Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway.

@article{French2010BiochemicalAS,
  title={Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway.},
  author={J. French and S. Ealick},
  journal={Biochemistry},
  year={2010},
  volume={49 29},
  pages={
          5975-7
        }
}
Many plants, fungi, and bacteria catabolize allantoin as a mechanism for nitrogen assimilation. Recent reports have shown that in plants and some bacteria the product of hydrolysis of allantoin by allantoinase is the unstable intermediate ureidoglycine. While this molecule can spontaneously decay, genetic analysis of some bacterial genomes indicates that an aminotransferase may be present in the pathway. Here we present evidence that Klebsiella pneumoniae HpxJ is an aminotransferase that… Expand
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References

SHOWING 1-10 OF 13 REFERENCES
Ureide catabolism in Arabidopsis thaliana and Escherichia coli.
Pyrimidine and purine biosynthesis and degradation in plants.
Allantoate hydrolysis by allantoate amidohydrolase.
...
1
2
...