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Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols

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Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols. / Grogan, Gideon James; Bennett, Megan; Ducrot, Laurine ; Vergne-Vaxelaire, Carine; Zaparucha, Anne; Bommarius, Andreas; Caparco, Adam; Champion, Julie.

In: Frontiers in Catalysis, 26.11.2021.

Research output: Contribution to journalArticlepeer-review

Harvard

Grogan, GJ, Bennett, M, Ducrot, L, Vergne-Vaxelaire, C, Zaparucha, A, Bommarius, A, Caparco, A & Champion, J 2021, 'Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols', Frontiers in Catalysis. https://doi.org/10.3389/fctls.2021.781284

APA

Grogan, G. J., Bennett, M., Ducrot, L., Vergne-Vaxelaire, C., Zaparucha, A., Bommarius, A., Caparco, A., & Champion, J. (2021). Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols. Frontiers in Catalysis. https://doi.org/10.3389/fctls.2021.781284

Vancouver

Grogan GJ, Bennett M, Ducrot L, Vergne-Vaxelaire C, Zaparucha A, Bommarius A et al. Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols. Frontiers in Catalysis. 2021 Nov 26. https://doi.org/10.3389/fctls.2021.781284

Author

Grogan, Gideon James ; Bennett, Megan ; Ducrot, Laurine ; Vergne-Vaxelaire, Carine ; Zaparucha, Anne ; Bommarius, Andreas ; Caparco, Adam ; Champion, Julie. / Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols. In: Frontiers in Catalysis. 2021.

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@article{5324d179b9b44257bae871cf23f41c47,
title = "Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols",
abstract = "Small optically active molecules, and more particularly short-chain chiral amines, are key 20 compounds in the chemical industry and precursors of various pharmaceuticals. Their chemo-21 biocatalytic production on a commercial scale is already established, mainly through lipase-22 catalyzed resolutions leading to ChiProsTM products among others. Nevertheless, their 23 biocatalytic synthesis still remains challenging for very short-chain C4 to C5 amines due to low 24 enantiomeric excess. To complement the possibilities recently offered by transaminases, this 25 work describes alternative biocatalytic access using amine dehydrogenases (AmDHs). Without 26 any protein engineering, some of the already described wild-type AmDHs (CfusAmDH, 27 MsmeAmDH, MicroAmDH and MATOUAmDH2) were shown to be efficient for the synthesis 28 of hydroxylated or unfunctionalized small 2-aminoalkanes. Conversions up to 97.1% were 29 reached at 50 mM, and moderate to high enantioselectivities were obtained, especially for (S)-30 1-methoxypropan-2-amine (98.1%), (S)-3-aminobutan-1-ol (99.5%), (3S)-3-aminobutan-2-ol 31 (99.4%) and the small (S)-butan-2-amine (93.6%) with MsmeAmDH. Semi-preparative scale 32 up experiments were successfully performed at 150 mM substrate concentrations for the 33 synthesis of (S)-butan-2-amine and (S)-1-methoxypropan-2-amine, the latter known as “(S)-34 MOIPA”. Modelling studies provided some preliminary results explaining the basis for the 35 challenging discrimination between similarly sized substituents in the active sites of these 36 enzymes.",
author = "Grogan, {Gideon James} and Megan Bennett and Laurine Ducrot and Carine Vergne-Vaxelaire and Anne Zaparucha and Andreas Bommarius and Adam Caparco and Julie Champion",
note = "{\textcopyright} 2021 Ducrot, Bennett, Caparco, Champion, Bommarius, Zaparucha, Grogan and Vergne-Vaxelaire.",
year = "2021",
month = nov,
day = "26",
doi = "10.3389/fctls.2021.781284",
language = "English",
journal = "Frontiers in Catalysis",
issn = "2673-7841",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Biocatalytic reductive amination by native Amine Dehydrogenases to access short chiral alkyl amines and amino alcohols

AU - Grogan, Gideon James

AU - Bennett, Megan

AU - Ducrot, Laurine

AU - Vergne-Vaxelaire, Carine

AU - Zaparucha, Anne

AU - Bommarius, Andreas

AU - Caparco, Adam

AU - Champion, Julie

N1 - © 2021 Ducrot, Bennett, Caparco, Champion, Bommarius, Zaparucha, Grogan and Vergne-Vaxelaire.

PY - 2021/11/26

Y1 - 2021/11/26

N2 - Small optically active molecules, and more particularly short-chain chiral amines, are key 20 compounds in the chemical industry and precursors of various pharmaceuticals. Their chemo-21 biocatalytic production on a commercial scale is already established, mainly through lipase-22 catalyzed resolutions leading to ChiProsTM products among others. Nevertheless, their 23 biocatalytic synthesis still remains challenging for very short-chain C4 to C5 amines due to low 24 enantiomeric excess. To complement the possibilities recently offered by transaminases, this 25 work describes alternative biocatalytic access using amine dehydrogenases (AmDHs). Without 26 any protein engineering, some of the already described wild-type AmDHs (CfusAmDH, 27 MsmeAmDH, MicroAmDH and MATOUAmDH2) were shown to be efficient for the synthesis 28 of hydroxylated or unfunctionalized small 2-aminoalkanes. Conversions up to 97.1% were 29 reached at 50 mM, and moderate to high enantioselectivities were obtained, especially for (S)-30 1-methoxypropan-2-amine (98.1%), (S)-3-aminobutan-1-ol (99.5%), (3S)-3-aminobutan-2-ol 31 (99.4%) and the small (S)-butan-2-amine (93.6%) with MsmeAmDH. Semi-preparative scale 32 up experiments were successfully performed at 150 mM substrate concentrations for the 33 synthesis of (S)-butan-2-amine and (S)-1-methoxypropan-2-amine, the latter known as “(S)-34 MOIPA”. Modelling studies provided some preliminary results explaining the basis for the 35 challenging discrimination between similarly sized substituents in the active sites of these 36 enzymes.

AB - Small optically active molecules, and more particularly short-chain chiral amines, are key 20 compounds in the chemical industry and precursors of various pharmaceuticals. Their chemo-21 biocatalytic production on a commercial scale is already established, mainly through lipase-22 catalyzed resolutions leading to ChiProsTM products among others. Nevertheless, their 23 biocatalytic synthesis still remains challenging for very short-chain C4 to C5 amines due to low 24 enantiomeric excess. To complement the possibilities recently offered by transaminases, this 25 work describes alternative biocatalytic access using amine dehydrogenases (AmDHs). Without 26 any protein engineering, some of the already described wild-type AmDHs (CfusAmDH, 27 MsmeAmDH, MicroAmDH and MATOUAmDH2) were shown to be efficient for the synthesis 28 of hydroxylated or unfunctionalized small 2-aminoalkanes. Conversions up to 97.1% were 29 reached at 50 mM, and moderate to high enantioselectivities were obtained, especially for (S)-30 1-methoxypropan-2-amine (98.1%), (S)-3-aminobutan-1-ol (99.5%), (3S)-3-aminobutan-2-ol 31 (99.4%) and the small (S)-butan-2-amine (93.6%) with MsmeAmDH. Semi-preparative scale 32 up experiments were successfully performed at 150 mM substrate concentrations for the 33 synthesis of (S)-butan-2-amine and (S)-1-methoxypropan-2-amine, the latter known as “(S)-34 MOIPA”. Modelling studies provided some preliminary results explaining the basis for the 35 challenging discrimination between similarly sized substituents in the active sites of these 36 enzymes.

U2 - 10.3389/fctls.2021.781284

DO - 10.3389/fctls.2021.781284

M3 - Article

JO - Frontiers in Catalysis

JF - Frontiers in Catalysis

SN - 2673-7841

ER -