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Volumn 8, Issue 11, 2016, Pages 1076-1082

Identification of (S)-selective transaminases for the asymmetric synthesis of bulky chiral amines

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; AMINOTRANSFERASE; QUINONE DERIVATIVE;

EID: 84992316292     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.2578     Document Type: Article
Times cited : (197)

References (28)
  • 1
    • 77149171446 scopus 로고    scopus 로고
    • Efficient production of enantiomerically pure chiral amines at concentrations of 50 g/L using transaminases
    • Truppo, M. D., Rozzell, J. D. & Turner, N. J. Efficient production of enantiomerically pure chiral amines at concentrations of 50 g/L using transaminases. Org. Process Res. Dev. 14, 234-237 (2010).
    • (2010) Org. Process Res. Dev. , vol.14 , pp. 234-237
    • Truppo, M.D.1    Rozzell, J.D.2    Turner, N.J.3
  • 2
    • 77954797329 scopus 로고    scopus 로고
    • Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture
    • Savile, C. K. et al. Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture. Science 329, 305-309 (2010).
    • (2010) Science , vol.329 , pp. 305-309
    • Savile, C.K.1
  • 3
    • 84946227043 scopus 로고    scopus 로고
    • The industrial age of biocatalytic transamination
    • Fuchs, M., Farnberger, J. E. & Kroutil, W. The industrial age of biocatalytic transamination. Eur. J. Org. Chem. 2015, 6965-6982 (2015).
    • (2015) Eur. J. Org. Chem. , vol.2015 , pp. 6965-6982
    • Fuchs, M.1    Farnberger, J.E.2    Kroutil, W.3
  • 4
    • 84931009357 scopus 로고    scopus 로고
    • Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications
    • Steffen-Munsberg, F. et al. Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications. Biotechnol. Adv. 33, 566-604 (2015).
    • (2015) Biotechnol. Adv. , vol.33 , pp. 566-604
    • Steffen-Munsberg, F.1
  • 5
    • 77953120732 scopus 로고    scopus 로고
    • σ-Transaminases for the synthesis of non-racemic α-chiral primary amines
    • Koszelewski, D., Tauber, K., Faber, K. & Kroutil, W. σ-Transaminases for the synthesis of non-racemic α-chiral primary amines. Trends Biotechnol. 28, 324-332 (2010).
    • (2010) Trends Biotechnol. , vol.28 , pp. 324-332
    • Koszelewski, D.1    Tauber, K.2    Faber, K.3    Kroutil, W.4
  • 6
    • 77954791339 scopus 로고    scopus 로고
    • Transaminations with isopropyl amine: Equilibrium displacement with yeast alcohol dehydrogenase coupled to in situ cofactor regeneration
    • Cassimjee, K. E., Branneby, C., Vahak, A., Wells, A. & Berglund, P. Transaminations with isopropyl amine: equilibrium displacement with yeast alcohol dehydrogenase coupled to in situ cofactor regeneration. Chem. Commun. 46, 5569-5571 (2010).
    • (2010) Chem. Commun. , vol.46 , pp. 5569-5571
    • Cassimjee, K.E.1    Branneby, C.2    Vahak, A.3    Wells, A.4    Berglund, P.5
  • 7
    • 56749102605 scopus 로고    scopus 로고
    • Asymmetric synthesis of optically pure pharmacologically relevant amines employing σ-transaminases
    • Koszelewski, D., Lavandera, I., Clay, D., Rozzell, D. & Kroutil, W. Asymmetric synthesis of optically pure pharmacologically relevant amines employing σ-transaminases. Adv. Synth. Catal. 350, 2761-2766 (2008).
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 2761-2766
    • Koszelewski, D.1    Lavandera, I.2    Clay, D.3    Rozzell, D.4    Kroutil, W.5
  • 8
    • 84915733006 scopus 로고    scopus 로고
    • Chiral amine synthesis using σ-transaminases: An amine donor that displaces equilibria and enables high-throughput screening
    • Green, A. P., Turner, N. J. & O'Reilly, E. Chiral amine synthesis using σ-transaminases: an amine donor that displaces equilibria and enables high-throughput screening. Angew. Chem. Int. Ed. 53, 10714-10717 (2014).
    • (2014) Angew. Chem. Int. Ed. , vol.53 , pp. 10714-10717
    • Green, A.P.1    Turner, N.J.2    O'Reilly, E.3
  • 9
    • 77958167211 scopus 로고    scopus 로고
    • Rational assignment of key motifs for function guides in silico enzyme identification
    • Höhne, M., Schätzle, S., Jochens, H., Robins, K. & Bornscheuer, U. T. Rational assignment of key motifs for function guides in silico enzyme identification. Nature Chem. Biol. 6, 807-813 (2010).
    • (2010) Nature Chem. Biol. , vol.6 , pp. 807-813
    • Höhne, M.1    Schätzle, S.2    Jochens, H.3    Robins, K.4    Bornscheuer, U.T.5
  • 10
    • 79951914183 scopus 로고    scopus 로고
    • Sitagliptin manufacture: A compelling tale of green chemistry, process intensification, and industrial asymmetric catalysis
    • Desai, A. A. Sitagliptin manufacture: a compelling tale of green chemistry, process intensification, and industrial asymmetric catalysis. Angew. Chem. Int. Ed. 50, 1974-1976 (2011).
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 1974-1976
    • Desai, A.A.1
  • 11
    • 85027954698 scopus 로고    scopus 로고
    • Mechanism-guided engineering of σ-transaminase to accelerate reductive amination of ketones
    • Han, S.-W., Park, E.-S., Dong, J.-Y. & Shin, J.-S. Mechanism-guided engineering of σ-transaminase to accelerate reductive amination of ketones. Adv. Synth. Catal. 357, 1732-1740 (2015).
    • (2015) Adv. Synth. Catal. , vol.357 , pp. 1732-1740
    • Han, S.-W.1    Park, E.-S.2    Dong, J.-Y.3    Shin, J.-S.4
  • 12
    • 84899937645 scopus 로고    scopus 로고
    • The substrate specificity, enantioselectivity and structure of the (R)-selective amine: Pyruvate transaminase from Nectria haematococca
    • Sayer, C. et al. The substrate specificity, enantioselectivity and structure of the (R)-selective amine: pyruvate transaminase from Nectria haematococca. FEBS J. 281, 2240-2253 (2014).
    • (2014) FEBS J. , vol.281 , pp. 2240-2253
    • Sayer, C.1
  • 13
    • 84890825384 scopus 로고    scopus 로고
    • Substrate profile of an σ-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids
    • Jiang, J., Chen, X., Feng, J., Wu, Q. & Zhu, D. Substrate profile of an σ-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids. J. Mol. Catal. B 100, 32-39 (2014).
    • (2014) J. Mol. Catal. B , vol.100 , pp. 32-39
    • Jiang, J.1    Chen, X.2    Feng, J.3    Wu, Q.4    Zhu, D.5
  • 14
    • 84922517376 scopus 로고    scopus 로고
    • Engineering the active site of the amine transaminase from Vibrio fluvialis for the asymmetric synthesis of aryl-alkyl amines and amino alcohols
    • Nobili, A. et al. Engineering the active site of the amine transaminase from Vibrio fluvialis for the asymmetric synthesis of aryl-alkyl amines and amino alcohols. ChemCatChem 7, 757-760 (2015).
    • (2015) ChemCatChem , vol.7 , pp. 757-760
    • Nobili, A.1
  • 15
    • 84946934980 scopus 로고    scopus 로고
    • Alteration of the donor/acceptor spectrum of the (S)-amine transaminase from Vibrio fluvialis
    • Genz, M. et al. Alteration of the donor/acceptor spectrum of the (S)-amine transaminase from Vibrio fluvialis. Int. J. Mol. Sci. 16, 26953-26963 (2015).
    • (2015) Int. J. Mol. Sci. , vol.16 , pp. 26953-26963
    • Genz, M.1
  • 16
    • 84871649774 scopus 로고    scopus 로고
    • Connecting unexplored protein crystal structures to enzymatic function
    • Steffen-Munsberg, F. et al. Connecting unexplored protein crystal structures to enzymatic function. ChemCatChem 5, 150-153 (2013).
    • (2013) ChemCatChem , vol.5 , pp. 150-153
    • Steffen-Munsberg, F.1
  • 17
    • 84871233538 scopus 로고    scopus 로고
    • Redesigning and characterizing the substrate specificity and activity of Vibrio fluvialis aminotransferase for the synthesis of imagabalin
    • Middelfort, K. S. et al. Redesigning and characterizing the substrate specificity and activity of Vibrio fluvialis aminotransferase for the synthesis of imagabalin. Protein Eng. Des. Sel. 26, 25-33 (2013).
    • (2013) Protein Eng. Des. Sel. , vol.26 , pp. 25-33
    • Middelfort, K.S.1
  • 18
    • 34547534084 scopus 로고    scopus 로고
    • Substrate spectrum of σ-transaminase from Chromobacterium violaceum DSM30191 and its potential for biocatalysis
    • Kaulmann, U., Smithies, K., Smith, M. E. B., Hailes, H. C. & Ward, J.M. Substrate spectrum of σ-transaminase from Chromobacterium violaceum DSM30191 and its potential for biocatalysis. Enzyme Microb. Technol. 41, 628-637 (2007).
    • (2007) Enzyme Microb. Technol. , vol.41 , pp. 628-637
    • Kaulmann, U.1    Smithies, K.2    Smith, M.E.B.3    Hailes, H.C.4    Ward, J.M.5
  • 19
    • 84863611002 scopus 로고    scopus 로고
    • Chromobacterium violaceum σ-transaminase variant Trp60Cys shows increased specificity for (S)-1-phenylethylamine and 4′-substituted acetophenones, and follows Swain-Lupton parameterisation
    • Cassimjee, K. E., Humble, M. S., Land, H., Abedi, V. & Berglund, P. Chromobacterium violaceum σ-transaminase variant Trp60Cys shows increased specificity for (S)-1-phenylethylamine and 4′-substituted acetophenones, and follows Swain-Lupton parameterisation. Org. Biomol. Chem. 10, 5466-5470 (2012).
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 5466-5470
    • Cassimjee, K.E.1    Humble, M.S.2    Land, H.3    Abedi, V.4    Berglund, P.5
  • 20
    • 84871644215 scopus 로고    scopus 로고
    • Revealing the structural basis of promiscuous amine transaminase activity
    • Steffen-Munsberg, F. et al. Revealing the structural basis of promiscuous amine transaminase activity. ChemCatChem 5, 154-157 (2013).
    • (2013) ChemCatChem , vol.5 , pp. 154-157
    • Steffen-Munsberg, F.1
  • 21
    • 84938326065 scopus 로고    scopus 로고
    • A quantum chemical study of the σ-transaminase reaction mechanism
    • Cassimjee, K. E., Manta, B. & Himo, F. A quantum chemical study of the σ-transaminase reaction mechanism. Org. Biomol. Chem. 13, 8453-8464 (2015).
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 8453-8464
    • Cassimjee, K.E.1    Manta, B.2    Himo, F.3
  • 22
    • 84928499388 scopus 로고    scopus 로고
    • The role of proline substitutions within flexible regions on thermostability of luciferase
    • Yu, H., Zhao, Y., Guo, C., Gan, Y. & Huang, H. The role of proline substitutions within flexible regions on thermostability of luciferase. Biochim. Biophys. Acta Prot. Proteomics 1854, 65-72 (2015).
    • (2015) Biochim. Biophys. Acta Prot. Proteomics , vol.1854 , pp. 65-72
    • Yu, H.1    Zhao, Y.2    Guo, C.3    Gan, Y.4    Huang, H.5
  • 23
    • 84934286966 scopus 로고    scopus 로고
    • Single active-sitemutants are sufficient to enhance serine:pyruvate α-transaminase activity in an σ-transaminase
    • Deszcz, D. et al. Single active-sitemutants are sufficient to enhance serine:pyruvate α-transaminase activity in an σ-transaminase. FEBS J. 282, 2512-2526 (2015).
    • (2015) FEBS J. , vol.282 , pp. 2512-2526
    • Deszcz, D.1
  • 24
    • 84862503319 scopus 로고    scopus 로고
    • The M5nr: A novel non-redundant database containing protein sequences and annotations from multiple sources and associated tools
    • Wilke, A. et al. The M5nr: a novel non-redundant database containing protein sequences and annotations from multiple sources and associated tools. BMC Bioinformatics 13, 141 (2012).
    • (2012) BMC Bioinformatics , vol.13 , pp. 141
    • Wilke, A.1
  • 25
    • 70349832423 scopus 로고    scopus 로고
    • Following evolutionary paths to protein-protein interactions with high affinity and selectivity
    • Levin, K. B. et al. Following evolutionary paths to protein-protein interactions with high affinity and selectivity. Nature Struct. Mol. Biol. 16, 1049-1055 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 1049-1055
    • Levin, K.B.1
  • 26
    • 84940063518 scopus 로고    scopus 로고
    • Handicap-recover evolution leads to a chemically versatile, nucleophile-permissive protease
    • Shafee, T., Gatti-Lafranconi, P., Minter, R. & Hollfelder, F. Handicap-recover evolution leads to a chemically versatile, nucleophile-permissive protease. ChemBioChem 16, 1866-1869 (2015).
    • (2015) ChemBioChem , vol.16 , pp. 1866-1869
    • Shafee, T.1    Gatti-Lafranconi, P.2    Minter, R.3    Hollfelder, F.4
  • 27
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin, N. V., Phillips, M. A. & Goldsmith, E. J. Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci. 4, 1291-1304 (1995).
    • (1995) Protein Sci. , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 28
    • 70349630445 scopus 로고    scopus 로고
    • Rapid and sensitive kinetic assay for characterization of σ-transaminases
    • Schätzle, S., Höhne, M., Redestad, E., Robins, K. & Bornscheuer, U. T. Rapid and sensitive kinetic assay for characterization of σ-transaminases. Anal. Chem. 81, 8244-8248 (2009).
    • (2009) Anal. Chem. , vol.81 , pp. 8244-8248
    • Schätzle, S.1    Höhne, M.2    Redestad, E.3    Robins, K.4    Bornscheuer, U.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.