Murein-metabolizing enzymes from Escherichia Coli: the lytic transglycosylases. Entering the protein engineering cycle and biotechnological application.

This thesis reports on two murein-metabolizing enzymes from Escherichia coli. The two lytic transglycosylases catalyze the cleavage of the B-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in the murein-polymer, yielding muropeptides with a 1,6-anhydro-muramic acid residue.
Studies on bacterial transglycosylases are of interest for at least three reasons. In the first place, such studies contribute to a better understanding of the metabolism of murein. In the second place, these enzymes can be used for the production of pharmacologically active compounds by specific degradation of murein in vitro. In the third place, a 3D-structure might lead to the design of selective inhibitors and thus to the development of a new class of antibiotics. ...

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Summary

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