Autor: |
Mitsakos V; School of Chemistry, University of Melbourne, Vic. 3010, Australia., Dobson RC, Pearce FG, Devenish SR, Evans GL, Burgess BR, Perugini MA, Gerrard JA, Hutton CA |
Jazyk: |
angličtina |
Zdroj: |
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2008 Jan 15; Vol. 18 (2), pp. 842-4. Date of Electronic Publication: 2007 Nov 13. |
DOI: |
10.1016/j.bmcl.2007.11.026 |
Abstrakt: |
Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis and an important antibiotic target. The specificity of a range of heterocyclic product analogues against DHDPS from three pathogenic species, Bacillus anthracis, Mycobacterium tuberculosis and methicillin-resistant Staphylococcus aureus, and the evolutionarily related N-acetylneuraminate lyase, has been determined. The results suggest that the development of species-specific inhibitors of DHDPS as potential antibacterials is achievable. |
Databáze: |
MEDLINE |
Externí odkaz: |
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