Publikationer av Per-Olof Syrén

Refereegranskade

Artiklar

[1]

B. A. Nebel et al., "A Career in Catalysis : Bernhard Hauer," ACS Catalysis, vol. 13, no. 13, s. 8861-8889, 2023.

[2]

D. A. Hueting et al., "Design, structure and plasma binding of ancestral Î²-CoV scaffold antigens," Nature Communications, vol. 14, no. 1, 2023.

[3]

S. Subramaniyan et al., "Designed for Circularity : Chemically Recyclable and Enzymatically Degradable Biorenewable Schiff Base Polyester-Imines," ACS Sustainable Chemistry and Engineering, vol. 11, no. 8, s. 3451-3465, 2023.

[4]

B. Guo et al., "Fast Depolymerization of PET Bottle Mediated by Microwave Pre-Treatment and An Engineered PETase," ChemSusChem, vol. 16, no. 18, 2023.

[5]

E. Sporre et al., "Metabolite interactions in the bacterial Calvin cycle and implications for flux regulation," Communications Biology, vol. 6, no. 1, 2023.

[6]

A. Biundo et al., "Regio- and stereoselective biocatalytic hydration of fatty acids from waste cooking oils en route to hydroxy fatty acids and bio-based polyesters," Enzyme and microbial technology, vol. 163, 2023.

[7]

X. Lopez-Lorenzo et al., "Whole-cell Mediated Carboxylation of 2-Furoic Acid Towards the Production of Renewable Platform Chemicals and Biomaterials," ChemCatChem, vol. 15, no. 6, 2023.

[8]

B. Guo et al., "Conformational Selection in Biocatalytic Plastic Degradation by PETase," ACS Catalysis, vol. 12, no. 6, s. 3397-3409, 2022.

[9]

D. A. Hueting, S. R. Vanga och P.-O. Syrén, "Thermoadaptation in an Ancestral Diterpene Cyclase by Altered Loop Stability," Journal of Physical Chemistry B, vol. 126, no. 21, s. 3809-3821, 2022.

[10]

N. Hendrikse et al., "Ancestral lysosomal enzymes with increased activity harbor therapeutic potential for treatment of Hunter syndrome," ISCIENCE, vol. 24, no. 3, 2021.

[11]

A. Hunold et al., "Assembly of a Rieske non-heme iron oxygenase multicomponent system from Phenylobacterium immobile E DSM 1986 enables pyrazon cis-dihydroxylation in E. coli," Applied Microbiology and Biotechnology, vol. 105, no. 5, s. 2003-2015, 2021.

[12]

C. Jönsson et al., "Biocatalysis in the Recycling Landscape for Synthetic Polymers and Plastics towards Circular Textiles," ChemSusChem, vol. 14, no. 19, s. 4028-4040, 2021.

[13]

K. Schriever et al., "Engineering of Ancestors as a Tool to Elucidate Structure, Mechanism, and Specificity of Extant Terpene Cyclase," Journal of the American Chemical Society, vol. 143, no. 10, s. 3794-3807, 2021.

[14]

A. E. Alexakis et al., "Modification of cellulose through physisorption of cationic bio-based nanolatexes - comparing emulsion polymerization and RAFT-mediated polymerization-induced self-assembly," Green Chemistry, vol. 23, no. 5, s. 2113-2122, 2021.

[15]

A. Stamm et al., "Pinene-Based Oxidative Synthetic Toolbox for Scalable Polyester Synthesis," JACS Au, vol. 1, no. 11, s. 1949-1960, 2021.

[16]

S. Zokaei et al., "Toughening of a Soft Polar Polythiophene through Copolymerization with Hard Urethane Segments," Advanced Science, vol. 8, no. 2, 2021.

[17]

N. M. Hendrikse et al., "Exploring the therapeutic potential of modern and ancestral phenylalanine/tyrosine ammonia-lyases as supplementary treatment of hereditary tyrosinemia," Scientific Reports, vol. 10, no. 1, 2020.

[18]

W. Farhat et al., "Lactone monomers obtained by enzyme catalysis and their use in reversible thermoresponsive networks," Journal of Applied Polymer Science, vol. 137, no. 18, 2020.

[19]

A. Stamm et al., "A retrobiosynthesis-based route to generate pinene-derived polyesters," ChemBioChem, vol. 20, s. 1664-1671, 2019.

[20]

W. Farhat et al., "Biocatalysis for terpene-based polymers," Zeitschrift für Naturforschung C - A Journal of Biosciences, vol. 74, no. 3-4, s. 90-99, 2019.

[21]

A. Stamm et al., "Chemo- enzymatic pathways toward pinene- based renewable materials," Green Chemistry, vol. 21, no. 10, s. 2720-2731, 2019.

[22]

A. Biundo et al., "Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering," RSC Advances, vol. 9, no. 62, s. 36217-36226, 2019.

[23]

N. Hendrikse et al., "Ancestral diterpene cyclases show increased thermostability and substrate acceptance," The FEBS Journal, vol. 285, no. 24, s. 4660-4673, 2018.

[24]

P.-O. Syrén, "Enzymatic Hydrolysis of Tertiary Amide Bonds by anti Nucleophilic Attack and Protonation," Journal of Organic Chemistry, vol. 83, no. 21, s. 13543-13548, 2018.

[25]

C. Gustafsson et al., "MD Simulations Reveal Complex Water Paths in Squalene–Hopene Cyclase: Tunnel-Obstructing Mutations Increase the Flow of Water in the Active Site," ACS Omega, vol. 2, no. 11, s. 8495-8506, 2017.

[26]

A. Eriksson, C. Kürten och P.-O. Syrén, "Protonation-Initiated Cyclization by a ClassII Terpene Cyclase Assisted by Tunneling," ChemBioChem, vol. 18, no. 23, s. 2301-2305, 2017.

[27]

N. M. Hendrikse et al., "Redesign of biosynthetic enzymes using ancestral sequence reconstruction," The FEBS Journal, vol. 284, s. 86-87, 2017.

[28]

M. J. Fink och P.-O. Syrén, "Redesign of water networks for efficient biocatalysis," Current opinion in chemical biology, vol. 37, s. 107-114, 2017.

[29]

J. Fagerland et al., "Template-assisted enzymatic synthesis of oligopeptides from a polylactide chain," Biomacromolecules, vol. 18, no. 12, s. 4271-4280, 2017.

[30]

C. Kürten, B. Carlberg och P.-O. Syren, "Mechanism-Guided Discovery of an Esterase Scaffold with Promiscuous Amidase Activity," Catalysts, vol. 6, no. 6, 2016.

[31]

P.-O. Syrén et al., "Squalene-hopene cyclases : evolution, dynamics and catalytic scope," Current opinion in structural biology, vol. 41, s. 73-82, 2016.

[32]

S. Hammer, P.-O. Syrén och B. Hauer, "Substrate Pre-Folding and Water Molecule Organization Matters for Terpene Cyclase Catalyzed Conversion of Unnatural Substrates," ChemistrySelect, vol. 1, s. 3589-3593, 2016.

[33]

C. Kürten och P.-O. Syren, "Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes," Journal of Visualized Experiments, no. 107, 2016.

[34]

P. Hendil-Forssell, M. Martinelle och P.-O. Syren, "Exploring water as building bricks in enzyme engineering," Chemical Communications, vol. 51, no. 97, s. 17221-17224, 2015.

[35]

C. Kürten, M. Uhlén och P.-O. Syrén, "Overexpression of functional human oxidosqualene cyclase in Escherichia coli," Protein Expression and Purification, vol. 115, s. 46-53, 2015.

[36]

P.-O. Syrén et al., "Entropy is Key to the Formation of Pentacyclic Terpenoids by Enzyme-Catalyzed Polycyclization," Angewandte Chemie International Edition, vol. 53, no. 19, s. 4845-4849, 2014.

[37]

P.-O. Syrén et al., "Proton Shuttle Mechanism in the Transition State of Lipase-Catalyzed N-Acylation of Amino Alcohols," ChemCatChem, vol. 5, no. 7, s. 1842-1853, 2013.

[38]

S. C. Hammer et al., "Squalene hopene cyclases : highly promiscuous and evolvable catalysts for stereoselective CC and CX bond formation," Current opinion in chemical biology, vol. 17, no. 2, s. 293-300, 2013.

[39]

M. Seitz et al., "Synthesis of Heterocyclic Terpenoids by Promiscuous Squalene-Hopene Cyclases," ChemBioChem, vol. 14, no. Copyright (C) 2013 American Chemical Society (ACS). All Rights Reserved., s. 436-439, 2013.

[40]

P.-O. Syren, "The solution of nitrogen inversion in amidases," The FEBS Journal, vol. 280, no. 13, s. 3069-3083, 2013.

[41]

P.-O. Syrén et al., "Esterases with an Introduced Amidase-Like Hydrogen Bond in the Transition State Have Increased Amidase Specificity," ChemBioChem, vol. 13, no. 5, s. 645-648, 2012.

[42]

S. C. Hammer et al., "Stereoselective Friedel-Crafts alkylation catalyzed by squalene hopene cyclases," Tetrahedron, vol. 68, no. Copyright (C) 2013 American Chemical Society (ACS). All Rights Reserved., s. 7624-7629, 2012.

[43]

P.-O. Syrén och K. Hult, "Amidases have a hydrogen bond that facilitates nitrogen inversion but esterases have not," ChemCatChem, vol. 3, no. 5, s. 853-860, 2011.

[44]

K. Engström et al., "Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols," Organic and biomolecular chemistry, vol. 9, no. 1, s. 81-82, 2011.

[45]

P.-O. Syren et al., "Increased activity of enzymatic transacylation of acrylates through rational design of lipases," Journal of Molecular Catalysis B : Enzymatic, vol. 65, no. 1-4, s. 3-10, 2010.

[46]

M. Vallin, P.-O. Syrén och K. Hult, "Mutant Lipase-Catalyzed Kinetic Resolution of Bulky Phenyl Alkyl sec-Alcohols : A Thermodynamic Analysis of Enantioselectivity," ChemBioChem, vol. 11, no. 3, s. 411-416, 2010.

[47]

Z. Marton et al., "Mutations in the stereospecificity pocket and at the entrance of the active site of Candida antarctica lipase B enhancing enzyme enantioselectivity," Journal of Molecular Catalysis B : Enzymatic, vol. 65, no. 1-4, s. 11-17, 2010.

[48]

P.-O. Syrén och K. Hult, "Substrate Conformations Set the Rate of Enzymatic Acrylation by Lipases," ChemBioChem, vol. 11, no. 6, s. 802-810, 2010.

[49]

P.-O. Syren et al., "Milligram scale parallel purification of plasmid DNA using anion-exchange membrane capsules and a multi-channel peristaltic pump," Journal of chromatography. B, vol. 856, s. 68-74, 2007.

Kapitel i böcker

[50]

I. V. Pavlidis, N. Hendrikse och P.-O. Syrén, "Computational Techniques for Efficient Biocatalysis," i Modern Biocatalysis : Advances Towards Synthetic Biological Systems, Gavin Williams, Mélanie Hall red., : Royal Society of Chemistry, 2018, s. 119-152.

[51]

P.-O. Syrén, "Understanding esterase and amidase reaction specificities by molecular modelling," i Understanding enzymes; Function, Design, Engineering and Analysis, : Pan Standford Publishing, 2016, s. 523.

Icke refereegranskade

Artiklar

[52]

F. Cadet et al., "Editorial : Machine learning, epistasis, and protein engineering: From sequence-structure-function relationships to regulation of metabolic pathways," Frontiers in Molecular Biosciences, vol. 9, 2022.

[53]

W. Farhat et al., "Enzymatic route for the synthesis of norcamphor lactone and its polymerization for applications as thermo-sensitive networks," Abstracts of Papers of the American Chemical Society, vol. 258, 2019.

[54]

L. Fogelström et al., "New chemo-enzymatic pathways for sustainable terpene-based polymeric materials," Abstracts of Papers of the American Chemical Society, vol. 257, 2019.

[55]

E. Malmström et al., "Sustainable terpene-based polymeric materials," Abstracts of Papers of the American Chemical Society, vol. 257, 2019.

[56]

A. Biundo et al., "Increasing amide acceptance on a polyester-hydrolyzing enzyme," New Biotechnology, vol. 33, s. S105-S105, 2016.

[57]

P.-O. Syrén och K. Hult, "Least-motion mechanism in enzyme catalysis," The FEBS Journal, vol. 277, s. 263-263, 2010.

Kapitel i böcker

[58]

P.-O. Syrén, "Understanding esterase and amidase reaction specificities by molecular modeling," i Understanding Enzymes: Function, Design, Engineering and Analysis, : Pan Stanford Publishing, 2016, s. 523-558.