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Cyclohexylamine Oxidase As Useful Biocatalyst for the Kinetic Resolution and Dereacemization of Amines

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Cyclohexylamine Oxidase As Useful Biocatalyst for the Kinetic Resolution and Dereacemization of Amines NRC Publications Archive Archives des publications du CNRC Cyclohexylamine oxidase as useful biocatalyst for the kinetic resolution and dereacemization of amines Leisch, Hannes; Grosse, Stephan; Iwaki, Hiroaki; Hasegawa, Yoshie; Lau, Peter C. K. This publication could be one of several versions: author’s original, accepted manuscript or the publisher’s version. / La version de cette publication peut être l’une des suivantes : la version prépublication de l’auteur, la version acceptée du manuscrit ou la version de l’éditeur. For the publisher’s version, please access the DOI link below./ Pour consulter la version de l’éditeur, utilisez le lien DOI ci-dessous. Publisher’s version / Version de l'éditeur: https://doi.org/10.1139/V11-086 Canadian Journal of Chemistry, 90, 1, pp. 39-45, 2011-10-19 NRC Publications Record / Notice d'Archives des publications de CNRC: https://nrc-publications.canada.ca/eng/view/object/?id=ddb28c81-104c-406a-84e7-418332bfeb72 https://publications-cnrc.canada.ca/fra/voir/objet/?id=ddb28c81-104c-406a-84e7-418332bfeb72 Access and use of this website and the material on it are subject to the Terms and Conditions set forth at https://nrc-publications.canada.ca/eng/copyright READ THESE TERMS AND CONDITIONS CAREFULLY BEFORE USING THIS WEBSITE. L’accès à ce site Web et l’utilisation de son contenu sont assujettis aux conditions présentées dans le site https://publications-cnrc.canada.ca/fra/droits LISEZ CES CONDITIONS ATTENTIVEMENT AVANT D’UTILISER CE SITE WEB. Questions? Contact the NRC Publications Archive team at [email protected]. If you wish to email the authors directly, please see the first page of the publication for their contact information. Vous avez des questions? Nous pouvons vous aider. Pour communiquer directement avec un auteur, consultez la première page de la revue dans laquelle son article a été publié afin de trouver ses coordonnées. Si vous n’arrivez pas à les repérer, communiquez avec nous à [email protected]. 39 Cyclohexylamine oxidase as a useful biocatalyst for the kinetic resolution and dereacemization of amines Hannes Leisch, Stephan Grosse, Hiroaki Iwaki, Yoshie Hasegawa, and Peter C.K. Lau Abstract: The biocatalytic performance of a cloned cyclohexylamine oxidase derived from Brevibacterium oxydans IH-35A towards structurally different amines was investigated. Cycloalkyl primary amines, alkyl aryl amines, and a-carbon-substituted aliphatic amines were identified as suitable substrates for the biocatalyst based on an activity assay. Kinetic resolutions of several amines by either recombinant whole cells or crude enzyme extracts prepared therefrom gave enantiomerically pure (R)-amines besides the corresponding ketones. When cyclohexylamine oxidase in combination with a borane– ammonia complex as reducing agent was applied to the deracemization of several substrates, excellent enantiomeric ratios (>99:1) and good isolated yields (62%–75%) of the corresponding (R)-amines were obtained. Key words: biocatalysis, cyclohexylamine oxidase, chiral amines, kinetic resolution, deracemization. Résumé : On a étudié la performance biocatalytique d’un clone de l’oxydase de la cyclohexylamine dérivé du Brevibacterium oxydans IH-35A vis-à-vis des amines de structures diverses. Sur la base d’un essai d’activité, il a été possible d’identi- fier les cycloalkylamines primaires, les alkylarylamines primaires et les amines aliphatiques portant un substituant sur le carbone en a comme des substrats appropriés pour le biocatalyseur. Les résolutions cinétiques de plusieurs amines par des cellules recombinantes complètes ou des extraits bruts d’enzyme préparés à partir de celles-ci conduisent à des amines (R) énantiomériquement pures aux côtés des cétones correspondantes. On a utilisé l’oxydase de la cyclohexylamine en combinaison avec un complexe de borane–ammoniac comme agent réducteur pour effectuer la déracémisation de plu- sieurs substrats, avec d’excellents rapports énantiomériques (>99/1) et de bons rendements en produits isolés (72 % à 75 %) des amines (R) correspondantes. Mots‐clés : biocatalyseur, oxydase de la cyclohexylamine, amines chirales, résolution cinétique, déracémisation. For personal use only. [Traduit par la Rédaction] Introduction applicatons of u-transaminases, which can be either used for the kinetic resolution of racemic amines and amino acids or The importance of enantiomerically pure amines as starting for the asymmetric synthesis of amines from ketones.4 materials for pharmaceuticals and agrochemicals, as chiral In addition, the ability of flavoproteins to oxidize amines auxiliaries, and as resolving agents is beyond question.1 De- to imines has been exploited for the synthesis of chiral spite the wide applications of chiral amines in chemistry, 5 medicine, and biology, their synthesis remains challenging. amines (Scheme 1). Initial experiments by Hafner and 6 Chemical protocols include the resolution of racemic amines Weller using D-amino acid oxidase in combination with so- as their diasteriomeric salts, enantioselective enamide and dium borohydride led to the preparation of L-amino acids imine reduction, reductive amination, olefin hydroamination, from the corresponding R-enantiomers. Applying the same and enantioselective carbanion addition to imines.2 Alterna- concept, Soda and co-workers7 demonstrated the deracemiza- tive to the chemical method biocatalytic routes have been de- tion of racemic amino acids. Synthetically useful protocols, veloped as promising strategies.3 Most notably are the which allowed for the synthesis of enantiopure amino acids Can. J. Chem. Downloaded from www.nrcresearchpress.com by National Research Council of Canada on 01/04/12 Received 11 April 2011. Accepted 26 June 2011. Published at www.nrcresearchpress.com/cjc on 19 October 2011. H. Leisch and S. Grosse. Biotechnology Research Institute, National Research Council Canada, 6100 Royalmount Avenue, Montreal, QC H4P 2R2, Canada. H. Iwaki and Y. Hasegawa. Department of Life Science and Biotechnology and ORDIST, Kansai University, Suita, Osaka 564-8680, Japan. P.C.K. Lau. Biotechnology Research Institute, National Research Council Canada, 6100 Royalmount Avenue, Montreal, QC H4P 2R2, Canada; McGill University, Department of Chemistry and Department of Microbiology and Immunology, 3775 University Street, Montreal, QC H3A 2B4, Canada; FQRNT Centre in Green Chemistry and Catalysis, Montreal, QC, Canada. Corresponding author: Peter C.K. Lau (e-mail: [email protected]). This article is part of a Special Issue dedicated to Professor Tak-Hang Chan in recognition and admiration of his long-standing contribu- tions to green catalysis and synthesis. Can. J. Chem. 90:39–45 (2012) doi:10.1139/V11-086 Published by NRC Research Press NRCC 53377 40 Can. J. Chem. Vol. 90, 2012 Scheme 1. Proposed mechanism for the oxidation of amines with flavoproteins by nucleophilic attack of the heteroatam at C-4 of the flavo- protein.5 N NO N NO NH N NH O - N H O Recycling of FADH H OH O H2O2 OH OO N NO N NO N NO NH NH NH N N N H O NH2 - O FA D O H FADH NH2 NH2 O NH3 H 2O in aqueous buffer in excellent yields from racemic starting materials, were de- catalyst produced would be capable of transforming 40 g of veloped by Turner and co-workers8 using porcine D-amino cyclohexylamine per h. Interestingly, 4-methyl cyclohexyl- acid oxidase. Subsequently, the application of recombinant amine (2) was oxidized 1.3 times faster than cyclohexylamine monoamine oxidase from Aspergillus niger9 and mutants (1). Additionally, a-alkyl aryl derivatives 9–15 and a-carbon- obtained by directed evolution led to the development of bio- substituted aliphatic amines 17–21 were acceptable sub- 10 catalytic protocols for the deracemization of primary, strates, whereas compounds of the structure R–CH2–NH2 secondary,11 and tertiary amines,12 desymmetrization of sub- (22–25) and straight-chain and cyclic secondary and tertiary stituted pyrrolidines,13 enantioselective oxidation of hydrox- amines showed very limited activity. Amino acids and mono- ylamines,14 and the design of tandem biocatalysis For personal use only. amine neurotransmitters such as dopamine (31) or serotonin multicomponent reactions.15 (32) were not oxidized by CHAO. With respect to enantiose- Prompted by the wide-ranging applications and excellent lectivity of CHAO we tested the oxidation rates of enantio- enantioselectivity of monoamine oxidase and its mutants merically pure (R)- and (S)-a-methyl benzylamine (9) and from A. niger, we were interested in the exploitation of a bac- 2-heptylamine (18). In both cases, CHAO displayed virtu- terial amine oxidase as an alternative or complementary bio- ally no detectable activity for the (S)-enantiomers, indicating catalyst. As a result, cyclohexylamine oxidase (CHAO), a a highly enantioselective biocatalyst. 50 kDa flavoprotein responsible for the oxidation of cyclo- To demonstrate the practicality of CHAO in the syntheses hexylamine to cyclohexanone in Brevibacterium oxydans IH- of chiral amines, we tested either whole cells overexpressing 35A,16 was investigated and this new biocatalytic potential is CHAO or crude enzyme extracts for the kinetic resolution of reported herein. racemic amines (Table 1). a-Alkyl aryl derivatives 9–12, 14, and 15 were resolved in excellent enantioselectivities and Results and discussion CHAO selectively oxidized the (S)-enantiomer of the aryl To gain access to sufficient amounts of CHAO, the amine derivative to the corresponding
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