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-acetyl spinoff. This result's in line with the development or collapse from the tetrahedral intermediate as the speed limiting move in the catalytic system of NagA.
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m is 1/400 of that measured for the wild variety enzyme. These success confirm the great importance with the position of H251 inside the binding of substrate in the active web site of NagA. The homologous residue was identified to communicate with d-glucosamine-six-phosphate while in the structure of NagA from B. subtilis
m though the Zn enzyme has the bottom. Identical trends from the array of the catalytic constants had been noted previously for that Co, Zn, Mn and Fe reconstitutions of apo-NagA from E. coli
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Web page certain mutants of NagA were made so as to verify the roles of particular residues in substrate recognition and catalytic operate. The metal content along with the kinetic parameters to the mutants of NagA constructed for this investigation are introduced in Desk four.
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