Gordonia hydrophobica Nitrile Hydratase for Amide Preparation from Nitriles
Abstract
:1. Introduction
2. Results and Discussion
2.1. Influence of Reaction Temperature, Substrate Load and Catalyst Amount on Amide Production and Enantiomeric Excess (ee)
2.2. Enzyme Activity in the Presence of Additives
2.3. Effect of Reaction pH
2.4. Synthesis Reaction from Single Components
2.5. Exploration of Substrate Scope
3. Materials and Methods
3.1. General
3.2. Biocatalyst Preparation
3.3. Conversions of (R,S)-1a to (S)-1b
3.4. Enzyme Activity in the Presence of Additives
3.5. One-Pot Enzymatic Dynamic Kinetic Resolution by Strecker Reaction from Three Precursors
3.6. Chromatographic Assay for Substrate Scope Determination
4. Conclusions
Supplementary Materials
Author Contributions
Funding
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
- Yukl, E.T.; Wilmot, C.M. Cofactor biosynthesis through protein post-translational modification. Curr. Opin. Chem. Biol. 2012, 16, 54–59. [Google Scholar] [CrossRef] [Green Version]
- Asano, Y.; Yasuda, T.; Tani, Y.; Yamada, H. A New Enzymatic Method of Acrylamide Production. Agric. Biol. Chem. 1982, 46, 1183–1189. [Google Scholar] [CrossRef]
- Martinkova, L.; Mylerova, V. Synthetic Applications of Nitrile-Converting Enzymes. Curr. Org. Chem. 2003, 7, 1279–1295. [Google Scholar] [CrossRef]
- van Pelt, S.; Zhang, M.; Otten, L.G.; Holt, J.; Sorokin, D.Y.; van Rantwijk, F.; Black, G.W.; Perry, J.J.; Sheldon, R.A. Probing the enantioselectivity of a diverse group of purified cobalt-centred nitrile hydratases. Org. Biomol. Chem. 2011, 9, 3011. [Google Scholar] [CrossRef] [PubMed]
- Gotor, V.; Gotor-Fernández, V.; Busto, E. 7.6 Hydrolysis and Reverse Hydrolysis: Hydrolysis and Formation of Amides. In Comprehensive Chirality; Elsevier Ltd.: Amsterdam, The Netherlands, 2012; Volume 7, pp. 101–121. ISBN 9780080951683. [Google Scholar]
- Lin Lin Lee, V.; Kar Meng Choo, B.; Chung, Y.-S.; Kundap, U.P.; Kumari, Y.; Shaikh, M. Treatment, Therapy and Management of Metabolic Epilepsy: A Systematic Review. Int. J. Mol. Sci. 2018, 19, 871. [Google Scholar] [CrossRef] [Green Version]
- Lynch, B.A.; Lambeng, N.; Nocka, K.; Kensel-Hammes, P.; Bajjalieh, S.M.; Matagne, A.; Fuks, B. The synaptic vesicle is the protein SV2A is the binding site for the antiepileptic drug levetiracetam. Proc. Natl. Acad. Sci. USA 2004, 101, 9861–9866. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sills, G.J.; Rogawski, M.A. Mechanisms of action of currently used antiseizure drugs. Neuropharmacology 2020, 168, 107966. [Google Scholar] [CrossRef]
- Lukyanetz, E.A.; Shkryl, V.M.; Kostyuk, P.G. Selective Blockade of N-Type Calcium Channels by Levetiracetam. Epilepsia 2002, 43, 9–18. [Google Scholar] [CrossRef] [PubMed]
- Carunchio, I.; Pieri, M.; Ciotti, M.T.; Albo, F.; Zona, C. Modulation of AMPA Receptors in Cultured Cortical Neurons Induced by the Antiepileptic Drug Levetiracetam. Epilepsia 2007, 48, 654–662. [Google Scholar] [CrossRef] [PubMed]
- Meehan, A.L.; Yang, X.; Yuan, L.L.; Rothman, S.M. Levetiracetam has an activity-dependent effect on inhibitory transmission. Epilepsia 2012, 53, 469–476. [Google Scholar] [CrossRef]
- Noyer, M.; Gillard, M.; Matagne, A.; Hénichart, J.P.; Wülfert, E. The novel antiepileptic drug levetiracetam (ucb L059) appears to act via a specific binding site in CNS membranes. Eur. J. Pharmacol. 1995, 286, 137–146. [Google Scholar] [CrossRef]
- Kotkar, S.P.; Sudalai, A. A short enantioselective synthesis of the antiepileptic agent, levetiracetam based on proline-catalyzed asymmetric α-aminooxylation. Tetrahedron Lett. 2006, 47, 6813–6815. [Google Scholar] [CrossRef]
- Arndt, S.; Grill, B.; Schwab, H.; Steinkellner, G.; Pogorevčnik, U.; Weis, D.; Nauth, A.M.; Gruber, K.; Opatz, T.; Donsbach, K.; et al. The sustainable synthesis of levetiracetam by an enzymatic dynamic kinetic resolution and an: Ex-cell anodic oxidation. Green Chem. 2021, 23, 388–395. [Google Scholar] [CrossRef]
- Prasad, S.; Bhalla, T.C. Nitrile hydratases (NHases): At the interface of academia and industry. Biotechnol. Adv. 2010, 28, 725–741. [Google Scholar] [CrossRef]
- Hopmann, K.H. Full reaction mechanism of nitrile hydratase: A cyclic intermediate and an unexpected disulfide switch. Inorg. Chem. 2014, 53, 2760–2762. [Google Scholar] [CrossRef]
- Petrillo, K.L.; Wu, S.; Hann, E.C.; Cooling, F.B.; Ben-Bassat, A.; Gavagan, J.E.; DiCosimo, R.; Payne, M.S. Over-expression in Escherichia coli of a thermally stable and regio-selective nitrile hydratase from Comamonas testosteroni 5-MGAM-4D. Appl. Microbiol. Biotechnol. 2005, 67, 664–670. [Google Scholar] [CrossRef] [PubMed]
- Grill, B.; Glänzer, M.; Schwab, H.; Steiner, K.; Pienaar, D.; Brady, D.; Donsbach, K.; Winkler, M. Functional Expression and Characterization of a Panel of Cobalt and Iron-Dependent Nitrile Hydratases. Molecules 2020, 25, 2521. [Google Scholar] [CrossRef]
- Přepechalová, I.; Martínková, L.; Stolz, A.; Ovesná, M.; Bezouška, K.; Kopecký, J.; Křen, V. Purification and characterization of the enantioselective nitrile hydratase from Rhodococcus equi A4. Appl. Microbiol. Biotechnol. 2001, 55, 150–156. [Google Scholar] [CrossRef] [PubMed]
- Pawar, S.V.; Yadav, G.D. Enantioselective Enzymatic Hydrolysis of rac- Mandelonitrile to R-Mandelamide by Nitrile Hydratase Immobilized on Poly(vinyl alcohol)/Chitosan–Glutaraldehyde Support. Ind. Eng. Chem. Res. 2014, 53, 7986–7991. [Google Scholar] [CrossRef]
- D’Antona, N.; Morrone, R.; Gambera, G.; Pedotti, S. Enantiorecognition of planar “metallocenic” chirality by a nitrile hydratase/amidase bienzymatic system. Org. Biomol. Chem. 2016, 14, 4393–4399. [Google Scholar] [CrossRef] [PubMed]
- Reisinger, C.; Osprian, I.; Glieder, A.; Schoemaker, H.E.; Griengl, H.; Schwab, H. Enzymatic hydrolysis of cyanohydrins with recombinant nitrile hydratase and amidase from Rhodococcus erythropolis. Biotechnol. Lett. 2004, 26, 1675–1680. [Google Scholar] [CrossRef]
- Bui, K.; Maestracci, M.; Thiery, A.; Arnaud, A.; Galzy, P. A note on the enzymic action and biosynthesis of a nitrile-hydratase from a Brevibacterium sp. J. Appl. Bacteriol. 1984, 57, 183–190. [Google Scholar] [CrossRef]
- Murakami, T.; Nojiri, M.; Nakayama, H.; Dohmae, N.; Takio, K.; Odaka, M.; Endo, I.; Nagamune, T.; Yohda, M. Post-translational modification is essential for catalytic activity of nitrile hydratase. Protein Sci. 2000, 9, 1024–1030. [Google Scholar] [CrossRef] [Green Version]
- Krammer, B.; Rumbold, K.; Tschemmernegg, M.; Pöchlauer, P.; Schwab, H. A novel screening assay for hydroxynitrile lyases suitable for high-throughput screening. J. Biotechnol. 2007, 129, 151–161. [Google Scholar] [CrossRef] [PubMed]
- Huang, W.; Jia, J.; Cummings, J.; Nelson, M.; Schneider, G.; Lindqvist, Y. Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. Structure 1997, 5, 691–699. [Google Scholar] [CrossRef] [Green Version]
- Nagasawa, T.; Nanba, H.; Ryuno, K.; TakeuchiI, K.; Yamada, H. Nitrile hydratase of Pseudomonas chlororaphis B23. Purification and characterization. Eur. J. Biochem. 1987, 162, 691–698. [Google Scholar] [CrossRef]
- Tucker, J.L.; Xu, L.; Yu, W.; Scott, R.W.; Zhao, L.; Ran, N. Chemoenzymatic processes for preparation of levetiracetam. PCT Int. Appl. 2009, 9, A3. [Google Scholar]
- Cheng, Z.; Peplowski, L.; Cui, W.; Xia, Y.; Liu, Z.; Zhang, J.; Kobayashi, M.; Zhou, Z. Identification of key residues modulating the stereoselectivity of nitrile hydratase toward rac-mandelonitrile by semi-rational engineering. Biotechnol. Bioeng. 2018, 115, 524–535. [Google Scholar] [CrossRef]
- Mashweu, A.R.; Chhiba-Govindjee, V.P.; Bode, M.L.; Brady, D. Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870. Molecules 2020, 25, 238. [Google Scholar] [CrossRef] [Green Version]
- Patel, R.N. Pharmaceutical Intermediates by Biocatalysis: From Fundamental Science to Industrial Applications. In Applied Biocatalysis: From Fundamental Science to Industrial Applications; Wiley-VCH Verlag GmbH & Co. KGaA: Weinheim, Germany, 2016; pp. 367–403. [Google Scholar]
- Arroyo, M.; de la Mata, I.; García, J.L.; Barredo, J.L. Biocatalysis for Industrial Production of Active Pharmaceutical Ingredients (APIs). In Biotechnology of Microbial Enzymes: Production, Biocatalysis and Industrial Applications; Elsevier Inc.: Amsterdam, The Netherlands, 2017; pp. 451–473. ISBN 9780128037461. [Google Scholar]
- Santi, M.; Sancineto, L.; Nascimento, V.; Braun Azeredo, J.; Orozco, E.V.M.; Andrade, L.H.; Gröger, H.; Santi, C. Flow Biocatalysis: A Challenging Alternative for the Synthesis of APIs and Natural Compounds. Int. J. Mol. Sci. 2021, 22, 990. [Google Scholar] [CrossRef]
- Cowan, D.; Cramp, R.; Pereira, R.; Graham, D.; Almatawah, Q. Biochemistry and biotechnology of mesophilic and thermophilic nitrile metabolizing enzymes. Extremophiles 1998, 2, 207–216. [Google Scholar] [CrossRef] [PubMed]
- Chhiba, V.; Bode, M.L.; Mathiba, K.; Kwezi, W.; Brady, D. Enantioselective biocatalytic hydrolysis of β-aminonitriles to β-amino-amides using Rhodococcus rhodochrous ATCC BAA-870. J. Mol. Catal. B Enzym. 2012, 76, 68–74. [Google Scholar] [CrossRef]
- Nagasawa, T.; Mathew, C.D.; Mauger, J.; Yamada, H. Nitrile Hydratase-Catalyzed Production of Nicotinamide from 3-Cyanopyridine in Rhodococcus rhodochrous J1. Appl. Environ. Microbiol. 1988, 54, 1766–1769. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Zhou, S.; Yang, S.; Huang, G. Design, synthesis and biological activity of pyrazinamide derivatives for anti-Mycobacterium tuberculosis. J. Enzyme Inhib. Med. Chem. 2017, 32, 1183–1186. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Orejanrena Pacheco, J.C.; Opatz, T. NEXT Ring Expansion of 1,2,3,4-Tetrahydroisoquinolines to Dibenzo[c,f]azonines. An Unexpected [1,4]-Sigmatropic Rearrangement of Nitrile-Stabilized Ammonium Ylides. J. Org. Chem. 2014, 79, 5182–5192. [Google Scholar] [CrossRef] [PubMed]
Entry | GhNHase 1 [mg/mL] | T [°C] | (R,S)-1a [mM] | (S)-1b [mM] | ee (S)-1b [%] |
---|---|---|---|---|---|
1 | 0.34 | 25 | 10 | 1.4 | 78 |
2 | 0.54 | 37 | 10 | 1.3 | 78 |
3 | 0.54 | 50 | 10 | 1.6 | 77 |
4 | 0.34 | 25 | 20 | 4.2 | 79 |
5 | 0.34 | 25 | 50 | 5.0 | 78 |
6 | 0.34 | 25 | 100 | 6.1 | 77 |
7 | 0.69 | 25 | 50 | 13.5 | 65 |
8 | 0.69 | 5 | 50 | 11.8 | 61 |
Entry | NHase | KCN [mM] | Pyrrolidine [mM] | Propanal [mM] | (S)-1b [mM] | ee (S)-1b [%] |
---|---|---|---|---|---|---|
1 | GhHNase | 26.9 | 29.4 | approx. 30 1 | 2.3 ± 0.0 | 75.9 ± 0.2 |
2 | CtNHase | 26.9 | 29.4 | approx. 30 1 | 0.1 ± 0.0 | n.d. 2 |
3 | GhHNase | 26.9 | 29.4 | approx. 90 1 | 8.4 ± 0.4 | 73.9 ± 0.1 |
4 | CtNHase | 26.9 | 29.4 | approx. 90 1 | 4.9 ± 0.1 | 82.1 ± 0.1 |
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. |
© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Grill, B.; Horvat, M.; Schwab, H.; Gross, R.; Donsbach, K.; Winkler, M. Gordonia hydrophobica Nitrile Hydratase for Amide Preparation from Nitriles. Catalysts 2021, 11, 1287. https://0-doi-org.brum.beds.ac.uk/10.3390/catal11111287
Grill B, Horvat M, Schwab H, Gross R, Donsbach K, Winkler M. Gordonia hydrophobica Nitrile Hydratase for Amide Preparation from Nitriles. Catalysts. 2021; 11(11):1287. https://0-doi-org.brum.beds.ac.uk/10.3390/catal11111287
Chicago/Turabian StyleGrill, Birgit, Melissa Horvat, Helmut Schwab, Ralf Gross, Kai Donsbach, and Margit Winkler. 2021. "Gordonia hydrophobica Nitrile Hydratase for Amide Preparation from Nitriles" Catalysts 11, no. 11: 1287. https://0-doi-org.brum.beds.ac.uk/10.3390/catal11111287