The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity.

@article{Abendroth2002TheSO,
  title={The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity.},
  author={Jan Abendroth and Karsten Niefind and Oliver Hart May and Martin Siemann and Christoph Syldatk and Dietmar Schomburg},
  journal={Biochemistry},
  year={2002},
  volume={41 27},
  pages={8589-97}
}
L-Hydantoinase from Arthrobacter aurescens (L-Hyd) is a member of the dihydropyrimidinases which in turn belong to the cyclic amidases. Dihydropyrimidinases catalyze the reversible hydrolytic ring opening of dihydropyrimidines as the second step in the catabolism of pyrimidines. In biotechnology, their hydroloytic activity on five-membered cyclic diamides (hydantoins) is used in the enantio-specific production of amino acids from racemic hydantoins. L-Hyd differs from most of the other… CONTINUE READING

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