New biocatalytic route for the production of enantioenriched -alanine derivatives starting from 5- and 6-monosubstituted dihydrouracils
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Martínez Gómez, Ana Isabel; Clemente Jiménez, Josefa María; Rodríguez Vico, Felipe; Kanerva, LT; Xian-Guo, L; [et al.]Fecha
2012Resumen
Taking advantage of the catalytic promiscuity of pyrimidine-catabolism enzymes (dihydropyrimidinase (E.C. 3.5.2.2), N-carbamoyl- -alanine amidohydrolase (E.C. 3.5.1.6)), the production of different -alanine derivatives starting from 5- and 6-monosubstituted dihydrouracils has been evaluated using a mimesis approach. In this work, the S-enantioselective character of dihydropyrimidinase
from Sinorizhobium meliloti toward 6-monosubstituted dihydrouracil derivatives has been shown. An inverted R-/S-enantioselectivity of N-carbamoyl- -alanine amidohydrolase from Agrobacterium tumefaciens toward two different N-carbamoyl- -amino acids has been proved. Our results have shown for the first time that this mimetic tandem constitutes an interesting biotechnological tool for the preparation of different -alanine derivatives in an environmentally friendly way, allowing the production of enantioenriched (R)- -phenyl- -alanine (e.e. > 95%) and (R)- -methyl- -alanine (e.e. > 90%).
Palabra/s clave
Hydantoinase
Dihydropyrimidinase
Carbamoylase
Ureidopropionase
-Amino acid
Biocatalysis
Kinetic resolution
Enzymatic preparation