This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.
We aim to characterize the three-dimensional structure of Escherichia coli spermidine synthase (SpeE) and to carry out functional studies for this enzyme. SpeE catalyzes the synthesis of spermidine, which is a known polyamine. Polyamines such as putrescine, spermidine and spermine, are polycationic and linear aliphatic compounds present in significant amount in living organisms. They neutralize intracellular polyanions, especially DNA and therefore providing stability for DNA molecules in the cell. They are also known to be important factors of DNA, RNA and protein synthesis. Bacteria growth is stimulated by polyamines. Polyamines accumulation has also been observed in cancerous tissues. Inhibition of polyamine biosynthesis and depletion of intracellular polyamine content has become a potential therapeutic method for the treatment of bacterial infection and cancer. Structure and functional characterization of SpeE is crucial as these studies will facilitate the rational design of such potential drugs that inhibit the enzyme.
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