Girish, Tavarekere S and Sharma, Eshita and Gopal, B (2008) Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase. In: FEBS Letters, 582 (19). pp. 2923-2930.
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Lysine biosynthesis is crucial for cell-wall formation in bacteria. Enzymes involved in lysine biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate synthase (DHDPS) catalyzes the first step of this pathway. Unlike its homologues, Staphylococcus aureus DHDPS is a dimer both in solution and in the crystal and is not feedback inhibited by lysine. The crystal structure of S. aureus DHDPS in the free and substrate bound forms provides a structural rationale for its catalytic mechanism. The structure also reveals unique conformational features of the S. aureus enzyme that could be crucial for the design of specific non-competitive inhibitors.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Federation of European Biochemical Societies.|
|Keywords:||Dihidrodipicolinate synthase;Lysine biosynthesis;Feedback inhibition;Ping-pong mechanism.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||31 Oct 2008 04:56|
|Last Modified:||19 Sep 2010 04:51|
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