Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis

Abstract

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 alpha-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.

SnIV Porphyrin Scaffolds for Axially Bonded Multiporphyrin Arrays: Synthesis and Structure Elucidation by NMR Studies

“…General Remarks: Starting arylpyruvic acids 7a – 7c were synthesized according to the literature procedure 10. 3‐Amino‐1,2,4‐triazole ( 1 ) and substituted aldehydes 2 were commercially available.…”

Purification of recombinant phenylalanine dehydrogenase by partitioning in aqueous two-phase systems

“…E-mail address: skandar@pasteur.ac.ir (E. Omidinia). blocks for inclusion in foods [8] and production of pharmaceutical peptides [9][10][11]. This enzyme has also been used in biosensors and diagnostic kits to screen blood serum of neonates for phenylketonuria (PKU) [12,13].…”

Intersecting Xenobiology and Neometabolism To Bring Novel Chemistries to Life

“…However, protein engineering has proven to be an effective strategy to expand the promiscuity of these enzymes to accept different 2-oxoacids as substrates. [145] Based on this potential, Busca and co-workers [146] used three different mutant versions of phenylalanine dehydrogenase from Bacillus sphaericus to synthesize 2-, 3-and 4fluorophenylalanine from the corresponding fluorophenylpyruvate derivatives and NH 3 . Another engineered version of the Figure 5.…”