Title : Properties of D-hydantoinase from Agrobacterium tumefaciens and its use for the preparation of N-carbamyl D-amino acids.

Pub. Date : 1995 Nov 22

PMID : 7488185






6 Functional Relationships(s)
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1 Properties of D-hydantoinase from Agrobacterium tumefaciens and its use for the preparation of N-carbamyl D-amino acids. n-carbamyl d-amino acids AWN88_RS03840 Agrobacterium tumefaciens
2 Agrobacterium tumefaciens strain 47C expresses an inducible D-hydantoinase that catalyzes the formation of optically pure N-carbamyl D-amino acids from racemic hydantoin precursors. n-carbamyl d-amino acids AWN88_RS03840 Agrobacterium tumefaciens
3 The D-Hydantoinase was shown to be active and stable at elevated temperatures and pH values, thus affording favorable bioreaction conditions that result in the racemization of DL-hydantoins to the utilizable D-isomer. dl-hydantoins AWN88_RS03840 Agrobacterium tumefaciens
4 A. tumefacins hydantoinase was most active on 5,6-dihydrouracil and DL-5-methylhydantoin with only slight activity on DL-benzylhydantoin. dihydrouracil AWN88_RS03840 Agrobacterium tumefaciens
5 A. tumefacins hydantoinase was most active on 5,6-dihydrouracil and DL-5-methylhydantoin with only slight activity on DL-benzylhydantoin. 5-methylhydantoin AWN88_RS03840 Agrobacterium tumefaciens
6 A. tumefacins hydantoinase was most active on 5,6-dihydrouracil and DL-5-methylhydantoin with only slight activity on DL-benzylhydantoin. dl-benzylhydantoin AWN88_RS03840 Agrobacterium tumefaciens