерелаUda, Narutoshi, Yasuyuki Matoba, Takanori Kumagai, Kosuke Oda, Masafumi Noda, and Masanori Sugiyama. "Establishment of anIn Vitrod-Cycloserine-Synthesizing System by UsingO-Ureido-l-Serine Synthase and d-Cycloserine Synthetase Found in the Biosynthetic Pathway." Antimicrobial Agents and Chemotherapy 57, no. 6 (March 25, 2013): 2603–12. http://dx.doi.org/10.1128/aac.02291-12.
Повний текст джерелаWilliams, Robert M., Glenn J. Fegley, Reneé Gallegos, Felicity Schaefer, and David L. Pruess. "Asymmetric Syntheses of (2S,3S,6S)-, (2S,3S,6R)-, and (2R,3R,6S)-2,3-Methano-2,6-diaminopimelic Acids. Studies Directed to the Design of Novel Substrate-based Inhibitors of L,L-Diaminopimelate Epimerase." Tetrahedron 52, no. 4 (January 1996): 1149–64. http://dx.doi.org/10.1016/0040-4020(95)00976-0.
Повний текст джерелаWILLIAMS, R. M., G. J. FEGLEY, R. GALLEGOS, F. SCHAEFER, and D. L. PRUESS. "ChemInform Abstract: Asymmetric Syntheses of (2S,3S,6S)-(X), (2S,3S,6R)-, and (2R,3R,6S)-2, 3-Methano-2,6-diaminopimelic Acids. Studies Directed to the Design of Novel Substrate-Based Inhibitors of L,L-Diaminopimelate (DAP) Epimerase." ChemInform 27, no. 19 (August 5, 2010): no. http://dx.doi.org/10.1002/chin.199619230.
Повний текст джерелаLiechti, George, Raghuveer Singh, Patricia L. Rossi, Miranda D. Gray, Nancy E. Adams, and Anthony T. Maurelli. "Chlamydia trachomatis dapFEncodes a Bifunctional Enzyme Capable of Both D-Glutamate Racemase and Diaminopimelate Epimerase Activities." mBio 9, no. 2 (April 3, 2018). http://dx.doi.org/10.1128/mbio.00204-18.
Повний текст джерелаYamanaka, Kazuya, Ryo Ozaki, Yoshimitsu Hamano, and Tadao Oikawa. "Molecular and Mechanistic Characterization of PddB, the First PLP-Independent 2,4-Diaminobutyric Acid Racemase Discovered in an Actinobacterial D-Amino Acid Homopolymer Biosynthesis." Frontiers in Microbiology 12 (June 10, 2021). http://dx.doi.org/10.3389/fmicb.2021.686023.
Повний текст джерелаChaudhary, Jyoti, Nagendra Singh, Vijay Kumar Srivastava, Anupam Jyoti, and Sanket Kaushik. "Exploring the significance of diaminopimelate epimerase as a drug target in multidrug resistant Enterococcus faecalis." Vegetos, September 30, 2022. http://dx.doi.org/10.1007/s42535-022-00485-1.
Повний текст джерелаSingh, Harpreet, Satyajeet Das, Jyoti Yadav, Vijay Kumar Srivastava, Anupam Jyoti, and Sanket Kaushik. "In silico prediction, molecular docking and binding studies of acetaminophen and dexamethasone to Enterococcus faecalis diaminopimelate epimerase." Journal of Molecular Recognition 34, no. 9 (March 14, 2021). http://dx.doi.org/10.1002/jmr.2894.
Повний текст джерелаSagong, Hye-Young, and Kyung-Jin Kim. "Structural basis for redox sensitivity in Corynebacterium glutamicum diaminopimelate epimerase: an enzyme involved in l-lysine biosynthesis." Scientific Reports 7, no. 1 (February 8, 2017). http://dx.doi.org/10.1038/srep42318.
Повний текст джерелаGELB, M. H., Y. LIN, M. A. PICKARD, Y. SONG, and J. C. VEDERAS. "ChemInform Abstract: Synthesis of 3-Fluorodiaminopimelic Acid Isomers as Inhibitors of Diaminopimelate Epimerase: Stereocontrolled Enzymatic Elimination of Hydrogen Fluoride." ChemInform 21, no. 40 (October 2, 1990). http://dx.doi.org/10.1002/chin.199040305.
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