Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids.
A cascade of hydantoinase, N-carbamoylase and hydantoinracemase can be used for the production of natural and unnatural chiral D- and L-amino acids from chemically synthesized hydantoin derivatives. Potentially, 100% conversion and 100% optically pure amino acids can be obtained at the same time if racemic substrates are used. Recent research activities concentrate on newly isolated or improved enzymes and include directed evolution techniques, structure elucidation, studies of fusion proteins and the use of specially designed whole cell biocatalysts.
Altenbuchner
J
J
Institute of Industrial Genetics, University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
Siemann-Herzberg
M
M
Syldatk
C
C
D000581:Amidohydrolases / Q000737:chemistry*; D000596:Amino Acids / Q000138:chemical synthesis* / Q000737:chemistry*; D001709:Biotechnology / Q000379:methods*; D019878:Carboxyl and Carbamoyl Transferases / Q000737:chemistry; D002384:Catalysis; D019143:Evolution, Molecular; D006827:Hydantoins / Q000378:metabolism; D008956:Models, Chemical; D019998:Racemases and Epimerases / Q000737:chemistry
D000596:Amino Acids; D006827:Hydantoins; D019878:Carboxyl and Carbamoyl Transferases; D000581:Amidohydrolases; C020047:dihydropyrimidinase; D019998:Racemases and Epimerases