Isomerizations

Asano, Yasuhisa; Hölsch, Kathrin

doi:10.1002/9783527639861.ch39

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Dehalogenases1

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Cited by 9 publications

(1 citation statement)

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“…They can convert both substrate enantiomers, which is quite unusual for enzymatic reactions and is only typical for the group of racemases [70]. Their reaction mechanism differs from l -2-haloacid dehalogenases such that it does not involve the formation of a covalent enzyme–substrate–ester intermediate, but proceeds through direct nucleophilic attack of an activated water molecule at the chiral carbon center.…”

Section: Dehalogenasesmentioning

confidence: 99%

Inverting hydrolases and their use in enantioconvergent biotransformations

Schöber¹,

Faber²

2013

Trends in Biotechnology

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Section: Dehalogenasesmentioning

confidence: 99%

Inverting hydrolases and their use in enantioconvergent biotransformations

Schöber¹,

Faber²

2013

Trends in Biotechnology

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Recent Developments in Aminopeptidases, Racemases, and Oxidases

2016

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An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity

et al. 2018

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The kinetic resolution of amino acid esters (AAEs) is a useful synthetic strategy for the preparation of single-enantiomer amino acids. The development of an enzymatic dynamic kinetic resolution (DKR) process for AAEs, which would give a theoretical yield of 100 % of the enantiopure product, would require an amino acid ester racemase (AAER); however, no such enzyme has been described. We have identified low AAER activity of 15 U mg in a homologue of a PLP-dependent α-amino ϵ-caprolactam racemase (ACLR) from Ochrobactrum anthropi. We have determined the structure of this enzyme, OaACLR, to a resolution of 1.87 Å and, by using structure-guided saturation mutagenesis, in combination with a colorimetric screen for AAER activity, we have identified a mutant, L293C, in which the promiscuous AAER activity of this enzyme towards l-phenylalanine methyl ester is improved 3.7-fold.

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Isomerizations

Cited by 9 publications

References 422 publications

Inverting hydrolases and their use in enantioconvergent biotransformations

Inverting hydrolases and their use in enantioconvergent biotransformations

Recent Developments in Aminopeptidases, Racemases, and Oxidases

An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity

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