%0 Journal Article %1 ISI:000172620200005 %A Altenbuchner, J %A Siemann-Herzberg, M %A Syldatk, C %C 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND %D 2001 %I CURRENT BIOLOGY LTD %J CURRENT OPINION IN BIOTECHNOLOGY %K imported myown %N 6 %P 559-563 %R 10.1016/S0958-1669(01)00263-4 %T Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids %U https://doi.org/10.1016/S0958-1669(01)00263-4 %V 12 %X 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.

@article{ISI:000172620200005, 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.}}, added-at = {2018-01-25T13:38:08.000+0100}, address = {{84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND}}, affiliation = {{Altenbuchner, J (Reprint Author), Univ Stuttgart, Inst Ind Genet, Allmandring 31, D-70569 Stuttgart, Germany. Univ Stuttgart, Inst Ind Genet, D-70569 Stuttgart, Germany. Univ Stuttgart, Inst Biochem Engn, D-70569 Stuttgart, Germany.}}, author = {Altenbuchner, J and Siemann-Herzberg, M and Syldatk, C}, biburl = {https://puma.ub.uni-stuttgart.de/bibtex/2a40352a42459edf262c7c4b9d4199e1a/siemannherzberg}, da = {{2018-01-25}}, doc-delivery-number = {{500HD}}, doi = {{10.1016/S0958-1669(01)00263-4}}, interhash = {01edae025e755785145c189a4bf622b2}, intrahash = {a40352a42459edf262c7c4b9d4199e1a}, issn = {{0958-1669}}, journal = {{CURRENT OPINION IN BIOTECHNOLOGY}}, journal-iso = {{Curr. Opin. Biotechnol.}}, keywords = {imported myown}, keywords-plus = {{ARTHROBACTER-AURESCENS DSM-3745; X-RAY ANALYSIS; DIRECTED EVOLUTION; ESCHERICHIA-COLI; N-CARBAMOYLASE; FUSION ENZYME; PURIFICATION; CRYSTALLIZATION; EXPRESSION}}, language = {{English}}, month = {{DEC}}, number = {{6}}, number-of-cited-references = {{24}}, pages = {{559-563}}, publisher = {{CURRENT BIOLOGY LTD}}, research-areas = {{Biochemistry \& Molecular Biology; Biotechnology \& Applied Microbiology}}, times-cited = {{94}}, timestamp = {2018-01-25T12:38:18.000+0100}, title = {{Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids}}, type = {{Review}}, unique-id = {{ISI:000172620200005}}, url = {https://doi.org/10.1016/S0958-1669(01)00263-4}, usage-count-last-180-days = {{2}}, usage-count-since-2013 = {{19}}, volume = {{12}}, web-of-science-categories = {{Biochemical Research Methods; Biotechnology \& Applied Microbiology}}, year = {{2001}} }