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Over onsWaar vindt u onsprof. dr. G.J. (Gerrit) Poelarends

prof. dr. G.J. Poelarends

Hoogleraar Farmaceutische Biotechnologie

 

Personal Details
 

Name & titels         Prof. dr. Gerrit Jan Poelarends

Date of birth           January 8, 1971, Ommen, The Netherlands

Citizenship             Dutch (The Netherlands)

Marital status         Married, 3 children

Private address      Rembrandtstraat 80, 7731 SG Ommen, The Netherlands,

                               Tel: +31-(0)529-454117

Office address       Antonius Deusinglaan 1, 9713 AV Groningen,

                               The Netherlands,

                               Tel: +31-(0)50-3633354, Fax: +31-(0)50-3633000,

                               E-mail: g.j.poelarends@rug.nl , website: www.farmbio.nl

Education
 

1989   Atheneum, Jan van Arkel, Hardenberg, NL

1994   M.Sc., Biology-Biochemistry, University of Groningen, NL

2001   Ph.D., Dept. of Biochemistry, University of Groningen, NL

 
Postdoctoral Training
 

Jan 2000 – Feb 2002      Dept. of Microbiology, University of Groningen, NL

March 2002 – Oct 2004  Div. of Medicinal Chemistry, University of Texas at Austin, TX, USA

Nov 2004 – Sept 2006    Dept. of Biochemistry, University of Groningen, NL

 
Academic Appointments
 

Oct 2006 – June 2012     Assistant Professor, Dept. of Pharmaceutical Biology, University of Groningen, NL

July 2012 – present         Associate Professor, Dept. of Pharmaceutical Biology, University of Groningen, NL

 
International Activities
 
  • 2.5 years in the Div. of Medicinal Chemistry, Univ. of Texas at Austin, TX, USA
  • Attended >20 international scientific meetings (1994-2012)
  • Several international collaborations (Dr. Strauss, Dr. Whitman)
  • EU research support, with international collaborations (2008, 2015)

 

Other Academic Activities
 
  • Teaching Cell Biology and Biochemistry for students Pharmacy (~150 students/yr)
  • Coordination and teaching of course Organic and Biosynthesis (~150 students/yr)
  • Coordination and teaching of course Pharmaceutical Biotechnology (~10 students/yr)
  • Supervision of Bachelor and Master students with their research projects
  • Supervision of Graduate students: (co)-promotor of several ongoing projects
  • Management – group leader of Pharmaceutical Biotechnology group
  • Member of the exam committee of Pharmacy
  • Ad hoc journal reviewer for several journals
  • Opponent of several Ph.D. theses at the University of Groningen

 

Memberships
 
  • American Chemical Society
  • Dutch Biotechnological Society
  • Study group Protein Research of NWO-CW
  • Study group Biomolecular Chemistry of NWO-CW

 

Grants and Awards
 
  • Innovational research grant (personal VENI grant) from the Netherlands Organisation for Scientific Research (NWO). Titel of the grant: “Design and selection of biocatalysts for amination reactions”. Period covered: 01-11-2004 until 31-05-2007.

  • Innovational research grant (personal VIDI grant) from the Netherlands Organisation for Scientific Research (NWO). Title of the grant: “Exploiting catalytic promiscuity: the tautomerase superfamily active site as a scaffold for new biocatalysts”. Period covered: 01-06-2007 until 01-06-2012.

  • Collaborative Project grant from the European Union (EU-FP7-CP grant). Titel of the grant: “Metagenomics for bioexploration: Tools and application”. Period covered: 2009-2014. Investigators: Prof. Dr. J.D. van Elsas, and 17 other partners, including Prof. G.J. Poelarends.

  • Starting Independent Research Grant from the European Research Council (personal ERC-2009-Starting Grant). Titel of the grant: "Bridging between organocatalysis and biocatalysis: The powerful enamine mechanism of organocatalysts engineered into the tautomerase superfamily scaffold". Period covered: 01-05-2010 until 01-05-2015.

  • Honorary Scholarship’ from the University of Groningen, which was awarded to all candidates reaching the second (interview) round in the prestigious ERC-2009-Starting Grant competition.

  • ECHO project grant from the Netherlands Organisation for Scientific Research (NWO). Title of the grant: "Engineering of methylaspartate ammonia lyase for synthesis of unnatural amino acids". Period covered: 11-10-2010 until 11-10-2012.

  • ALW project grant from the Netherlands Organisation for Scientific Research (NWO). Title of the grant: "Importance of plasticity residues for natural and laboratory evolution of promiscuous protein functions". Period covered: 2011-2015. Investigators: Prof. Dr. W.J. Quax and Prof. Dr. G.J. Poelarends.

  • KIEM project grant from the Netherlands Organisation for Scientific research (NWO). Title of the grant: “Environmentally friendly synthesis of complex amino acids: Enzymatic synthesis of 3-aryl and 3-aryloxy substituted aspartic acid derivatives starting from readily available fumaric acids”. Period covered: 01-04-2014 until 01-10-2014.

  • Collaborative project grant from the European Union (H2020-LEIT-BIO-2014-1). Titel of the grant: “Sustainable industrial processes based on a C-C bond-forming enzyme platform”. Period covered: 01-04-2015 until 31-03-2019. Investigators: Prof. Dr. G.J. Poelarends, and 13 other partners.

  • KIEM project grant from the Netherlands Organisation for Scientific research (NWO). Title of the grant: “Efficient synthesis of selective inhibitors of glutamate transporters”. Period covered: 16-06-2016 until 16-12-2016.

  • ECHO project grant from the Netherlands Organisation for Scientific Research (NWO). Title of the grant: "Exploiting enzyme promiscuity for biocatalysis: Engineering novel ‘Michaelases’ for carbon-carbon bond formation". Period covered: 01-07-2016 until 01-07-2020.

  • Proof of Concept grant from the European Research Council (personal ERC-2015-PoC). Acronym of the grant: "SynBioGABA". Period covered: 01-07-2016 until 01-10-2017.

  • International training networks grant from the European Union (H2020-MSCA-ITN-2016). Title of the grant: "Harnessing the power of enzymatic oxygen activation". Period covered: 01-01-2017 until 01-01-2021. Investigators: Prof. Dr. G.J. Poelarends, and 10 other partners.
  • Cofund project grant from the European Union (H2020-MSCA-COFUND-2016). Title of the grant: "Personalised Medicine in Diabetic Chronic Disease Management". Period covered: 2017 until 2021. Investigators: Prof. Dr. G.J. Poelarends, and 15 other partners.
  • Innovational research grant (personal VICI grant) from the Netherlands Organisation for Scientific Research (NWO). Title of the grant: “Modular synthetic enzyme cascades for the production of pharmaceutically active γ-aminobutyric acids”. Period covered: 2017 until 2022.

 

Selection of research presentations
 
  • Probing Molecular Interactions and Mechanisms at the Chemistry/Biology Interface (Tällberg, Sweden, Nov 2016). Title of presentation: "Engineering enzymes to control substrate and catalytic promiscuity".

  • Gordon Research Conference on Biocatalysis (Biddeford, USA, July 2016). Title of presentation: "Exploiting catalytic promiscuity: Design of novel biocatalysts for carbon-carbon bond formation".

  • Netherlands' Catalysis and Chemistry Conference (Noordwijkerhout, The Netherlands, March 2016). Title of presentation: "Exploiting catalytic promiscuity: Design of novel biocatalysts for C-C bond formation".

  • European Symposium on Biological and Organic Chemistry - ESBOC (Gregynog, Wales, May 2015); Title of presentation: "Design of novel biocatalysts for carbon-carbon bond formation".

  • Transam 2.0 - Chiral Amines Through (Bio)Catalysis Conference (Greifswald, Germany, March 2015); Title of presentation: "Enzymatic Synthesis of Substituted Aspartic Acids".

  • Enzyme Mechanisms Conference (Galveston, TX-USA, January 2015); Title of presentation: "Design of proline-based biocatalysts for C-C bond formation: From catalytic promiscuity to protein mutability landscapes".

  • International Congress on Biocatalysis (Hamburg, Germany, September 2014); Title of presentation: ”Discovery and engineering of new enzymes for carbon-nitrogen bond formation".

  • Texas Enzyme Mechanisms Conference (Austin, TX-USA, January 2014); Title of presentation: "Exploiting catalytic promiscuity: Design of proline-based biocatalysts for C-C bond formation".

  • Biotrans (Manchester, UK, July 2013); Title of presentation: "Exploiting catalytic promiscuity: Design of new biocatalysts for carbon-carbon bond formation".

  • International Congress on Biocatalysis (Hamburg, Germany, September 2012); Title of presentation: “New promiscuous C-C bond-forming activities of 4-oxalocrotonate tautomerase ”.

  • Protein engineering conference (Greifswald, Germany, August 2012); Title of presentation: "Engineering ammonia lyases for asymmetric synthesis of amino acids".

  • Biotrans (Berne, Switzerland, July 2009); Title of presentation: "4-Oxalocrotonate Tautomerase: A Small Promiscuous Template for Natural and Laboratory Evolution of New Enzymes".

  • Enzyme Engineering XIX conference (Harrison Hot Springs, BC, Canada, September 2007); Title of presentation: “Catalytic promiscuity and the divergence of enzyme activity in the tautomerase superfamily”.

  • International Congress on Biocatalysis (Hamburg, Germany, September 2006); Title of presentation: “ The Impact of Catalytic Promiscuity on the Evolution of Enzymes”.

  • International Network of Protein Engineering Centers (Elsinore, Denmark, June 2006); Title of presentation: “Exploiting catalytic promiscuity: the tautomerase superfamily active site as a scaffold for new biocatalysts”.

  • Gordon Research Conference on Enzymes, Coenzymes, and Metabolic Pathways (Meriden, NH, USA, July 2003); Title of presentation: “New reactions in the tautomerase superfamily: malonate semialdehyde decarboxylase and cis- and trans-3-chloroacrylic acid dehalogenase”.

  • European Congress on Biotechnology (Brussels, Belgium, June 1999); Title of presentation: “Novel mechanisms of carbon halogen bond cleavage in haloaliphatic compounds”. 

 

Research profile/Track-Record
 

Gerrit J. Poelarends received his PhD degree from the University of Groningen (RUG) in 2001 with Professor Dick B. Janssen. At the RUG, he worked on the isolation and characterization of the first pure bacterial cultures capable of utilizing 1,3-dichloropropene and 1,2-dibromoethane, two important environmental pollutants, as sole sources of carbon and energy (see Poelarends et al., 1998, Appl. Environ. Microbiol. 64:2931-2936; Poelarends et al., 1999, J. Bacteriol. 181:2050-2058). This work would later pique the interests of others, and expand our understanding of the evolution and distribution of xenobiotic degrading activities (see Poelarends et al., 2000, J. Bacteriol. 182: 2191-2199; Poelarends et al., 2000, J. Bacteriol. 182:2725-2731; Poelarends et al., 2001, J. Bacteriol. 183: 4269-4277).

He then worked as a postdoctoral fellow with Professors Wil N. Konings and Arnold J.M. Driessen at the RUG, where he tackled mechanistic questions on bacterial multidrug efflux systems. This work provided evidence for the broad substrate specificity and the aqueous nature of the solute translocation path in ATP-driven multidrug transporters and the important role of acidic residues in proton translocation by secondary multidrug efflux systems (see Mazurkiewicz et al., 2002, J. Biol. Chem. 277:26081-26088; Poelarends et al., 2002, J. Biol. Chem. 277:42891-42898; Mazurkiewicz et al., 2004, J. Biol. Chem. 279:103-108). [For overviews of this work, see Poelarends et al., 2000, Drug Resist. Updat. 3:330-334; Konings and Poelarends, 2002, IUBMB Life 53:213-218; Poelarends et al., 2002, Biochim. Biophys. Acta. 1555:1-7.]

Subsequently, he worked as a postdoctoral fellow with Professor Christian P. Whitman at the University of Texas at Austin (USA), where he tackled mechanistic and evolutionary questions about the enzymes comprising the tautomerase superfamily. From this period, he has numerous publications on enzymes and the structural factors that dictate activity (see Poelarends et al., 2003, J. Biol. Chem. 278:48674-48683; Poelarends et al., 2004, Biochemistry 43:759-772; Poelarends et al., 2004, Biochemistry 43:7187-7196; Poelarends et al., 2004, J. Am. Chem. Soc. 126:15658-15659; Poelarends et al., 2005, Biochemistry 44:9375-9381; Poelarends et al., 2006, Biochemistry 45:7700-7708). This work led to the identification of new reactions in the tautomerase superfamily, provided evidence for the important role of catalytic promiscuity in the emergence of new enzymes, and revealed new mechanisms for enzyme-catalyzed dehalogenation and decarboxylation reactions (for an overview of this work see: Poelarends and Whitman, 2004, Bioorg. Chem. 32:376-392). The contribution of Dr. Poelarends to the dehalogenase field was recognized by others and led, for example, to an invited lecture at the Gordon Research Conference on Enzymes, Coenzymes, and Metabolic Pathways (2003) and an invited chapter on microbial dehalogenases included in the prestigious work Comprehensive Natural Products Chemistry II edited by Lew Mander and Hung-Wen Liu (published in 2010).

Dr. Poelarends was appointed as an assistant professor in the Department of Pharmaceutical Biology at the RUG in 2006, and was promoted to associate professor in 2012 and full professor in 2017. His current research interests are in the field of biocatalysis with a focus on the discovery and design of new protein catalysts and on the answers to the fundamental question: how do enzymes evolve? One research line focuses on the selection, characterization, and development of new biocatalysts for asymmetric addition reactions that lead to chiral amino acids with synthetically and/or pharmacologically useful properties (see Weiner et al., 2008, Chem. Eur. J. 14:10094-10100; Raj et al., 2009, ChemBioChem. 10:2236-2245; Fibriansah et al., 2011, Biochemistry 50:6053-6062; Raj et al., 2012, Appl. Microbiol. Biotechnol. 94:385-397; Raj et al., 2012, Nat. Chem.  4:478-484; Puthan Veetil et al., 2012, Biochemistry 51:4237-4243). Another research line is aimed at exploring the abundance of promiscuous enzyme activities, their mechanisms, and possible relevance as evolutionary starting points for both natural and laboratory evolution of new enzymes (see Wasiel et al., 2010, Biochemistry 49:7572-7581; Zandvoort et al., 2011, ChemBioChem 12:602-609; Baas et al., 2011,  Biochemistry 50:2889-2899; Zandvoort et al., 2012, Angew. Chem. Int. Ed. 51:1240-1243; Wasiel et al., 2012, ChemBioChem 13:1270-1273; Zandvoort et al., 2012, ChemBioChem 13:1274-1277).

The work of Dr. Poelarends on enzyme engineering has led to invited lectures at the most important international conferences in the areas of biocatalysis, protein engineering, and mechanistic enzymology. The quality of the work of Dr. Poelarends is also reflected in >90 publications (and book chapters) in high impact journals, of which >50 as first or last author. He was awarded prestigious personal VENI-NWO, VIDI-NWO, ERC-StG, ERC-PoC and VICI-NWO research grants for his innovative enzyme engineering work in 2004, 2006, 2010, 2016 and 2017, respectively.

 
Publications                                    
[2017]

  • Rahimi, M., van der Meer, J.Y., Geertsema, E.M., and Poelarends, G.J. (2017). Engineering a promiscuous tautomerase into a more efficient aldolase for self-condensations of linear aliphatic aldehydes. ChemBioChem., in press.
  • Rahimi, M., Geertsema, E.M., Miao, Y., van der Meer, J.Y., van den Bosch, T., de Haan, P., Zandvoort, E., and Poelarends, G.J. (2017) Inter- and intramolecular aldol reactions promiscuously catalyzed by a proline-based tautomerase. Org. Biomol. Chem., 15, 2809-2816.
  • Fu, H., Younes, S.H.H., Saifuddin, M., Tepper, P.G., Zhang, J., Keller, E., Heeres, A., Szymanski, W., and Poelarends, G.J. (2017) Rapid chemoenzymatic route to glutamate transporter inhibitor L-TFB-TBOA and related amino acids. Org. Biomol. Chem., 15, 2341-2344.
 
[2016]
 
  • Miao, Y., Tepper, P.G., Geertsema, E.M., and Poelarends, G.J. (2016) Stereochemical control of enzymatic carbon-carbon bond-forming Michael-type additions by 'substrate engineering'. Eur. J. Org. Chem. 32:5350–5354.

  • Van der Meer, J.Y., Biewenga, L., and Poelarends, G.J. (2016) The generation and exploitation of protein mutability landscapes for enzyme engineering. ChemBioChem. 17:1792-1799.

  • Rahimi, M., van der Meer, J.Y., Geertsema, E.M., Poddar, H., Baas, B.J., and Poelarends, G.J. (2016) Mutations closer to the active site improve the promiscuous aldolase activity of 4-oxalocrotonate tautomerase more effectively than distant mutations. ChemBioChem. 17:1225-1228.

  • Van der Meer, J.Y., Poddar, H., Baas, B.J., Miao, Y., Rahimi, M., Kunzendorf, A., van Merkerk, R., Tepper, P.G., Geertsema, E.M., Thunnissen, A.M.W.H., Quax, W.J., and Poelarends, G.J. (2016) Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases. Nat. Commun. 7:10911 doi: 10.1038/ncomms10911. 

  • Geertsema, E.M., Miao, Y., and Poelarends, G.J. (2016) Asymmetric Michael-type additions of acetaldehyde to nitroolefins catalyzed by 4-oxalocrotonate tautomerase (4-OT) yielding valuable γ-nitroaldehydes. In J. Whittal, P. Sutton, and W. Kroutil (eds.), Practical Methods in Biocatalysis and Biotransformations, volume 3, pp. 85-90. Wiley, UK.

[2015]
 
  • de Villiers, J., de Villiers, M., Geertsema, E.M., Raj, H., and Poelarends, G.J. (2015) Chemoenzymatic synthesis of ortho-, meta-, and para-substituted derivatives of L-threo-3-benzyloxyaspartate, an important glutamate transporter blocker. ChemCatChem. 7:1931-1934.

  • Ourailidou, M.E., Dockerty, P., Witte, M., Poelarends, G.J., and Dekker, F.J. (2015) Metabolic alkene labeling and in vitro detection of histone acylation via the aqueous oxidative Heck reaction. Org. Biomol. Chem. 13:3648-3653.

  • Baas, B.J., Poddar, H., Geertsema, E.M., Rozeboom, H.J., de Vries, M.P., Permentier, H.P., Thunnissen, A.M.W.H., and Poelarends, G.J. (2015) Functional and structural characterization of an unusual cofactor-independent oxygenase. Biochemistry 54:1219-1232.

  • Poddar, H., Rahimi, M., Geertsema, E.M., Thunnissen, A.M.W.H., and Poelarends, G.J. (2015) Evidence for formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomerase. ChemBioChem. 16:738-741.

  • Miao, Y., Rahimi, M., Geertsema, E.M., and Poelarends, G.J. (2015) Recent developments in enzyme promiscuity for carbon-carbon bond-forming reactions. Curr. Opin. Chem. Biol. 25:115-123.
 
[2014]
 
  • Geertsema, E.M., and Poelarends, G.J. (2014) Enzymatic carbon-carbon bond-forming Michael-type additions.  In K. Faber, W.-D. Fessner, and N. Turner (eds.), Science of Synthesis: Biocatalysis in Organic Synthesis, volume 2, pp. 313-334. Thieme Chemistry, Stuttgart, Germany.

  • Baas, B.J., Zandvoort, E., Wasiel, A.A., and Poelarends, G.J. (2014) Demethionylation of Pro-1 variants of 4-oxalocrotonate tautomerase in Escherichia coli by co-expression with an engineered methionine aminopeptidase. FEBS Open Bio 4:651-658.

  • Lambrechts, R.A., Srinivasan, B., Geertsema, E.M., Poelarends, G.J., Sibon, O.C.M., and de Villiers, M. (2014) Synthesis and characterization of 4-thiobutyl triphenylphosphonium-pantetheine, a pantetheine derivative. American Chemical Science Journal 4:676-686.

  • Ourailidou, M.E., van der Meer, J.Y., Baas, B.J., Jeronimus-Stratingh, M., Gottumukkala, A.L., Poelarends, G.J., Minnaard, A.J., and Dekker, F.J. (2014) Aqueous oxidative Heck reaction as a protein labeling strategy. ChemBioChem. 15:209-212.

  [2013]
 
  • Geertsema, E.M., Miao, Y., Tepper, P.G., de Haan, P., Zandvoort, E., and Poelarends, G.J. (2013) Biocatalytic Michael-type additions of acetaldehyde to nitroolefins with the proline-based enzyme 4-oxalocrotonate tautomerase yielding enantioenriched γ-nitroaldehydes. Chem. Eur. J. 19:14407-14410.

  • Poelarends, G.J., Serrano, H., Huddleston, J.P., Johnson, W.H., Jr., and Whitman, C.P. (2013) A mutational analysis of active site residues in trans-3-chloroacrylic acid dehalogenase. FEBS lett. 587:2842-2850.

  • Raj, H., and Poelarends, G.J. (2013) The roles of active site residues in the catalytic mechanism of methylaspartate ammonia-lyase. FEBS Open Bio 3:285-290.

  • Raj, H., Szymanski, W., de Villiers, J., Puthan Veetil, V., Quax, W.J., Shimamoto, K., Janssen, D.B., Feringa, B.L., and Poelarends, G.J. (2013) Kinetic resolution and stereoselective synthesis of 3-substituted aspartic acids using engineered methylaspartate ammonia lyases. Chem. Eur. J. 19:11148-11152.

  • Guo, Y., Serrano, H., Poelarends, G.J., Johnson, W.H., Jr., Hackert, M.L., and Whitman, C.P. (2013) Kinetic, mutational, and structural analysis of malonate semialdehyde decarboxylase from coryneform bacterium strain FG41: Mechanistic implications for the decarboxylase and hydratase activities. Biochemistry 52:4830-4841.

  • Baas, B.J., Zandvoort, E., Geertsema, E.M., and Poelarends, G.J. (2013) Recent advances in the study of enzyme promiscuity in the tautomerase superfamily. ChemBioChem. 14:917-926.

  • Puthan Veetil, V.,  Raj, H., de Villiers, M., Tepper, P.G., Dekker, F.J., Quax, W.J., and Poelarends, G.J. (2013) Enantioselective synthesis of N-substituted aspartic acids using an engineered variant of methylaspartate ammonia lyase. ChemCatChem. 5:1325-1327.

  • Miao, Y., Geertsema, E.M., Tepper, P.G., Zandvoort, E., and Poelarends, G.J. (2013) Promiscuous catalysis of asymmetric Michael-type additions of linear aldehydes to β-nitrostyrene by the proline-based enzyme 4-oxalocrotonate tautomerase. ChemBioChem. 14:191-194.

  • Crismaru, C.G., Wybenga, G.G., Szymański, W., Wijma, H.J., Wu, B., Bartsch, S., de Wildeman, S., Poelarends, G.J., Feringa, B.L., Dijkstra, B.W., and Janssen, D.B. (2013) Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus. Appl. Environ. Microbiol. 79:185-195.

[2012]
 
  • Godinho, L.F., Reis, C.R., van Merkerk, R., Poelarends, G.J., and Quax, W.J. (2012) An esterase with superior activity and enantioselectivity towards 1,2-O-isopropylideneglycerol esters obtained by protein design. Adv. Synth. Catal. 354:3009-3015.

  • Zandvoort, E., Geertsema, E.M., Baas, B.J., Quax, W.J., and Poelarends, G.J. (2012) An unexpected promiscuous activity of 4-oxalocrotonate tautomerase: the cis-trans isomerization of nitrostyrene. ChemBioChem. 13:1869-1873.

  • de Villiers, M., Puthan Veetil, V., Raj, H., de Villiers, J., and Poelarends, G.J. (2012) Catalytic mechanisms and biocatalytic applications of aspartate and methylaspartate ammonia lyases. ACS Chem. Biol. 7: 1618-1628.

  • Zandvoort, E., Geertsema, E.M., Quax, W.J., and  Poelarends, G.J. (2012) Enhancement of the promiscuous aldolase and dehydration activities of 4-oxalocrotonate tautomerase by protein engineering. ChemBioChem. 13:1274-1277.

  • Wasiel, A.A., Baas, B.J., Zandvoort, E., Quax, W.J., and Poelarends, G.J. (2012) Dehalogenation of an anthropogenic compound by an engineered variant of the mouse cytokine macrophage migration inhibitory factor. ChemBioChem. 13:1270-1273.

  • Raj, H., Szymański , W.,  de Villiers, J., Rozeboom, H.J., Puthan Veetil, V.,  Reis , C.R., de Villiers, M., Dekker, F.J., de Wildeman, S.,  Quax, W.J., Thunnissen, A.-M.W.H., Feringa, B.L., Janssen, D.B., and Poelarends, G.J. (2012) Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids. Nat. Chem. 4:478-484.

  • Puthan Veetil, V., Fibriansah, G., Raj, H., Thunnissen, A.-M.W.H., and Poelarends, G.J. (2012) Aspartase/fumarase superfamily: a common catalytic strategy involving general base-catalyzed formation of a highly stabilized aci- carboxylate intermediate. Biochemistry 51:4237-4243.

  • Godinho, L.F., Reis, C.R., Rozeboom, H.J., Dekker, F.J., Dijkstra, B.W., Poelarends, G.J., and Quax, W.J. (2012) Enhancement of the enantioselectivity of carboxylesterase A by structure-based mutagenesis. J. Biotechnol. 158:36-43.

  • Zandvoort, E., Geertsema, E.M., Baas, B.J., Quax, W.J., and  Poelarends, G.J. (2012) Bridging between organocatalysis and biocatalysis: asymmetric addition of acetaldehyde to β-nitrostyrenes catalyzed by a promiscuous proline-based tautomerase. Angew. Chem. Int. Ed. 51:1240-1243.

  • Wu, B., Szymański, W., Wybenga, G.G., Heberling, M.M., Bartsch, S., de Wildeman, S., Poelarends, G.J., Feringa, B.L., Dijkstra, B.W., and Janssen, D.B. (2012) Mechanism-inspired engineering of phenylalanine aminomutase for enhanced β-regioselective asymmetric amination of cinnamates. Angew. Chem. Int. Ed. 51:482-486.

  • Raj, H., Puthan Veetil, V., Szymański, W., Dekker, F.J., Quax, W.J., Feringa, B.L., Janssen, D.B., and Poelarends, G.J. (2012) Characterization of a thermostable methylaspartate ammonia lyase from Carboxydothermus hydrogenoformans. Appl. Microbiol. Biotechnol. 94:385-397.

[2011]
 
  • Godinho, L.F., Reis, C.R., Tepper, P.G., Poelarends, G.J., and Quax, W.J. (2011) Discovery of an E. coli esterase with high activity and enantioselectivity toward 1,2-O-isopropylideneglycerol esters. Appl. Environ. Microbiol. 77:6094-6099.

  • Fibriansah, G., Puthan Veetil, V., Poelarends, G.J.,1 and Thunnissen, A.-M.W.H.1 (2011) Structural basis for the catalytic mechanism of aspartate ammonia lyase. Biochemistry 50:6053-6062. [1Shared corresponding authorship]

  • Wahjudi, M., Papaioannou, E., Hendrawati, O., van Assen, A.H., van Merkerk, R., Cool, R.H., Poelarends, G.J., and Quax, W.J. (2011) PA0305 of Pseudomonas aeruginosa is a quorum quenching acyl homoserine lactone acylase belonging to the Ntn hydrolase superfamily. Microbiology 157:2042-2055.

  • Baas, B.J., Zandvoort, E., Wasiel, A.A., Quax, W.J., and Poelarends, G.J. (2011) Characterization of a newly identified mycobacterial tautomerase with promiscuous dehalogenase and hydratase activities reveals a functional link to a recently diverged cis -3-chloroacrylic acid dehalogenase. Biochemistry 50:2889-2899.

  • Zandvoort, E., Baas, B.J., Quax, W.J., and Poelarends, G.J. (2011) Systematic screening for catalytic promiscuity in 4-oxalocrotonate tautomerase: Enamine formation and aldolase activity. ChemBioChem. 12:602-609.

[2010]
 
  • Wu, B., Szymanski, W., Wijma, H.J., Crismaru, C.G., de Wildeman, S., Poelarends, G.J., Feringa, B.L., and Janssen, D.B. (2010) Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase. Chem. Commun. 46:8157-8159.

  • Wasiel, A.A., Rozeboom, H.J., Hauke, D., Baas, B.J., Zandvoort, E., Quax, W.J., Thunnissen, A.-M.W.H., and Poelarends, G.J. (2010) Structural and functional characterization of a macrophage migration inhibitory factor homologue from the marine cyanobacterium Prochlorococcus marinus. Biochemistry 49:7572-7581.

  • Wu, B., Szymanski, W., de Wildeman, S., Poelarends, G.J., Feringa, B.L., and Janssen, D.B. (2010) Efficient tandem biocatalytic process for the kinetic resolution of aromatic β-amino acids. Adv. Synth. Catal. 352:1409-1412.

  • Poelarends, G.J. , and Whitman, C.P. (2010) Mechanistic and structural studies of microbial dehalogenases: How Nature cleaves a carbon-halogen bond. In L.N. Mander and H.-W. Liu (eds.), Comprehensive Natural Products II: Chemistry and Biology , volume 8, pp. 89-123. Elsevier, Oxford, UK.

[2009]
 
  • Raj, H., Weiner, B., Puthan Veetil, V., Reis, C.R., Quax, W.J., Janssen, D.B., Feringa, B.L., and Poelarends, G.J. (2009) Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis. ChemBioChem. 10:2236-2245.

  • Puthan Veetil, V., Raj, H., Quax, W.J., Janssen, D.B., and Poelarends, G.J. (2009) Site-directed mutagenesis, kinetic, and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55-1. FEBS J. 276:2994-3007.

  • Wu, B., Szymanski, W., Wietzes, P., de Wildeman, S., Poelarends, G.J., Feringa, B.L., and Janssen, D.B. (2009) Enzymatic synthesis of enantiopure α- and β-amino acids by phenylalanine aminomutase-catalyzed amination of cinnamic acid derivatives. ChemBioChem. 10:338-344.

[2008]
 
  • Weiner, B., Poelarends, G.J. 1, Janssen, D.B.1, and Feringa, B.L.1 (2008) Biocatalytic enantioselective synthesis of N-substituted aspartic acids by aspartate ammonia lyase. Chem. Eur. J. 14:10094-10100. [1Shared corresponding authorship]

  • Poelarends, G.J. , Puthan Veetil, V., and Whitman, C.P. (2008) The chemical versatility of the β-α-β fold: catalytic promiscuity and divergent evolution in the tautomerase superfamily. Cell. Mol. Life Sci. 65:3606-3618. [Cover story]

  • Poelarends, G.J. , Serrano, H., Person, M.D., Johnson, W.H., Jr., and Whitman, C.P. (2008) Characterization of Cg10062 from Corynebacterium glutamicum: implications for the evolution of cis-3-chloroacrylic acid dehalogenase activity in the tautomerase superfamily. Biochemistry 47:8139-8147.

[2007]
 
  • Poelarends, G.J., Johnson, W.H., Jr., Serrano, H., and Whitman, C.P. (2007) The phenylpyruvate tautomerase activity of trans-3-chloroacrylic acid dehalogenase: Evidence for an enol intermediate in the dehalogenase reaction? Biochemistry 46:9596-9604.

  • de Jong, R.M., Bazzacco, P., Poelarends, G.J., Johnson, W.H., Jr., Kim, Y.J., Burks, E.A., Serrano, H., Thunnissen, A-M.W.H., Whitman, C.P., and Dijkstra, B.W. (2007) Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase: structural basis for substrate specificity and inactivation by (R)-oxirane-2-carboxylate. J. Biol. Chem. 282:2440-2449.

[2006]
 
  • Poelarends, G.J. , Almrud, J.J., Serrano, H., Darty, J.E., Johnson, W.H., Jr., Hackert, M.L., and Whitman, C.P. (2006) Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase. Biochemistry 45:7700-7708.

[2005]
 
  • Janssen, D.B., Dinkla, I.J.T., Poelarends, G.J., and Terpstra, P. (2005) Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activities. Environ. Microbiol. 7:1868-1882.

  • Almrud, J.J.1, Poelarends, G.J. 1, Johnson, W.H., Jr., Serrano, H., Hackert, M.L., and Whitman, C.P. (2005) Crystal structures of the wild-type, P1A mutant, and inactivated malonate semialdehyde decarboxylase: A structural basis for the decarboxylase and hydratase activities. Biochemistry 44:14818-14827. [1Shared first authorship]

  • Poelarends, G.J. , Serrano, H., Johnson, W.H., Jr., and Whitman, C.P. (2005) Inactivation of malonate semialdehyde decarboxylase by 3-halopropiolates: Evidence for hydratase activity. Biochemistry 44:9375-9381.

  • Mazurkiewicz, P., Sakamoto, K., Poelarends, G.J., and Konings, W.N. (2005) Multidrug transporters in lactic acid bacteria. Mini Rev. Med. Chem. 5:173-181.

[2004]
 
  • Poelarends, G.J. , Serrano, H., Johnson, W.H., Jr., Hoffman, D.W., and Whitman, C.P. (2004) The hydratase activity of malonate semialdehyde decarboxylase: Mechanistic and evolutionary implications. J. Am. Chem. Soc. 126:15658-15659.

  • Poelarends, G.J. , and Whitman, C.P. (2004) Evolution of enzymatic activity in the tautomerase superfamily: Mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes. Bioorg. Chem. 32:376-392.

  • Ecker, G.F., Pleban, K., Kopp, S., Csaszar, E., Poelarends, G.J., Putman, M., Kaiser, D., Konings, W.N., and Chiba, P. (2004) A three-dimensional model for the substrate binding domain of the multidrug ABC transporter LmrA. Mol. Pharmacol. 66:1169-1179.

  • Johnson, W.H., Jr., Wang, S.C., Stanley, T.M., Czerwinski, R.M., Almrud, J.J., Poelarends, G.J., Murzin, A.G., and Whitman, C.P. (2004) 4-Oxalocrotonate tautomerase, its homologue YwhB, and active vinylpyruvate hydratase: synthesis and evaluation of 2-fluoro substrate analogues. Biochemistry 43:10490-10501.

  • Poelarends, G.J. , Serrano, H., Johnson, W.H., Jr., and Whitman, C.P. (2004) Stereospecific alkylation of cis-3-chloroacrylic acid dehalogenase by (R)-oxirane-2-carboxylate: Analysis and mechanistic implications. Biochemistry 43:7187-7196.

  • Azurmendi, H.F., Wang, S.C., Massiah, M.A., Poelarends, G.J., Whitman, C.P., and Mildvan, A.S. (2004) The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: A kinetic, NMR, and mutational analysis. Biochemistry 43:4082-4091.

  • Poelarends, G.J. , Serrano, H., Person, M.D., Johnson, W.H., Jr., Murzin, A.G., and Whitman, C.P. (2004) Cloning, expression, and characterization of a cis-3-chloroacrylic acid dehalogenase: Insights into the mechanistic, structural, and evolutionary relationship between isomer-specific 3-chloroacrylic acid dehalogenases. Biochemistry 43:759-772.

  • de Jong, R.M., Brugman, W., Poelarends, G.J., Whitman, C.P., and Dijkstra, B.W. (2004) The X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily. J. Biol. Chem. 279:11546-11552.

  • Mazurkiewicz, P., Poelarends, G.J. , Driessen, A.J.M., and Konings, W.N. (2004) Facilitated drug influx by an energy-uncoupled secondary multidrug transporter. J. Biol. Chem. 279:103-108.

[2003]
 
  • Alqawi, O., Poelarends, G.J., Konings, W.N., and Georges, E. (2003) Photoaffinity labeling under non-energized conditions of a specific drug-binding site of the ABC multidrug transporter LmrA from Lactococcus lactis. Biochem. Biophys. Res. Commun. 311:696-701.

  • Poelarends, G.J. , Johnson, W.H., Jr., Murzin, A.G., and Whitman, C.P. (2003) Mechanistic characterization of a bacterial malonate semialdehyde decarboxylase: Identification of a new activity in the tautomerase superfamily. J. Biol. Chem. 278:48674-48683.

  • Lewinson, O., Adler, J., Poelarends, G.J., Mazurkiewicz, P., Driessen, A.J.M., and Bibi, E. (2003) The Escherichia coli multidrug transporter MdfA catalyzes both electrogenic and electroneutral transport reactions. Proc. Natl. Acad. Sci. USA. 100:1667-1672.

  • Poelarends, G.J. , Vigano, C., Ruysschaert, J.-M., and Konings, W.N. (2003) Bacterial multidrug resistance mediated by ABC transporters. In B. Holland, K. Kuchler, C. Higgins, S. Cole (eds.), ABC proteins: from bacteria to man, p. 243-262. Elsevier Science Ltd.

  • Janssen, D.B., Oppentocht, J.E., and Poelarends, G.J. (2003) Bacterial growth on halogenated aliphatic hydrocarbons: genetics and biochemistry. In M.M. Häggblom and I.D. Bossert (eds.), Dehalogenation: microbial processes and environmental applications, p. 207-226. Kluwer Academic Publishers, Dordrecht, The Netherlands.

[2002]
 
  • Poelarends, G.J. , Mazurkiewicz, P., and Konings, W.N. (2002) Multidrug transporters and antibiotic resistance in Lactococcus lactis. Biochim. Biophys. Acta. 1555:1-7.

  • Poelarends, G.J. , and Konings, W.N. (2002) The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within the membrane. J. Biol. Chem. 277:42891-42898.

  • Konings, W.N., and Poelarends, G.J. (2002) Bacterial multidrug resistance mediated by a homologue of the human multidrug transporter P-glycoprotein. IUBMB Life 53:213-218.

  • Mazurkiewicz, P., Konings, W.N., and Poelarends, G.J. (2002) Acidic residues in the lactococcal multidrug efflux pump LmrP play critical roles in transport of lipophilic cationic compounds. J. Biol. Chem. 277:26081-26088.

  • Poelarends, G.J. , van Hylckama Vlieg, J.E.T., Bosma, T., and Janssen, D.B. (2002) The haloalkane dehalogenase genes dhlA and dhaA are globally distributed and highly conserved. In S.N. Agathos and W. Reineke (eds.), Biotechnology for the environment: strategy and fundamentals, p. 59-66. Kluwer Academic Publishers, Dordrecht, The Netherlands.

[2001]
 
  • Van Hylckama Vlieg, J.E.T., Tang, L., Lutje Spelberg, J.H., Smilda, T., Poelarends, G.J., Bosma, T., van Merode, A.E.J., Fraaije, M.W., and Janssen, D.B. (2001) Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases/reductases. J. Bacteriol. 183:5058-5066.

  • Poelarends, G.J. , Saunier, R., and Janssen, D.B. (2001) trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase. J. Bacteriol. 183:4269-4277.

  • Janssen, D.B., Oppentocht, J.E., and Poelarends, G.J. (2001) Microbial Dehalogenation. Curr. Opin. Biotechnol. 12:254-258.

[2000]
 
  • Poelarends, G.J. , Mazurkiewicz, P., Putman, M., Cool, R.H., van Veen, H.W., and Konings, W.N. (2000) An ABC-type multidrug transporter of Lactococcus lactis possesses an exceptionally broad substrate specificity. Drug Resist. Updat. 3:330-334.

  • Van Hylckama Vlieg, J.E.T., Poelarends, G.J., Mars, A.E., and Janssen, D.B. (2000) Detoxification of reactive intermediates during microbial metabolism of halogenated compounds. Curr. Opin. Microbiol. 3:257-262.

  • Poelarends, G.J. , Zandstra, M., Bosma, T., Kulakov, L.A., Larkin, M.J., Marchesi, J.R., Weightman, A.J., and Janssen, D.B. (2000) Haloalkane-utilizing Rhodococcus strains isolated from geographically distinct locations possess a highly conserved gene cluster encoding haloalkane catabolism. J. Bacteriol. 182:2725-2731.

  • Poelarends, G.J. ,Kulakov, L.A., Larkin, M.J., van Hylckama Vlieg, J.E.T., and Janssen, D.B. (2000) Roles of horizontal gene transfer and gene integration in evolution of 1,3-dichloropropene- and 1,2-dibromoethane-degradative pathways. J. Bacteriol. 182:2191-2199.

[1999]
 
  • Bosma, T., Kruizinga, E., de Bruin, E.J., Poelarends, G.J., and Janssen, D.B. (1999) Utilization of trihalogenated propanes by Agrobacterium radiobacter AD1 through heterologous expression of the haloalkane dehalogenase from Rhodococcus sp. strain m15-3. Appl. Environ. Microbiol. 65:4575-4581.

  • Kulakov, L.A., Poelarends, G.J., Janssen, D.B., and Larkin, M.J. (1999) Characterization of IS2112, a new insertion sequence from Rhodococcus, and its relationship with mobile elements belonging to the IS110 family. Microbiology 145:561-568.

  • Poelarends, G.J. , van Hylckama Vlieg, J.E.T., Marchesi, J.R., Freitas dos Santos, L.M., and Janssen, D.B. (1999) Degradation of 1,2-dibromoethane by Mycobacterium sp. strain GP1. J. Bacteriol. 181:2050-2058.

  • Janssen, D.B., Poelarends, G.J. , and Rink, R. (1999) Engineering hydrolases for the conversion of halogenated aliphatic hydrocarbon and epoxides. In R. Fass, Y. Flashner, and S. Reuveny (eds.) Novel approaches for bioremediation of organic pollutants, p. 105-117. Kluwer Academic Publishers, USA.

[1994-1998]
 
  • Poelarends, G.J. , Wilkens, M., Larkin, M.J., van Elsas, J.D., and Janssen, D.B. (1998) Degradation of 1,3-dichloropropene by Pseudomonas cichorii 170. Appl. Environ. Microbiol. 64:2931-2936.

  • Janssen, D.B., Poelarends, G.J. , van Pée, K.H., Weightman, A.J., and Larkin, M.J. (1998) Microbial adaptation to degradation of natural and synthetic organohalogens: Effects on ecosystem acclimation and natural bioremediation of polluted sites. In J. Büsing, C.A. Nogueira, and F. Rodrigues (eds.), Recycling technologies, treatment of waste, remediation of contaminated sites and life cycle assessment, p. 349-355. INETI workshop, Lisbon, Portugal.

  • Schanstra, J.P., Poelarends, G.J. , Bosma, T., and Janssen, D.B. (1997) Engineering enzymes and microorganisms for the transformation of synthetic compounds. In J. Sanseverino and G. Sayler (eds.), Biotechnology and a sustainable environment, p. 47-57. Plenum Publishing Corporation, New York, USA.

  • Janssen, D.B., Bosma, T., and Poelarends, G.J. (1997) Diversity and mechanisms of bacterial dehalogenation reactions. In D.B. Janssen, K. Soda, and R. Wever (eds.), Mechanisms of biohalogenation and dehalogenation, p. 119-129. Elsevier Science, The Netherlands.

  • Schanstra, J.P., Ridder, I.S., Heimeriks, G.J., Rink, R., Poelarends, G.J., Kalk, K.H., Dijkstra, B.W., and Janssen, D.B. (1996) Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate range. Biochemistry 35:13186-13195.

  • Poelarends, G.J. , and Janssen, D.B. (1995) Genetic adaptation to 1,2-dichloroethane and related compounds. In M. Cuno (ed.), Mikrobielle eliminierung chlororganischer verbindungen, p. 159-167. Techn. Univ. Berlin, Berlin, Germany.

  • Bolhuis, H., Poelarends, G.J., van Veen, H.W., Poolman, B., Driessen, A.J.M., and Konings, W.N. (1995) The lactococcal lmrP gene encodes a proton motive force-dependent drug transporter. J. Biol. Chem. 270:26092-26098.

  • Bolhuis, H., Molenaar, D., Poelarends, G.J., van Veen, H.W., Poolman, B., Driessen, A.J.M., and Konings, W.N. (1994) Proton motive force-driven and ATP-dependent drug extrusion systems in multidrug-resistant Lactococcus lactis. J. Bacteriol. 176:6957-6964.

Laatst gewijzigd:05 augustus 2017 10:51