Development of an R-selective amine oxidase with broad substrate specificity and high enantioselectivityCitation formats

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Development of an R-selective amine oxidase with broad substrate specificity and high enantioselectivity. / Heath, Rachel; Pontini, Marta; Turner, Nicholas; Bechi, Beatrice.

In: ChemCatChem, Vol. 6, No. 4, 2014, p. 996-1002.

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Heath, Rachel ; Pontini, Marta ; Turner, Nicholas ; Bechi, Beatrice. / Development of an R-selective amine oxidase with broad substrate specificity and high enantioselectivity. In: ChemCatChem. 2014 ; Vol. 6, No. 4. pp. 996-1002.

Bibtex

@article{5a9b497e4e53416f85aecc0a74ddc7de,
title = "Development of an R-selective amine oxidase with broad substrate specificity and high enantioselectivity",
abstract = "Amine oxidases are useful bio-catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO-N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R-selective amine oxidase based on 6-hydroxy-D-nicotine oxidase (6-HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6-HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S-configured products, for example, (S)-nicotine, in high ee.",
author = "Rachel Heath and Marta Pontini and Nicholas Turner and Beatrice Bechi",
year = "2014",
doi = "10.1002/cctc.201301008",
language = "English",
volume = "6",
pages = "996--1002",
journal = "ChemCatChem (Online)",
issn = "1867-3880",
publisher = "John Wiley & Sons Ltd",
number = "4",

}

RIS

TY - JOUR

T1 - Development of an R-selective amine oxidase with broad substrate specificity and high enantioselectivity

AU - Heath, Rachel

AU - Pontini, Marta

AU - Turner, Nicholas

AU - Bechi, Beatrice

PY - 2014

Y1 - 2014

N2 - Amine oxidases are useful bio-catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO-N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R-selective amine oxidase based on 6-hydroxy-D-nicotine oxidase (6-HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6-HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S-configured products, for example, (S)-nicotine, in high ee.

AB - Amine oxidases are useful bio-catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO-N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R-selective amine oxidase based on 6-hydroxy-D-nicotine oxidase (6-HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6-HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S-configured products, for example, (S)-nicotine, in high ee.

U2 - 10.1002/cctc.201301008

DO - 10.1002/cctc.201301008

M3 - Article

VL - 6

SP - 996

EP - 1002

JO - ChemCatChem (Online)

JF - ChemCatChem (Online)

SN - 1867-3880

IS - 4

ER -