Article Abstract:
An Escherichia coli rmlC mutant was developed and a crude enzyme extract prepared from it failed to produce dTDP-4-keto-rhamnose. This is in contrast to a crude enzyme extract prepared from a wild-type E. coli strain where small quantities of this intermediate were observed after incubation with dTDP-glucose in the absence of NADPH. These findings indicate that dTDP-4-keto-rhamnose, the product of RmlC, exists as a free intermediate. Mycobacterium tuberculosis rmlC gene was expressed and incubation of the purified M. tuberculosis RmlC enzyme with dTDP-4-keto-6-deoxyglucose caused the conversion of dTDP-4-keto-6-deoxyglucose to dTDP-4-keto-rhamnose.
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Article Abstract:
A direct screening protocol was employed in the identification of the autolysis gene from the Listeria monocytogenes strain EGD expression library. The amino terminal sequence of the autolysin bears significant homology to the amydase region of the Staphylococcus aureus autolysin while the carboxy terminal sequence contains domains believed to bind to the cell-wall. Site-specific insertional inactivation reveals that this autolysin is responsible for 66% of enzymatic degradation of L. monocytogenes wall substrates.
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Article Abstract:
Various approaches were utilized to study the role of teichoic acids (TA) as bacteriophage receptors among selected Listeria strains. Specific receptor structures of host cells belonging to different serovars were also determined and characterized. Findings confirmed the need for TA in general and of rhamnose and glucosamine in particular for adsorption of Listeria phage A118, which is a temperate Siphovirus, attacking predominantly serovars 1/2.
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