Girish, Tavarekere S. ; Sharma, Eshita ; Gopal, B. (2008) Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase FEBS Letters, 582 (19). pp. 2923-2930. ISSN 0014-5793
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Official URL: http://www.febsletters.org/article/S0014-5793%2808...
Related URL: http://dx.doi.org/10.1016/j.febslet.2008.07.035
Abstract
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: | Article |
|---|---|
| Source: | Copyright of this article belongs to Federation of European Biochemical Societies. |
| Keywords: | Dihidrodipicolinate Synthase; Lysine Biosynthesis; Feedback Inhibition; Ping-pong Mechanism |
| ID Code: | 98271 |
| Deposited On: | 06 May 2014 12:05 |
| Last Modified: | 06 May 2014 12:05 |
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