Identification, expression, and characterization of Escherichia coli guanine deaminase.

@article{Maynes2000IdentificationEA,
  title={Identification, expression, and characterization of Escherichia coli guanine deaminase.},
  author={J. Maynes and R. Yuan and F. Snyder},
  journal={Journal of bacteriology},
  year={2000},
  volume={182 16},
  pages={
          4658-60
        }
}
Using the human cDNA sequence corresponding to guanine deaminase, the Escherichia coli genome was scanned using the Basic Local Alignment Search Tool (BLAST), and a corresponding 439-residue open reading frame of unknown function was identified as having 36% identity to the human protein. The putative gene was amplified, subcloned into the pMAL-c2 vector, expressed, purified, and characterized enzymatically. The 50.2-kDa protein catalyzed the conversion of guanine to xanthine, having a K(m) of… Expand
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