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Microbial and enzymatic synthesis of optically pure D- and L-3-trimethylsilyl-alanine by deracemization of D,L-5-trimethylsilyl-methyl-hydantion


Pietzsch, Markus; Waniek, Thomas; Smith, Richard J; Bratovanov, Svetoslav; Bienz, Stefan; Syldatk, Christoph (2000). Microbial and enzymatic synthesis of optically pure D- and L-3-trimethylsilyl-alanine by deracemization of D,L-5-trimethylsilyl-methyl-hydantion. Monatshefte Für Chemie / Chemical Monthly, 131(6):645-653.

Abstract

The sterospecificities of hydantoinases and N-carbamoyl amino acid amidohydrolases (N-carbamoylases) from different microbial sources were investigated for the stereoselective syntheses of the unnatural silicon-containing amino acids D- and L-3-trimethylsilyl-alanine (3) from the respective racemic hydantoin D,L-1. In a preparative biotransformation, whole resting cells of Agrobacterium sp. IP I 671, immobilized in a Ca-alginate matrix, were used for the synthesis of amino acid D-3 in 88% yield and 95% enantiomeric excess. Since the purified D-N-carbamoylase from Agrobacterium sp. IP I 671 was shown to be 100%D-selective, the enantiomeric purity of 95% of D-3 arising from the transformation with the immobilized cells must be explained by the participation of a further, L-selective N-carbamoylase or, which is more likely, by racemization of the final hydrolysis product by the action of an amino acid racemase. Isolated hydantoinases from Bacillus thermoglucosidasius, Thermus sp., Arthrobacter aurescens DSM 3745, and Arthrobacter crystallopoietes DSM 20117 turned out to be stereospecific for the conversion of the D-form of hydantoin D,L-1. The enantiomerically pure L-form of 3 was also prepared. It was synthesized from racemic N-carbamoyl amino acid D,L-2 by enantiomer-specific hydrolysis of the L-form in presence of L-N-carbamoylase from Arthrobacter aurescens DSM 3747.

Abstract

The sterospecificities of hydantoinases and N-carbamoyl amino acid amidohydrolases (N-carbamoylases) from different microbial sources were investigated for the stereoselective syntheses of the unnatural silicon-containing amino acids D- and L-3-trimethylsilyl-alanine (3) from the respective racemic hydantoin D,L-1. In a preparative biotransformation, whole resting cells of Agrobacterium sp. IP I 671, immobilized in a Ca-alginate matrix, were used for the synthesis of amino acid D-3 in 88% yield and 95% enantiomeric excess. Since the purified D-N-carbamoylase from Agrobacterium sp. IP I 671 was shown to be 100%D-selective, the enantiomeric purity of 95% of D-3 arising from the transformation with the immobilized cells must be explained by the participation of a further, L-selective N-carbamoylase or, which is more likely, by racemization of the final hydrolysis product by the action of an amino acid racemase. Isolated hydantoinases from Bacillus thermoglucosidasius, Thermus sp., Arthrobacter aurescens DSM 3745, and Arthrobacter crystallopoietes DSM 20117 turned out to be stereospecific for the conversion of the D-form of hydantoin D,L-1. The enantiomerically pure L-form of 3 was also prepared. It was synthesized from racemic N-carbamoyl amino acid D,L-2 by enantiomer-specific hydrolysis of the L-form in presence of L-N-carbamoylase from Arthrobacter aurescens DSM 3747.

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Additional indexing

Item Type:Journal Article, not refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:D-3-Trimethylsilyl-alanine; Hydantoinase; N-Carbamoyl amino acid amidohydrolase; N-Carbamoylase; Biotransformation
Language:English
Date:2000
Deposited On:23 Aug 2017 15:52
Last Modified:23 Aug 2017 15:52
Publisher:Springer
ISSN:0026-9247
Publisher DOI:https://doi.org/10.1007/s007060070093

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