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==Histidinol Dehydrogenase== | ==Histidinol Dehydrogenase== | ||
Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> | Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199<http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf></ref> | ||
HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">J. Pascale, M. Abdo, R. Boigegrain, J. Montero, J. Winum, S. Kohler. "Targeting of the Brucella Suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen." American Society for Microbiology (2007): N. pag. Web. 27 Nov. 2013. <http://aac.asm.org/content/51/10/3752.short>.</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> | HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">J. Pascale, M. Abdo, R. Boigegrain, J. Montero, J. Winum, S. Kohler. "Targeting of the Brucella Suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen." American Society for Microbiology (2007): N. pag. Web. 27 Nov. 2013. <http://aac.asm.org/content/51/10/3752.short>.</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> | ||
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The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. | The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. | ||
Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/ | Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">Turtaut, Francois, Safia Ouahrani-Bettache, Jean Montero, Stephan Kohler, and Jean-Yves Winum. "Synthesis and Biological Evaluation of a New Class of Anti-brucella Compounds Targeting Histidinol Dehydrogenase: α-O-arylketones and α-S-arylketones Derived from Histidine." Med. Chem. Commun. 2(2011): 995-1000. Web. 27 Nov. 2013. <http://pubs.rsc.org.prox.lib.ncsu.edu/en/Content/ArticleLanding/2011/MD/c1md00146a#!divCitation>.</ref> | ||
==References== | ==References== | ||
<references /> | <references /> | ||