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Article: Studies from University of Notre Dame in the area of drug resistance published.
- Article from:
- Biotech Week
- Article date:
- August 12, 2009
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According to recent research from the United States, "The bacterial, enzyme AmpD is an early catalyst in commitment of cell wall metabolites to the recycling events within the cytoplasm. The key internalized metabolite of Cell watt recycling, beta-D-N-acetytgtucosamine-(1 → 4)-1,6-anhydro-beta-N-acetytmuramyl-L-Ala-gamma-D-Glu-meso-DAP-D-Ala-D-Ala (compound 1), is a poor substrate for AmpD."
"Two additional metabolites, 1,6-anhydro-N-acetyimuramyl-peptidyl derivatives 2a and 2c, served as substrates for AmpD with a k(cat)/K-m of >10(4) M-1 s(-1). The enzyme hydrolytically processes the lactyl amide bond of the 1,6-anhydro-N-acetylmuramyl moiety. The ...
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Article: Research results from University of Notre Dame ...
Chemicals & Chemistry;
June 19, 2009 ;
700+ words
... ... American Chemical Society, 2009 ... University of Notre Dame, Dept ... Biochemistry, Notre Dame, IN 46556 ... American Chemical Society is: American Chemical Society, 1155 16th ... States, Notre Dame, Life Sciences ...
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