Allantoate hydrolysis by allantoate amidohydrolase.

@article{Drift1970AllantoateHB,
  title={Allantoate hydrolysis by allantoate amidohydrolase.},
  author={C. van der Drift and F. D. de Windt and G. Vogels},
  journal={Archives of biochemistry and biophysics},
  year={1970},
  volume={136 1},
  pages={
          273-9
        }
}
Abstract The degradation of allantoate by allantoate amidohydrolase from Streptococcus allantoicus resulted in the production of 1 mole of carbon dioxide, 2 moles of NH 3 , and probably 1 mole of (−)-ureidoglycolate per mole of allantoate. Ureidoglycine was an intermediate and presumably also a substrate for allantoate amidohydrolase. A nonenzymic transamination reaction of ureidoglycine and glyoxylate resulted in the formation of glycine and oxalurate. The enzymic and nonenzymic reactions… Expand
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