CHED 510 |
| T4 lysozyme, an enzyme produced by T4 bacteriophage, hydrolyzes the β(1-4) glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) in polysaccharides chains of the bacterial cell wall. The T4 lysozyme also requires that NAM be substituted with a peptide side chain in order for hydrolysis to occur. The only available substrate is actual cell wall, which is heterogeneous, preventing detailed, accurate kinetic analysis. Synthesis of a smaller, well-defined and convenient substrate, and the ability to modify the peptide side chain in that substrate, would allow us to study the kinetics and mechanism of T4 lysozyme. O-nitrophenyl and p-nitrophenyl β-glycosides of N-acetylmuramic acid linked to Ala-D-Glu(Lys) peptides were synthesized and purified by HPLC and characterized by NMR. Synthesis of the substrates and activity, analyzed by UV/Vis spectroscopy, of the T4 lysozyme will be discussed. |
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Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |