Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids.

J Altenbuchner, M Siemann-Herzberg, C Syldatk

Journal: Current opinion in biotechnology 2002;12(6):559-63

PMID: 11849938

Full Text on Elsevier Science View on PubMed

Abstract

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.

Address: Institute of Industrial Genetics, University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.

DOI: 10.1016/s0958-1669(01)00263-4

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MeSH Terms: Amidohydrolases, Amino Acids, Biotechnology, Carboxyl and Carbamoyl Transferases, Catalysis, Evolution, Molecular, Hydantoins, Models, Chemical, Racemases and Epimerases