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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I03-Macromolecular Crystallography	A reductive aminase from Aspergillus oryzae Godwin A. Aleku , Scott P. France , Henry Man , Juan Mangas-Sanchez , Sarah L. Montgomery , Mahima Sharma , Friedemann Leipold , Shahed Hussain , Gideon Grogan , Nicholas J. Turner Nature Chemistry 94 DOI: 10.1038/nchem.2782 Diamond Proposal Number(s): [9948] Show Abstract ▼ 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.	May 2017

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I02-Macromolecular Crystallography
I03-Macromolecular Crystallography

A reductive aminase from Aspergillus oryzae

Godwin A. Aleku , Scott P. France , Henry Man , Juan Mangas-Sanchez , Sarah L. Montgomery , Mahima Sharma , Friedemann Leipold , Shahed Hussain , Gideon Grogan , Nicholas J. Turner

Nature Chemistry 94

DOI: 10.1038/nchem.2782

Diamond Proposal Number(s): [9948]

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May 2017