917247-85-9Relevant articles and documents
Nitrilases, nucleic acids encoding them and methods for making and using them
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Page/Page column 63; 72, (2016/01/09)
The invention relates to nitrilases and to nucleic acids encoding the nitrilases. In addition methods of designing new nitrilases and method of use thereof are also provided. The nitrilases have increased activity and stability at increased pH and temperature.
Biocatalytic racemization of (hetero)aryl-aliphatic α- hydroxycarboxylic acids by Lactobacillus spp. proceeds via an oxidation-reduction sequence
Nestl, Bettina M.,Glueck, Silvia M.,Hall, Melanie,Kroutil, Wolfgang,Stuermer, Rainer,Hauer, Bernhard,Faber, Kurt
, p. 4573 - 4577 (2007/10/03)
The biocatalytic racemization of a range of (hetero)aryl- and (di)aryl-aliphatic α-hydroxycarboxylic acids has been achieved by using whole resting cells of Lactobacillus spp. The essentially mild (physiological) reaction conditions ensure the suppression of undesired side reactions, such as elimination, decomposition or condensation. Cofactor/inhibitor studies using a cell-free extract of Lactobacillus paracasei DSM 20207 reveal that the addition of redox cofactors (NAD+/NADH) leads to a distinct increase in the racemization rate, while strong inhibition is observed in the presence of Thio-NAD+, which suggests that the racemization proceeds by an oxidation-reduction sequence rather than involvement of a "racemase" enzyme. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.
An enzyme library approach to biocatalysis: Development of nitrilases for enantioselective production of carboxylic acid derivatives
DeSantis, Grace,Zhu, Zuolin,Greenberg, William A.,Wong, Kelvin,Chaplin, Jenny,Hanson, Sarah R.,Farwell, Bob,Nicholson, Lawrence W.,Rand, Cynthia L.,Weiner, David P.,Robertson, Dan E.,Burk, Mark J.
, p. 9024 - 9025 (2007/10/03)
The discovery, from Nature, of a large and diverse set of nitrilases is reported. The utility of this nitrilase library for identifying enzymes that catalyze efficient production of valuable hydroxy carboxylic acid derivatives is demonstrated. Unprecedented enantioselectivity and substrate scope are highlighted for three newly discovered and distinct nitrilases. For example, a wide array of (R)-mandelic acid derivatives and analogues were produced with high rates, yields, and enantiomeric excesses (95-99% ee). We also have found nitrilases that provide direct access to (S)-phenyllactic acid and other aryllactic acid derivatives, again with high yields and enantioselectivities. Finally, different nitrilases have been discovered that catalyze enantiotopic hydrolysis of 3-hydroxyglutaronitrile to afford either enantiomer of 4-cyano-3-hydroxybutyric acid with high enantiomeric excesses (>95% ee). The first enzymes are reported that effect this transformation to furnish the (R)-4-cyano-3-hydroxybutyric acid which is a precursor to the blockbuster drug Lipitor. Copyright
