A reductive aminase from Aspergillus oryzaeCitation formats

  • External authors:
  • Godwin Aleku
  • Scott France
  • Henry Man
  • Juan Mangas-Sanchez
  • Sarah Montgomery
  • Mahima Sharma
  • Friedemann Leipold
  • Shahed Hussain
  • Gideon Grogan

Standard

A reductive aminase from Aspergillus oryzae. / Aleku, Godwin; France, Scott; Man, Henry; Mangas-Sanchez, Juan; Montgomery, Sarah; Sharma, Mahima; Leipold, Friedemann; Hussain, Shahed; Grogan, Gideon; Turner, Nicholas.

In: Nature Chemistry, 2017.

Research output: Contribution to journalArticle

Harvard

Aleku, G, France, S, Man, H, Mangas-Sanchez, J, Montgomery, S, Sharma, M, Leipold, F, Hussain, S, Grogan, G & Turner, N 2017, 'A reductive aminase from Aspergillus oryzae', Nature Chemistry. https://doi.org/10.1038/nchem.2782

APA

Aleku, G., France, S., Man, H., Mangas-Sanchez, J., Montgomery, S., Sharma, M., ... Turner, N. (2017). A reductive aminase from Aspergillus oryzae. Nature Chemistry. https://doi.org/10.1038/nchem.2782

Vancouver

Aleku G, France S, Man H, Mangas-Sanchez J, Montgomery S, Sharma M et al. A reductive aminase from Aspergillus oryzae. Nature Chemistry. 2017. https://doi.org/10.1038/nchem.2782

Author

Aleku, Godwin ; France, Scott ; Man, Henry ; Mangas-Sanchez, Juan ; Montgomery, Sarah ; Sharma, Mahima ; Leipold, Friedemann ; Hussain, Shahed ; Grogan, Gideon ; Turner, Nicholas. / A reductive aminase from Aspergillus oryzae. In: Nature Chemistry. 2017.

Bibtex

@article{721ce2103af148c39fa8bd757afa1c88,
title = "A reductive aminase from Aspergillus oryzae",
abstract = "Reductive amination is one of the most important methods for the synthesis of chiral amines. Here we report the discovery of an NADP(H)-dependent reductive aminase from Aspergillus oryzae (AspRedAm, Uniprot code Q2TW47) that can catalyse the reductive coupling of a broad set of carbonyl compounds with a variety of primary and secondary amines with up to >98{\%} conversion and with up to >98{\%} enantiomeric excess. In cases where both carbonyl and amine show high reactivity, it is possible to employ a 1:1 ratio of the substrates, forming amine products with up to 94{\%} conversion. Steady-state kinetic studies establish that the enzyme is capable of catalysing imine formation as well as reduction. Crystal structures of AspRedAm in complex with NADP(H) and also with both NADP(H) and the pharmaceutical ingredient (R)-rasagiline are reported. We also demonstrate preparative scale reductive aminations with wild-type and Q240A variant biocatalysts displaying total turnover numbers of up to 32,000 and space time yields up to 3.73 g l−1 d−1.",
author = "Godwin Aleku and Scott France and Henry Man and Juan Mangas-Sanchez and Sarah Montgomery and Mahima Sharma and Friedemann Leipold and Shahed Hussain and Gideon Grogan and Nicholas Turner",
year = "2017",
doi = "10.1038/nchem.2782",
language = "English",
journal = "Nature Chemistry",
issn = "1755-4330",
publisher = "Springer Nature",

}

RIS

TY - JOUR

T1 - A reductive aminase from Aspergillus oryzae

AU - Aleku, Godwin

AU - France, Scott

AU - Man, Henry

AU - Mangas-Sanchez, Juan

AU - Montgomery, Sarah

AU - Sharma, Mahima

AU - Leipold, Friedemann

AU - Hussain, Shahed

AU - Grogan, Gideon

AU - Turner, Nicholas

PY - 2017

Y1 - 2017

N2 - Reductive amination is one of the most important methods for the synthesis of chiral amines. Here we report the discovery of an NADP(H)-dependent reductive aminase from Aspergillus oryzae (AspRedAm, Uniprot code Q2TW47) that can catalyse the reductive coupling of a broad set of carbonyl compounds with a variety of primary and secondary amines with up to >98% conversion and with up to >98% enantiomeric excess. In cases where both carbonyl and amine show high reactivity, it is possible to employ a 1:1 ratio of the substrates, forming amine products with up to 94% conversion. Steady-state kinetic studies establish that the enzyme is capable of catalysing imine formation as well as reduction. Crystal structures of AspRedAm in complex with NADP(H) and also with both NADP(H) and the pharmaceutical ingredient (R)-rasagiline are reported. We also demonstrate preparative scale reductive aminations with wild-type and Q240A variant biocatalysts displaying total turnover numbers of up to 32,000 and space time yields up to 3.73 g l−1 d−1.

AB - Reductive amination is one of the most important methods for the synthesis of chiral amines. Here we report the discovery of an NADP(H)-dependent reductive aminase from Aspergillus oryzae (AspRedAm, Uniprot code Q2TW47) that can catalyse the reductive coupling of a broad set of carbonyl compounds with a variety of primary and secondary amines with up to >98% conversion and with up to >98% enantiomeric excess. In cases where both carbonyl and amine show high reactivity, it is possible to employ a 1:1 ratio of the substrates, forming amine products with up to 94% conversion. Steady-state kinetic studies establish that the enzyme is capable of catalysing imine formation as well as reduction. Crystal structures of AspRedAm in complex with NADP(H) and also with both NADP(H) and the pharmaceutical ingredient (R)-rasagiline are reported. We also demonstrate preparative scale reductive aminations with wild-type and Q240A variant biocatalysts displaying total turnover numbers of up to 32,000 and space time yields up to 3.73 g l−1 d−1.

U2 - 10.1038/nchem.2782

DO - 10.1038/nchem.2782

M3 - Article

JO - Nature Chemistry

JF - Nature Chemistry

SN - 1755-4330

ER -