Sandbox Reserved 1508: Difference between revisions
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The Tuberculosis begins with a dormant phase in which Mycobacterium tuberculosis is surviving within granulomas in the lungs of infected individuals where the environment is characterized by oxidative stress (characterized among other things by the reduction of peroxides). This one leads to the formation of nitrogen monoxide which are used by phagocytic cells to kill internalized bacteria. The first targets of reactive nitrogen intermediates (which comes from the transformation of nitrogen monoxide) are cysteine and tyrosine side chains. | The Tuberculosis begins with a dormant phase in which Mycobacterium tuberculosis is surviving within granulomas in the lungs of infected individuals where the environment is characterized by oxidative stress (characterized among other things by the reduction of peroxides). This one leads to the formation of nitrogen monoxide which are used by phagocytic cells to kill internalized bacteria. The first targets of reactive nitrogen intermediates (which comes from the transformation of nitrogen monoxide) are cysteine and tyrosine side chains. | ||
The cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-Phosphoserine Sulfhydrylase (Ägren et al, 2008). The metabolic | The cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-Phosphoserine Sulfhydrylase (Ägren et al, 2008). The metabolic pathways of biosynthesis of cysteine are important for the synthesis of de novo proteins and for reduced thiol as a component of the oxidative defense mechanisms. That occurs in the dormant state of Mycobacterium tuberculosis. | ||
The cysteine synthase CysM is a O-phosphoserine-specific cysteine synthase which belongs to the fold type II pyridoxal 5’-phosphate-dependant enzymes (Ägren et al, 2008). The side chain of Arg220 interacts with the phosphate group by an hydrogen bound allowing the O-phosphoserine bound to the enzyme. | The cysteine synthase CysM is a O-phosphoserine-specific cysteine synthase which belongs to the fold type II pyridoxal 5’-phosphate-dependant enzymes (Ägren et al, 2008). The side chain of Arg220 interacts with the phosphate group by an hydrogen bound allowing the O-phosphoserine bound to the enzyme. | ||
