3di1

Publication Abstract from PubMed

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.

Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase.,Girish TS, Sharma E, Gopal B FEBS Lett. 2008 Aug 20;582(19):2923-30. Epub 2008 Jul 29. PMID:18671976^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.