Streptococcus faecalis inhibitors

Microbial cells maintain low internal [Ca2+] levels through the operation of several types of highly active and specific efflux processes.180,184 Efflux of Ca2+ can only be studied with difficulty in whole cells, partly because of complications resulting from the binding of Ca2+ to the cell walls. Nevertheless, the presence of active mechanisms for the efflux of calcium are shown by the fact that extreme temperatures or inhibitors result in increased levels of intracellular calcium. Efflux of Ca2+ has been demonstrated for B. megaterium, while ATP-linked efflux of Ca2+ has been demonstrated for Streptococcus faecalis.lss... 

The last step in the fatty acid biosynthetic pathway is catalyzed by enoyl-acyl carrier protein (ACP) reductase, which is responsible for reduction of the double bond in the enoyl-ACP derivative (Heath and Rock, 1995 Payne et al., 2002). While fabl genes encode enoyl-ACP reductases (FabI enzymes) in S. aureus and E. coli, an alternative enoyl-ACP reductase, FabK, replaces the function of Fabl in a number of bacterial species such as Streptococcus pneumoniae (Heath and Rock, 2000). More interestingly, a number of bacterial species (such as Enterococcus faecalis and Pseudomonas aeruginosa) possess both the Fabl and FabK enzymes (Heath and Rock, 2000). To discover Fabl-specific antibacterial inhibitors, Payne and colleagues at GlaxoSmithKline (GSK) developed assays for various versions of enoyl-ACP reductases (Payne et al., 2002 Seefeld et al., 2003) based on the following reaction scheme ... 

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