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Cover Illustration: GlmU is an essential, bifunctional enzyme that catalyzes production of UDP-N-acetylglucosamine (UDPGlcNAc), which is involved in the peptidoglycan and lipopolysaccharide biosynthetic pathways in bacteria. Shown here is a ribbon representation of a monomeric unit of Haemophilus influenzae GlmU with UDP-GlcNAc bound at the uridyltransferase active site. The structural and biochemical characterization of GlmU suggests that GlmU activity follows a sequential substrate-binding order primarily through an associative mechanism with a pentavalent phosphate intermediate and an inversion of stereochemistry. For details, see Mochalkin et al. (this issue). This refined catalytic mechanism provides a basis for the structure-guided design of novel antibacterial agents targeting GlmU activity. (See Mochalkin et al., pp. 2657–2666).