207910-78-9Relevant articles and documents
A novel synthetic protocol for the synthesis of pulvinones, and naturally occurring Aspulvinone E, molecules of medicinal interest
Igglessi-Markopoulou, Olga,Katsamakas, Sotirios,Markopoulos, John,Prousis, Kyriakos C.
supporting information, (2021/11/22)
A novel two step methodology for readily accessible natural “pulvinone” derivatives in excellent yields has been developed starting from activated precursors, bearing a functionalized 1,3-dioxolane-2,4-diones (OCA’s), as dually protected-activated synthon
Single-Biocatalyst Synthesis of Enantiopure d-Arylalanines Exploiting an Engineered d-Amino Acid Dehydrogenase
Parmeggiani, Fabio,Ahmed, Syed T.,Thompson, Matthew P.,Weise, Nicholas J.,Galman, James L.,Gahloth, Deepankar,Dunstan, Mark S.,Leys, David,Turner, Nicholas J.
, p. 3298 - 3306 (2016/10/20)
A practical and efficient biocatalytic synthesis of aromatic d-amino acids has been developed, based on the reductive amination of the corresponding α-keto acids via a recombinant whole cell system composed of an engineered dehydrogenase and cofactor recycling apparatus. The reaction was shown to give excellent enantioselectivity (≥98%) and good yields at the preparative scale across a broad range of substrates. Additionally, the structure of the variant enzyme was solved to allow rationalisation of the observed reaction rates. The engineered whole cell catalyst was also used to mediate the production of d-phenylalanine derivatives from racemic mixtures and cheaper l-amino acids by combining it with an enantiocomplementary deaminase. (Figure presented.).
Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis
Busca, Patricia,Paradisi, Francesca,Moynihan, Eamonn,Maguire, Anita R.,Engel, Paul C.
, p. 2684 - 2691 (2007/10/03)
The substrate scope of three mutants of phenylalanine dehydrogenase as biocatalysts for the transformation of a series of 2-oxo acids, structurally related to phenylpyruvic acid, to the analogous -amino acids, non-natural analogues of phenylalanine, has been investigated. The mutant enzymes are more tolerant than the wild type enzyme of the non-natural substrates, especially those with substituents at the 4-position on the phenyl ring. Excellent enantiocontrol resulted in all cases.
