Chemistry for Life Sciences by Protein Engineering of Enzymes

Publications

jacsat_v143i010J Appl Polym Sci 2020Publication1

joceah_v083i021-4

chembiochem cover

     

       2022

  1. A. Hueting, S. R. Vanga, P.-O. Syrén*. Thermoadaptation in an Ancestral Diterpene Cyclase by Altered Loop Stability. J. Phys. Chem. B. 2022, 126, 3809–3821. doi: 10.1021/acs.jpcb.1c10605Microsoft Word - jp1c10605

  2. B. Guo, S. Reddy Vanga, P. Saenz-Mendez, X. Lopez-Lorenzo, S. Rönnblad Ericsson, Y. Fang, X. Ye, K. Schriever, E. Bäckström, A. Biundo, R. A Zubarev, I. Furó, M. Hakkarainen, P.-O. Syrén*. Conformational selection in biocatalytic plastic degradation by PETase. ACS Catal. 2022, 12, 3397–3409. doi:10.1021/acscatal.1c05548images_large_cs1c05548_0008

    2021

  3. A. Stamm, J. Öhlin, C. Mosbech, P. Olsén, B. Guo, E. Söderberg, A. Biundo, L. Fogelström, S. Bhattacharyya, U. T. Bornscheuer, E. Malmström, P.-O. Syrén*. Pinene-based oxidative synthetic toolbox for scalable polyester synthesis. JACS Au 2021, 11, 1949–1960. doi: 10.1021/jacsau.1c00312dTOC_updated
  4. K. Schriever, P. Saenz-Mendez, R. Srilakshmi Rudraraju, N. M. Hendrikse, E. P. Hudson, A. Biundo, R. Schnell, P.-O. Syrén*. Engineering of Ancestor as a Tool To Elucidate Structure, Mechanism and Specificity of Extant Terpene Cyclase. J. Am. Chem. Soc. 2021,  143, 3794–3807. doi: 10.1021/jacs.0c10214schriever et al 2021 jacs toc
  5. C. Jönsson, R. Wei, A. Biundo, J. Landberg, L. Schwarz Bour, F. Pezzotti, A. Toca, L. M. Jacques, U. T. Bornscheuer, P.-O. Syrén*. Biocatalysis in the recycling landscape for synthetic polymers and plastics towards circular textiles. ChemSusChem 2021, 14, 4028–4040. https://doi.org/10.1002/cssc.202002666Biocatalysis plastic textiles TOC
  6. A. E. Alexakis, J. Engström, A. Stamm, A. V. Riazanova, C. J. Brett, S. V. Roth, P-O Syrén, L. Fogelström, M. S. Reid, E. Malmström. Modification of cellulose through physisorption of cationic bio-based nanolatexes – Comparing emulsion polymerization and RAFT-mediated polymerization-induced self-assembly. Green Chem. 2021,23, 2113.
  7. N. M. Hendrikse, A. Sandegren, T. Andersson, J. Blomqvist, Å. Makower, D. Possner, C. Su, N. Thalén, A. Tjernberg, U. Westermark, J. Rockberg, S. Svensson Gelius, P.-O. Syrén*, E. Nordling. Ancestral lysosomal enzymes with increased activity harbor therapeutic potential for treatment of Hunter syndrome. iScience 2021, 24, 102154. https://doi.org/10.1016/j.isci.2021.102154Ancestral lysosomal enzyme TOC
  8. A. Hunold, W. Escobedo-Hinojosa, E. Potoudis, D. Resende, T. Farr, P.-O. Syrén, B. Hauer. Assembly of a Rieske non-heme iron oxygenase multicomponent system from Phenylobacterium immobile E DSM 1986 enables pyrazon cis-dihydroxylation in E. coli. Appl. Microbiol. Biotechnol. 2021, 105, 2003–2015.

    2020

  9. S. Zokaei, R. Kroon, J. Gladisch, B. Paulsen, A. I. Hofmann, G. Persson, A. Stamm, P.-O. Syrén, E. Olsson, J. Rivnay, E. Stavrinidou, A. Lund, C. Müller. Toughening of a Soft Polar Polythiophene through Copolymerization with Hard Urethane Segments. Adv. Sci. 2020, 2002778.
  10. I Biundo, A. Stamm, U. T. Bornscheuer, P.-O. Syrén*, Enzymatic synthesis of pinene-derived lactones. Applied Biocatalysis: The Chemist’s Enzyme Toolbox. 2020, pp 319-326. (First Edition, John Wiley & Sons Ltd).
  11. N. Hendrikse, A. Holmberg Larsson, S. Svensson Gelius, S. Kuprin, E. Nordling, Per-Olof Syrén*. Ancestral phenylalanine/tyrosine ammonia-lyases have potential for supplementary treatment to Nitisinone of hereditary tyrosinemia. Sci. Rep. 2020, 10, 1315.TOC Ancestral ammonia lyases

  12. W. Farhat, A. Biundo, A. Stamm, E. Malmström, P.-O. Syrén*. Lactone monomers obtained by enzyme catalysis and their use in reversible thermoresponsive networks. J. Appl. Polym. Sci. 2020, 137, 48949.TOC manuscript 32

    2019

  13. Biundo, R. Subagia, M. Maurer, D. Ribitsch, P.-O. Syrén*, G. M. Guebitz. Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering. RSC Adv. 2019, 9, 36217-36226.Water design Figure 2C
  14. Special issue on emerging future research leaders: Stamm, A. Biundo, B. Schmidt, J. Brücher, S. Lundmark, P. Olsén, L. Fogelström, E. Malmström, U. T. Bornscheuer,    P.-O. Syrén* A retrobiosynthesis-based route to generate pinene-derived polyesters. ChemBioChem 2019, 20, 1664-1671.Stamm et al 2019 TOC
  15. Special issue on Chemo-enzymatic cascade reactions: Farhat, A. Stamm, M. Robert-Monpate, A. Biundo, P.-O. Syrén*. Biocatalysis for terpene-based polymers. Z. Naturforsch. C. 2019, 74, 91–100.TOC Farhat et al 2019

  16. A. Stamm, M. Tengdelius, B. Schmidt, J. Engström, P. O. Syrén, L. Fogelström, E. Malmström. Chemo-enzymatic pathways toward pinene-based renewable materials. Green Chem. 2019, 21, 2720–2731.TOC Stamm et al Green Chem 2019

    2018

  17. M. Hendrikse, G. Charpentier, E. Nordling, P.-O. Syrén*, Ancestral diterpene cyclases show increased thermostability and substrate acceptance. FEBS J 2018, 285 4660–4673.Hendrikse et al 2018 TOC

  18. Elected among the top 25 papers in JOC during 2018

    Featured on the cover of J. Org. Chem:

    P.-O. Syrén*, Enzymatic hydrolysis of tertiary amide bonds by anti nucleophilic attack and protonation. J. Org. Chem. 2018, 83, 13543–13548.TOC Syrén 2018

    2016-2017

  19. A. Eriksson, C. Kürten, P.-O. Syrén*, Protonation-initiated cyclization by a class II terpene cyclase assisted by tunneling. ChemBioChem 2017, 18, 2301-2305.
  20. A. Eriksson, C. Kürten, P.-O. Syrén*, Cover Feature: Protonation-initiated cyclization by a class II terpene cyclase assisted by tunneling. ChemBioChem 2017, 18, 2293.
  21. J. Fagerland, D. Pappalardo, B. Schmidt, P.-O. Syrén, A. F. Wistrand, Template assisted enzymatic synthesis of oligopeptides from a polylactide chain. Biomacromolecules, 2017, 18, 4271−4280.
  22. C. Gustafsson, S. Vassiliev, C. Kürten, P.-O. Syrén, T. Brinck. MD Simulations Reveal Complex Water Paths in Squalene–Hopene Cyclase: Tunnel-Obstructing Mutations Increase the Flow of Water in the Active Site. ACS Omega 2017, 2, 8495−8506.
  23. M. J. Fink, P.-O. Syrén*, Redesign of water networks for efficient biocatalysis. Curr. Opin. Chem. Biol. 2017, 37, 107-114.
  24. S. C. Hammer, P.-O. Syrén#, B. Hauer. Substrate Pre-Folding and Water Molecule Organization Matters for Terpene Cyclase Catalyzed Conversion of Unnatural Substrates. ChemistrySelect, 2016, 1, 3589–3593.
  25. P.-O. Syrén, S. Henche, A. Eichler, B. Nestl, B. Hauer. Squalene-hopene cyclases – evolution, dynamics and catalytic scope. Curr. Opin. Struct. Biol. 2016, 41, 73-82.
  26. Special issue: Enzyme catalysis: C. Kürten, B. Carlberg, P.-O. Syrén*. Mechanism-guided discovery of an esterase scaffold with promiscuous amidase activity. Catalysts, 2016, 6, 90.
  27. C. Kürten, P.-O. Syrén*. Unraveling entropic rate acceleration induced by solvent dynamics in membrane enzymes. J. Vis. Exp. 2016, 107, e53168, doi:10.3791/53168.

    Publications before 2016

  28. C. Kürten, M. Uhlén, P.-O. Syrén*. Overexpression of functional human oxidosqualene cyclase in Escherichia coli. Protein Express Purif, 2015, 115, 46-53.
  29. Featured on the cover of Chemical Communications: P. Hendil-Forssell, M. Martinell, P.-O. Syrén*. Exploring water as building bricks in enzyme engineering. Chem. Commun. 2015, 51, 17221-17224.
  30. P.-O. Syrén*, S.C. Hammer, B. Claasen, B. Hauer. Entropy is Key to the Formation of Pentacyclic Terpenoids by Enzyme-Catalyzed Polycyclization. Angew. Chem. Int. Ed. 2014, 126, 4945-4949.
  31. P.-O. Syrén*, The solution to nitrogen inversion in amidases. FEBS J 2013, 280, 3069-3083.
  32. M. Seitz, P.-O. Syrén, L. Steiner, J. Klebensberger, B. Nestl, B. Hauer, Synthesis of heterocyclic terpenoids by promiscuous squalene-hopene cyclases. ChemBioChem 2013, 14, 436-439.
  33. S. C. Hammer#, P.-O. Syrén#, M. Seitz, B. Nestl, B. Hauer, Squalene hopene cyclases: highly promiscuous and evolvable catalysts for stereoselective C-C and C-X bond formation. Curr. Opin. Chem. Biol. 2013, 17, 293-300.
  34. P.-O. Syrén*, F. Le Joubioux, Y. Ben Henda, T. Maugard, K. Hult, M. Graber, Proton shuttle mechanism in the transition state of lipase catalyzed N-acylation of amino alcohols. ChemCatChem 2013, 5, 1842-1853.
  35. S. C. Hammer, J. Dominicus, P.-O. Syrén, B. Nestl, B. Hauer, Stereoselective Friedel–Crafts alkylation catalyzed by squalene hopene cyclases. Tetrahedron, 2012, 68, 7624-7629.
  36. P.-O. Syrén, P. Hendil-Forssell, L. Aumailley, W. Besenmatter, F. Gounine, A. Svendsen, M. Martinelle, K. Hult, Esterases with an introduced amidase-like hydrogen bond in transition state display increased amidase specificity. ChemBioChem 2012, 13, 645–648.
  37. P.-O. Syrén, K. Hult, Amidases have a hydrogen bond that facilitates nitrogen inversion but esterases have not. ChemCatChem 2011, 3, 853-860.
  38. K. Engström, M. Vallin, P.-O. Syrén, K. Hult, J.-E. Bäckvall, Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols. Org. Biomol. Chem. 2011, 9, 81-82.
  39. P.-O. Syrén, K. Hult, Substrate Conformations Set the Rate of Enzymatic Acrylation by Lipases. ChemBioChem 2010, 11, 802 – 810.
  40. S. Marton, V. Léonard-Nevers, P.-O. Syrén, C. Bauer, S. Lamare, K. Hult, V. Tranc, M. Graber, Mutations in the stereospecificity pocket and at the entrance of the active site of Candida antarctica lipase B enhancing enzyme enantioselectivity. J. Mol. Catal. B: Enzym. 2010, 65, 11-17.
  41. P.-O. Syrén, E. Lindgren, H. W. Hoeffken, C. Branneby, S. Maurer, B. Hauer, K. Hult, Increased activity of enzymatic transacylation of acrylates through rational design of lipases. J. Mol. Catal. B: Enzym. 2010, 65, 3-10.
  42. M. Vallin, P.-O. Syrén, K. Hult, Mutant Lipase-Catalyzed Kinetic Resolution of Bulky Phenyl Alkyl sec-Alcohols: A Thermodynamic Analysis of Enantioselectivity. ChemBioChem 2010, 11, 411-416.
  43. P.-O. Syrén, A. Rozkov, S. R. Schmidt, P. Strömberg, Milligram scale parallel purification of plasmid DNA using anion-exchange membrane capsules and a multi-channel peristaltic pump. J. Chromatogr. B 2007, 856, 68-74.
  44. I. V. Pavlidis, N.M. Hendrikse, P.-O. Syrén*, Computational Techniques for Efficient Biocatalysis. Modern Biocatalysis: Advances Towards Synthetic Biological Systems. 2018, 5, 119-152 (Royal Society of Chemistry).
  45. P.-O. Syrén*, Understanding esterase and amidase reaction specificities by molecular modelling. Understanding enzymes; Function, Design, Engineering and Analysis. 2016, 15, 523-558 (PanStandford Publishing).

 

 

Life is easy to identify, but remarkably hard to define. One fundamental property of living organisms is the order they create in their environment through evolved metabolic pathways, organized structures and self-replication which are basal energy-consuming processes dependent on enzymes that accelerate the chemistry of life up to 10^26-fold. Fundamental and organizational tasks, for instance energy conversion and information processing, would take millions – or even billions – of years in the absence of enzymes, thus representing timescales that would be incompatible with life.

The Syrén lab works with computer simulations and bioinformatics, as well as experimental biotechnology and protein engineering to enhance our fundamental understanding of enzymes, their mechanisms and evolution at the atomistic level. Towards reaching this goal we bridge fundamental chemical principles with state-of-the art biotechnology. Through transdisciplinary scientific methods we are developing novel enzyme engineering strategies for applications within biopolymer science and for the generation of superior biopharmaceuticals and fine chemicals from renewable sources.

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