Sandbox Reserved 772: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 13: Line 13:
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">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</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">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.  This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref>  HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref>   
HDH is encoded by the structural gene ''his''D in Brucellosis, commonly known as Maltafeve.  This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref>  HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref>   


__TOC__
__TOC__