Structure-function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria.

@article{Sakamoto2004StructurefunctionRO,
  title={Structure-function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria.},
  author={Hirokazu Sakamoto and St{\'e}phanie Landais and C{\'e}cile Evrin and Christine Laurent-Winter and Octavian B{\^a}rzu and Rod A. Kelln},
  journal={Microbiology},
  year={2004},
  volume={150 Pt 7},
  pages={
          2153-9
        }
}
Bacterial uridine monophosphate (UMP) kinases are essential enzymes encoded by pyrH genes, and conditional-lethal or other pyrH mutants were analysed with respect to structure-function relationships. A set of thermosensitive pyrH mutants from Escherichia coli was generated and studied, along with already described pyrH mutants from Salmonella enterica serovar Typhimurium. It is shown that Arg-11 and Gly-232 are key residues for thermodynamic stability of the enzyme, and that Asp-201 is… CONTINUE READING

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