N-carbamoyl-P-alanine amidohydrolase

Figure 7.2 Reaction scheme for production (a) a-D-amino acids from 5-monosubstituted hydantoins and (b) p-amino acids from 5-dihydrouracils. HYD, hydantoinase/dihydropyrimi-dinase a-DCAR, D-N-a-carbamoylase NCpAA, N-carbamoyl-p-alanine amidohydrolase.

J., Tessaro, D., Servi, S., Clemente-Jimenez, J.M., Rodriguez-Vico, F., and Las Heras-Vazquez, F.J. (2009) Potential application of N-Carbamoyl-P-Alanine amidohydrolase from Agrobacterium tumefaciens C58 for P-Amino acid production. Appl. Environ. Microbiol, 75 (2), 514-520. 

S., and Las Heras-Vazquez, F.J. (2011) N-carbamoyl-P-alanine amidohydrolase from Agrobacterium tumefaciens C58 a promiscuous enzyme for the production of amino acids. J. Chromatogr. B Anal. Technd. Biomed. Life Sci., 879 (29), 3277-3282. 

Natural cyclic amides such as 5,6-dihydrouracil, uracil and 5,6-dihydrothymine as well as hydantoin, 5-methylhydantoin and 5-hydroxymethylhydantoin are effective inducers for enzyme biosynthesis (for a more detailed review on induction experiments see reference13 ). In some cases, the dihydropyrimidinase (D-hydantoinase) is associated with an N-carbamoyl-D-amino acid amidohydrolase (D-carbamoylase) and a hydantoin racemase1301. The previously proposed identity of the D-N-carbamoylase with the p-ureidopropionase (E. C. 3.5.1.6), which was assumed to be responsible for the hydrolysis of N-carbamoyl-P-alanine (see Fig. 12.4-7) 131-351 is no longer valid since the investigations of Ogawa et al. on different aerobic bacteria showed that the... 

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