A Multi-Enzymatic Cascade Reaction for the Stereoselective Production of γ-Oxyfunctionalyzed Amino Acids

Junichi Enoki, Jaqueline Meisborn, Ann-Christin Müller, Robert Kourist

Research output: Contribution to journalArticleResearchpeer-review

Abstract

A stereoselective three-enzyme cascade for synthesis of diasteromerically pure γ-oxyfunctionalized α-amino acids was developed. By coupling a dynamic kinetic resolution (DKR) using an N-acylamino acid racemase (NAAAR) and an L-selective aminoacylase from Geobacillus thermoglucosidasius with a stereoselective isoleucine dioxygenase from Bacillus thuringiensis, diastereomerically pure oxidized amino acids were produced from racemic N-acetylamino acids. The three enzymes differed in their optimal temperature and pH-spectra. Their different metal cofactor dependencies led to inhibitory effects. Under optimized conditions, racemic N-acetylmethionine was quantitatively converted into L-methionine-(S)-sulfoxide with 97% yield and 95% de. The combination of these three different biocatalysts allowed the direct synthesis of diastereopure oxyfunctionalized amino acids from inexpensive racemic starting material.

Original languageEnglish
Pages (from-to)425
JournalFrontiers in Microbiology
Volume7
DOIs
Publication statusPublished - 2016
Externally publishedYes

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Amino Acids
Geobacillus
Enzymes
Racemases and Epimerases
Dioxygenases
Bacillus thuringiensis
Acids
Isoleucine
Methionine
Metals
Temperature
N-acetylmethionine
methionine sulfoxide
aminoacylase I

Keywords

  • Journal Article

Cite this

A Multi-Enzymatic Cascade Reaction for the Stereoselective Production of γ-Oxyfunctionalyzed Amino Acids. / Enoki, Junichi; Meisborn, Jaqueline; Müller, Ann-Christin; Kourist, Robert.

In: Frontiers in Microbiology , Vol. 7, 2016, p. 425.

Research output: Contribution to journalArticleResearchpeer-review

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