Relevant bibliographies by topics / Diaminopimelate epimerase

Academic literature on the topic 'Diaminopimelate epimerase'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "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.

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Usha, 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.

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Lam, 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.

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Stenta, 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.

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Hor, 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.

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BARTLETT, 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.

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Hor, 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.

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Pillai, 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.

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9

Vederas, 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.

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The development of bacterial resistance to current antibiotic therapy has stimulated the search for novel antimicrobial agents. The essential peptidoglycan cell wall layer in bacteria is the site of action of many current drugs, such as β-lactams and vancomycin. It is also a target for a number of very potent bacterially produced antibiotic peptides, such as nisin A and lacticin 3147, both of which are highly posttranslationally modified lantibiotics that act by binding to lipid II, the peptidoglycan precursor. Another set of potential targets for antibiotic development are the bacterial enzymes that make precursors for lipid II and peptidoglycan, for example, those in the pathway to diamino pimelic acid (DAP) and its metabolic product, L-lysine. Among these, DAP epimerase is a unique nonpyridoxal phosphate (PLP) dependent enzyme that appears to use two active site thiols (Cys73 and Cys217) as a base and an acid to depro tonate the α-hydrogen of LL-DAP or meso-DAP from one side and reprotonate from the other. This process cannot be easily duplicated in the absence of the enzyme. A primary goal of our work was to generate inhibitors of DAP epi merase that would accurately mimic the natural substrates (meso-DAP and LL-DAP) in the enzyme active site and, through crystallographic analysis, provide insight into mechanism and substrate specificity. A series of aziridine-containing DAP analogs were chemically synthesized and tested as inhibitors of DAP epimerase from Haemophilus influenzae. Two diastereomers of 2-(4-amino-4-carboxybutyl)aziridine-2-carboxylic acid (AziDAP) act as rapid irreversible inactivators of DAP epimerase; the AziDAP analog of LL-DAP reacts selectively with the sulfhydryl of Cys73, whereas the corresponding analog of meso-DAP reacts with Cys217. AziDAP isomers are too unstable to be useful antibiotics. However, mass spectral and X-ray crystallographic analyses of the inactivated enzymes confirm that the thiol attacks the methylene group of the aziridine with concomitant ring opening to give a DAP analog bound in the active site. Further crystallographic analyses should yield useful mechanistic insights.Key words: enzyme mechanism, enzyme inhibition, antibiotics, aziridines, amino acids.
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Park, 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.

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Dissertations / Theses on the topic "Diaminopimelate epimerase"

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QUAGLIAROLI, DANIEL. "Etude d'une enzyme appartenant a la voie de la lysine : la diaminopimelate epimerase d'escherichia coli. antibiotiques analogues de l'acide diaminopimelique: action sur le metabolisme bacterien." Paris 6, 1991. http://www.theses.fr/1991PA066296.

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L'acide meso diaminopimelique, biosynthetise uniquement par les procaryotes et les plantes superieures, est un intermediaire clef dans le metabolisme des bacteries. C'est le precurseur direct de la lysine et un composant essentiel et specifique des parois bacteriennes ou il est implique dans la reticulation du peptidoglycane. Les enzymes intervenant dans la biosynthese et le metabolisme de l'acide diaminopimelique constituent des cibles potentielles pour de nouveaux agents antibacteriens. La conception de tels agents nous a conduit a purifier la diaminopimelate epimerase a partir d'une souche escherichia coli porteuse du gene dapf clone sur un plasmide. Nous avons determine le poids moleculaire de l'enzyme native et de l'enzyme denaturee. L'analyse de la cinetique de renaturation de cette enzyme montre que la reapparition de l'activite enzymatique est gouvernee par une cinetique d'ordre deux, suggerant une forme dimerique (homodimere) pour l'enzyme native. Le schema reactionnel est compose d'une reaction monomoleculaire rapide suivit d'une reaction bimoleculaire plus lente qui est l'etape limitante du processus. L'etude de l'inhibition de la diaminopimelate epimerase par les analogues de l'acide diaminopimelique nous a permis de montrer que l'ensemble des modifications effectuees sur l'acide 4-methylene-diaminopimelique n'a pas pour effet d'ameliorer son activite. Malgre des proprietes antibiotiques interessantes ces composes ne sont que de modestes inhibiteurs de la diaminopimelate epimerase. Certains de ces analogues peuvent en outre assurer la croissance d'un mutant auxotrophe en acide diaminopimelique. Cette propriete a ete mise a profit pour concevoir de nouvelles molecules pouvant s'incorporer dans un precurseur du peptidoglycane, a la place du meso-diaminopimelate, mais ne permettant plus aux etapes ulterieures de se produire. L'action de ces composes sur l'incorporation de l'acide meso-diaminopimelique dans la mureine a ete etudiee sur des bacteries permeabilisees. L'etude de l'inhibition du transport du meso-diaminopimelate par ces analogues a montre qu'ils presentaient des affinites differentes pour le systeme general de la cystine. Le meilleur inhibiteur est l'acide 4-methylene-diaminopimelique, qui est aussi le compose presentant la meilleure activite antibiotique. Les resultats obtenus revelent que tous les composes antibiotiques sont des inhibiteurs de la diaminopimelate epimerase et de l'incorporation de l'acide meso-diaminopimelique dans le peptidoglycane
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Conference papers on the topic "Diaminopimelate epimerase"

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Stenta, Marco, Matteo Calvaresi, Piero Altoè, Domenico Spinelli, Marco Garavelli, Andrea Bottoni, Theodore E. Simos, and George Maroulis. "The Catalytic Activity of Diaminopimelate Epimerase: a QM∕MM Study." In COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1. AIP, 2007. http://dx.doi.org/10.1063/1.2836189.

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