One-Pot Biocatalytic Synthesis of Substituted d -Tryptophans from Indoles Enabled by an Engineered Aminotransferase
d-Tryptophan and its derivatives are important precursors of a wide range of indole-containing pharmaceuticals and natural products. Here, we developed a one-pot biocatalytic process enabling the synthesis of d-tryptophans from indoles in good yields and high enantiomeric excess (91% to >99%). Our method couples the synthesis of l-tryptophans catalyzed by Salmonella enterica tryptophan synthase with a stereoinversion cascade mediated by Proteus myxofaciens l-amino acid deaminase and an aminotransferase variant that we engineered to display native-like activity toward d-tryptophan. Our process is applicable to preparative-scale synthesis of a broad range of d-tryptophan derivatives containing electron-donating or -withdrawing substituents at all benzene-ring positions on the indole group.
Parmeggiani, Fabio,Rué Casamajo, Arnau,Walton, Curtis J. W.,Galman, James L.,Turner, Nicholas J.,Chica, Roberto A.
p. 3482 - 3486
(2019/04/13)
The facile synthesis of a series of tryptophan derivatives
This study reports a facile method for the synthesis of a variety of 5- and 6-substituted tryptophan derivatives that are difficult to prepare using alternative enzymatic approaches. Acylation of an activated amino acid, derived from serine in situ, is coupled with an enzymatic resolution step to furnish enantiopure analogues bearing a range of electron withdrawing and releasing substituents. Isolation of a dehydroalanine derivative as a by-product from some reactions provides some insights into the likely mechanism of the reaction.
Blaser, Georg,Sanderson, John M.,Batsanov, Andrei S.,Howard, Judith A.K.
p. 2795 - 2798
(2008/09/19)
Concise synthesis of optically active ring-A substituted tryptophans
A concise synthesis of optically active tryptophan derivatives was developed via diastereoselective alkylation of the Schollkopf chiral auxiliary 4 to provide alkyne 2 which underwent palladium-catalyzed heteroannulation with iodoanilines 1 to furnish protected tryptophans 3. Hydrolysis and subsequent saponification of 3 provided the desired tryptophans 12 in good yields.
Ma, Chunrong,Liu, Xiaoxiang,Yu, Shu,Zhao, Shuo,Cook, James M.
p. 657 - 660
(2007/10/03)
Process for preparing optically active tryptophans
Biochemical optical resolution of DL-tryptophans in which DL-tryptophan amides are interacted with the culture products, or their treated products, of a microorganism capable of producing amidase is described. L-Tryptophan amides in racemic DL-tryptophan amides are asymmetrically hydrolyzed to form optically active L-tryptophans at a high yield and almost all D-tryptophan amides remain without being subjected to hydrolysis. The resultant D-tryptophan amides are readily hydrolyzed, after separating L-tryptophans, to form optically active D-tryptophans at a high yield.
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(2008/06/13)
Process for preparing optically active tryptophanes
Biochemical optical resolution of DL-tryptophanes in which DL-tryptophane amides are interacted with the culture products, or their treated products, of a microorganism capable of producing amidase is described. L-tryptophane amides in racemic DL-tryptophane amides are asymmetrically hydrolyzed to form optically active L-tryptophanes at a high yield and almost all D-tryptophane amides remain without being subjected to hydrolysis. The resultant D-tryptophane amides are readily hydrolyzed, after separating L-tryptophanes, to form optically active D-tryptophanes at a high yield.
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(2008/06/13)
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