443650-31-5Relevant articles and documents
Kinetic Resolution of Unnatural and Rarely Occuring Amino Acids: Enantioselective Hydrolysis of N-Acyl Amino Acids Catalyzed by Acylase I
Chenault, H. Keith,Dahmer, Juergen,Whitesides, George M.
, p. 6354 - 6364 (2007/10/02)
Acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14, from porcine kidney and the fungus Aspergillus) is broadly applicable enzymatic catalyst for the kinetic resolution of unnatural and rarely occuring α-amino acids.Its enantioselectivity for the hydrolysis of N-acyl L-α-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure and functionality.This paper reports the initial rates of enzyme-catalyzed hydrolysis of over 50 N-acyl amino acids and analogues, the stabilities of the enzymes in aqueous and aqueous/organic solutions, and the effects of different acyl groups and metal ions on the rates of enzymatic hydrolysis.Eleven α-amino and α-methyl α-amino acids were resolved on a 2-29-g scale.Crude L- and D-amino acid products had generally >90percent ee.The utility of resolved amino acids as chiral synthons was illustrated by the preparation of (R)- and (S)-1-butene oxide and the diastereoselective (cis:trans, 7-8:1) iodolactonization of three 2-amino-4-alkenoic acid derivatives.
Synthesis of (R)-5-Aminohex-2-enedioic acid and the (+/-)-2-Bromo Derivative as Unsaturated Analogues of the Neurotransmitter Antagonist D-&α-Aminoadipic Acid
Allan, Robin D.
, p. 4658 - 4667 (2007/10/02)
5-Aminohex-2-enedioic acid (2), an unsaturated analogue of the neurotransmitter antagonist D-α-aminoadipic acid, has been synthesised by a convenient route using a phase-transfer alkylation of N-diphenylmethyleneglycine ethyl ester.The unsaturated amino acid has been resolved and the absolute stereochemistry of the (-) isomer determined as R by reduction to D-α-aminoadipic acid.A more conventional synthetic scheme failed to yield (2), but led to the preparation of the (+/-)-2-bromo derivative (4) in low yield.
