2011 12 27 Name: van Loo bert

Status: Postdoc

Email: b.vanloo[at]wwu.de

Tel.: +49-(0)251-83-21636

Room: 100.22


  • 05/2013-present: Postdoc at the Institute for Evolution and Biodiversity, University of Münster
  • 02/2013-04/2013: Visiting Postdoctoral research associate at the Department of Cell and Molecular Biology, Uppsala University, Sweden
  • 04/2005-01/2013: Postdoctoral research associate at the Department of Biochemistry, University of Cambridge, United Kingdom
  • 04/1999-03/2005: PhD in Biochemistry at the Biochemical Laboratory, University of Groningen, The Netherlands.
  • 09/1994-03/1999: MSc in Molecular Sciences, Wageningen University Research Centre, The Netherlands

Research interests

  • Protein evolution
  • Enzyme mechanism
  • Catalytic promiscuity



  • SoSe 2014 -present: Bioinformatics 2 (supervisor practicals)
  • WiSe 2018/2019: Vertiefungs Modul Evolutionairy Protein Design (lecturer)
  • March -August: Projekt Modul/Bachelor thesis
    • 2019: Christopher Finke
    • 2017: Margaux Aubel, Frederik Klodt
    • 2016: Nadine Ritter
    • 2015: Manuel Kösters


  • SoSe 2017 - present: Fortgeschrittenenmodul Molecular Protein Engineering (coordinator/main lecturer)
  • WiSe 2015/2016 - present: Fortgeschrittenenmodul Molecular Phlyogeny (lecturer)
  • WiSe 2014/2015 - present: Fortgeschrittenenmodul Biocomputing I/II (project supervisor)
  • SoSe 2017 - present: Forschungsmodul Molecular Protein Engineering and Design (coordinator/project supervisor)
  • Master Thesis
    • Elias Dohmen (Feb 2014 - Feb 2015)
    • Margaux Aubel (June 2019 - present)


  • van Loo B. (2017) Misannotation of the Catalytic Function of Hydrolases in Plasmodium falciparum . mBio, submitted.
  • van Loo B.*, Heberlein M.*, Mair P., Zinchenko A., Schüürmann J., Eenink B.D.G., Holstein J.M., Dilkaute C., Jose J., Hollfelder F., and Bornberg-Bauer E. (2019) High-Throughput, Lysis-free Screening for Sulfatase Activity Using Escherichia coli Autodisplay in Microdroplets. submitted
  • van Loo B., Berry R., Boonyuen U., Mohamed M.F., Golicnik M., Hengge A.C., and Hollfelder F. (2019) Transition State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase. Biochemistry 58, 1363-1378.
  • van Loo B., Bayer C.D., Fischer G., Jonas S., Valkov E., Mohamed M.F., Vorobieva A., Dutruel C., Hyvönen M., and Hollfelder F. (2019) Balancing specificity and promiscuity in enzyme evolution: multidimensional activity transitions in the alkaline phosphatase superfamily. J. Am. Chem Soc. 141, 370-387.
  • Miton C.M., Jonas S. Fischer G., Duarte F., Mohamed M.F., van Loo B., Kintses B., Kamlerlin S.C.L., Tokuriki N., Hyvönen M., and Hollfelder F. (2018) Evolutionary repurposing of a sulfatase: a new Michaelis complex leads to efficient transition state charge offset. Proc. Natl. Acad. Sci. U. S. A. 115, E7293-E7302.
  • van Loo B., Schober M., Valkov E., Heberlein M., Bornberg-Bauer E., Faber K., Hyvönen M., and Hollfelder F. (2018) Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: a Class I Sulfatase Specific for an Alkyl Sulfate Ester. J. Mol. Biol. 430, 1004-1023
  • van Loo B. and Bornberg-Bauer E. (2017) Enzyme sub-functionalization driven by regulation. EMBO Rep. 18, 1043-1045.
  • Bayer C.D.*, van Loo B.*, and Hollfelder F. (2017) Specificity effects of amino acid substitutions in promiscuous hydrolases - context-dependence of catalytic residue contributions to local fitness landscapes in nearby sequence space. ChemBioChem 18, 1001-1015.
  • Schober M., Toesch M., Knaus T., Strohmeier G. A., van Loo, B., Fuchs M., Hollfelder F., Macheroux P., and Faber K. (2013) One-Pot Deracemization of sec-Alcohols: Enantioconvergent Enzymatic Hydrolysis of Alkyl Sulfates Using Stereocomplementary Sulfatases. Angew. Chem. Int. Ed. 52, 3277-3279.
  • Luo J., van Loo B., and Kamerlin S. C. L. (2012) Catalytic Promiscuity in Pseudomonas aeruginosa Arylsulfatase as an example of Chemistry-Driven Protein Evolution. FEBS Lett. 586, 1622-1630.
  • Luo J., van Loo B., and Kamerlin S. C. L. (2012) Examining the promiscuous phosphatase activity of Pseudomonas aeruginosa arylsulfatase: A comparison to analogous phosphatases. Prot. Struct. Funct. Bioinform. 80, 1211-1226.
  • van Loo B.*, Jonas S.*, Babtie A. C., Benjdia A., Berteau O., Hyvonen M., and Hollfelder F. (2010) An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily. Proc. Natl. Acad. Sci. U. S. A. 107, 2740-2745.
  • van Loo B. and Hollfelder F. (2010) Enzyme Promiscuity and the Evolution of New Protein Functions, p. 524-538. In Baltz et al. (ed.) Manual of Industrial Microbiology and Biotechnology, 3rd edition, ASM press, Herndon, United States.
  • van Loo B., Kingma J., Heyman G., Wittenaar A., Lutje Spelberg J. H., Sonke T., and Janssen D. B. (2009) Improved Kinetic Resolution of Styrene Epoxides and meso Epoxides Through Epoxide Hydrolases with a Mutated Nucleophile Flanking Residue. Enz. Microb. Technol. 44, 145-153.
  • Jonas S., van Loo B., Hyvonen M., and Hollfelder F. (2008) A New Member of the Alkaline Phosphatase Superfamily with a Formylglycine Nucleophile: Structural and Kinetic Characterisation of Phosphonate Monoester Hydrolase/Phosphodiesterase from Rhizobium leguminosarum. J. Mol. Biol. 384, 120-136.
  • van Loo, B., Permentier, H. P., Kingma, J., Baldascini, H., and Janssen, D. B. (2008) Inactivation of Epoxide Hydrolase by Catalysis Induced Formation of Isoaspartate. FEBS Lett. 582, 1581-1586.
  • van Loo B., Kingma J., Arand M., Wubbolts M. G., and Janssen D. B. (2006) Diversity and Biocatalytic Potential of Epoxide Hydrolases Identified by Genome Analysis. Appl. Environ. Microbiol. 72, 2905 2917.
  • van Loo B., Lutje Spelberg J. H., Kingma, J., Sonke T., Wubbolts M. G., and Janssen D. B. (2004) Directed Evolution of Epoxide Hydrolase from A. radiobacter toward Higher Enantioselectivity by Error Prone PCR and DNA Shuffling. Chem. Biol. 11, 981-990.
  • Kaper T., van Heusden H. H., van Loo B., Vasella A., van der Oost J., and de Vos W. M. (2002) Substrate Specificity Engineering of β- Mannosidase and β-Glucosidase from Pyrococcus by Exchange of Unique Active Site Residues. Biochemistry 41, 4147-4155.
  • Bouwmeester H. J., Wallaart T. E., Janssen M. H., van Loo, B., Jansen, B. J., Posthumus M. H., Schmidt C. O., de Kraker J. W., König W. A., and Franssen M. C. (1999) Amorpha-4,11-diene synthase catalyses the first probable step in artemisinin biosynthesis. Phytochemistry 52, 843-854.