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Biochemie II

Faculty of Biology and Preclinical Medicine
Institute of Biophysics and Physical Biochemistry
Biochemistry II


In the focus of our research are enzymes, which are elaborate proteins that catalyse cellular reactions with high specificity and efficiency.

Model system

Our preferred model system is the (βα)8-barrel family of enzymes, which is the most frequently encountered protein fold. (βα)8-barrel enzymes catalyse a large variety of mechanistically diverse reactions. The fold of the canonical (βα)8-barrel consists of a central barrel of eight parallel β-strands, which are surrounded by eight external α-helices. Connecting loops are located at both the N-terminal (α-β loops) and the C-terminal (β-α loops) face of the barrel. Due to the spatial separation of structural elements that are important for stability and catalytic activity, (βα)8-barrels provide an ideal scaffold for the study of enzyme evolution and the design of new enzymatic activities.


We are using rational design and directed evolution to engineer the stability and catalytic activity of enzymes, experimentally reconstruct the natural evolution of enzymes, assign functions to uncharacterised enzymes, and characterize allosteric interactions within multi-enzyme complexes. To this end, we apply a broad range of experimental and computational methods.



Dr. Steffen Schmidt 1998-1999

MPI für Entwicklungsbiologie



Dr. Silke Beissmann-


Jan 1998 -

Jan 2001

Ortlieb Vegetables & Nuts GmbH


Vera Röhlich

Juli 2000 -

Juni 2001

Weleda AG EMail
Dr. Martina Henn-Sax

Sept 1998 -

Dez 2001

abiturlernen.de EMail
Dr. Andreas Ivens

 Jan 2000 -

Juni 2002

Baxter AG Wien EMail
Dr. Stefan Hettwer

Apr 1998 -

Sept 2002

Neurotune AG

Schlieren, Schweiz

Dr. Satoshi Akanuma

Juli 2001 -

Feb 2003

University of Pharmacy and Life

Sciences, Tokyo

Jeannine Mohrlüder

März 2002 -

März 2003

Universität Düsseldorf INB-2

Forschungszentrum Jülich

Dr. Birte Höcker

Nov 1998 -

Juni 2003

MPI für Entwicklungsbiologie


Dr. Manal Bosnali

Okt 2002 -

März 2004

LIFE & BRAIN GmbH, Bonn EMail
Natalie Heuer

Okt 2002 -

März 2004

Universität Köln

Institut für Biochemie

Simona Jansen

Juli 2000 -

April 2004

Universität Köln

Institut für Biochemie

Iris Lambeck

Dez 2003 -

Dez 2004

Roche Pharma Basel

QA Manager

Dr. Catharina Dönges

März 2000 -

Jan 2005

Noeh Johannes Dönges

24-h Service

Susanne Marquardt

April 2004 -

März 2005

Geneart AG, Regensburg EMail
Birgit Schwarz

Dez 2003 -

April 2005

Abbott Diagnostics


Dr. Michaela Häger

Feb 2001 -

Juni 2005

Preglem / Gedeon Richter, Köln und

Hochschule Bonn-Rhein-Sieg

Dr. Karin Babinger

Juni 2005 -

Okt 2005

Universität Regensburg

Lehrstuhl für Anatomie I

Dr. Sonja Leopoldseder

2001 - 

Jan 2006

Profos AG, Regensburg x
Christian Bolz

Jan 2006 -

Nov 2006

ImevaX GmbH, München x
Philipp Riede

Mai 2006 -

Dez 2006

Oxford University


Anne Schwabe

Dez 2006 -

Juni 2007

University of Colorado

grad student

Maximilian Plank

Juni 2006 -

Aug 2007

University of Newcastle

Australien, PhD student

Lorella Ungar

Jan 2004 -

Aug 2007

FH Kempten Sekretariat x
Sabine Einhell

Dez 2006 -

Sept 2007

Universität Regensburg


Matthias Zwick

Sep 2006 -

Dez 2007

Biozentrum Basel, Schweiz x
Dr. Markus Richter

Mai 2004 -

Aug 2008

Geneart AG, Regensburg x
Dr. Jörg Claren

Nov 2004 -

Dez 2008

Süd-Chemie AG, München EMail
Ulrike Eßlinger

Juni 2008 -

Mai 2009

Universität Regensburg, Klinik 

und Poliklinik für Innere Medizin II

Daniel Roderer

Sep 2008 -

Aug 2009

ETH Zürick, Institut für

Molekularbiologie und Biophysik

Bettina Sommer

Feb 2009 -

Nov 2009

University of Prince Edward Island, Charlottetown, Canada EMail
Dr. Felix List

Nov 2004 -

März 2010

EMBL Hamburg x
Dr. Alexander Ehrmann

Okt 2005 -

Aug 2010

Bayer Schering Pharma AG EMail
Dr. Tobias Seitz

April 2006 -

Sept 2010

Roche Diagnostics GmbH (Pharma Biotech Penzberg) EMail
Nadine Borst

Jan 2010 -

Sept 2010

TU München, Lehrstuhl für

biogene Rohstoffe (WZ Straubing)

Dr. Thomas Schwab

Jan 2006 -

Dez 2010

Boehringer Ingelheim Pharma

GmbH & Co KG, Biberach a.d.Riß

Dr. Susanne Dietrich

Okt 2005 -

Dez 2010

Universitätsklinikum Regensburg

AG Prof. Kerkhoff

Dr. Harald Guldan

Feb 2007 -

Juni 2011

Lophius Biosciences GmbH


Dr. Marco Bocola

Okt 20069 -

Juli 2011

RWTH Aachen University

Dept of Biotechnology

Dr. Hermann Zellner

April 2007 -

Okt 2011

European Bioinformatics Institute

EMBL - EBI Hinxton

Barbara Beer

Mai 2011 -

Mai 2012

TU München (WZ Straubing)

LS f. Chemie biogener Rohstoffe

Dr. Daniel Schneider

Dez 2006 -

Mai 2012

Universität Konstanz, Lehrstuhl

organische / zelluläre Chemie

Dr. Linn Carstensen

Okt 2008 -

Juni 2012

Bayer Schering Pharma AG EMail
Veronika Schmid

Jan 2012 -

Sept 2012

Universitätsklinikum Regensburg

AG Prof. Wagner

Bastian Groitl

Jan 2012 -

Sept 2012

Universität Michigan, Ann Arbor

Dept of Molecular, Cellular and

Developmental Biology

Dr. Monika Meier

Feb 2008 -

Jan 2013

Roche Diagnostics GmbH EMail
Dr. Dietmar Birzer

März 2009 -

Aug 2013

TNG Technology Consulting GmbH


Dr. Josef Sperl

Aug 2009 -

Aug 2013

TU München, Lehrstuhl für Chemie Biogener Rohstoffe (wiss.MA) EMail
Dr. David Peterhoff

Aug 2009 -

Okt 2013

Universitätsklinikum Regensburg
Institut für Med. Mikrobiologie und Hygiene

Dr. Bernd Reisinger

Aug 2009 -

Juli 2014

Physikalisch-Technische Bundesanstalt, Braunschweig EMail
Dr. Florian Busch

Jan 2010 -

Aug 2015

The Ohio State University, Columbus, USA EMail


The following list summarizes all contributions of the scientific employees

2016 - 2015

Ruther, J., Hagström, A.K., Brandstetter, B., Hofferbert, J., Bruckmann, A., Semmelmann, F., Fink, M., Lowack, H., Laberer, S., Niehuis, O., Deutzmann, R., Löfstedt, C. & Sterner, R. (2016).  Epimerisation of chiral hydroxylactones by short-chain dehydrogenases / reductases accounts for sex pheromone evolution in Nasonia. Sci. Rep., 6:34697.

Linde, M., Peterhoff, D., Sterner, R. & Babinger, P. (2016).  Identification and characterization of heptaprenylglyceryl phosphate processing enzymes in Bacillus subtilis. J. Biol. Chem  291,14861-70.

Busch, F., Rajendran, C., Heyn, K., Schlee, S., Merkl, R. & Sterner, R. (2016). Ancestral tryptophan synthase reveals functional sophistication of primordial enzyme complexes. Cell Chem. Biol. 23, 709-715.

Plach, M. G., Reisinger, B., Sterner, R. &  Merkl, R. (2016). Long-term persistence of bi-functionality contributes to the robustness of microbial life through exaptation. PLoS Genet. 12, e1005836.

Plach, M. G., Löffler, P., Merkl, R. & Sterner, R. (2015). Conversion of anthranilate synthase into isocorismate synthase: implications for the evolution of chorismate-utilizing enzymes. Angew. Chem. Int. Ed. Engl. 54, 11270-11274.

Ece S., Evran, S., Janda, J. O. Merkl, R. & Sterner, R. (2015).  Improving thermal and detergent stability of Bacillus stearothermophilus neopullulanase by rational enzyme design. Protein Eng Des Sel 28, 147-151.

Woriedh, M., Merkl, R. & Dresselhaus, T. (2015). Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells. J .Exp. Bot. 66, 5205-5216.

Filarsky, M., Zillner, K., Araya, I., Villar-Garea, A., Merkl, R., Längst, G. & Németh, A. (2015). The extended AT-hook is a novel RNA binding motif. RNA Biol. 12, 864-876.

Schneider, D., Kaiser, W., Stutz, C., Holinski, A., Mayans, O. & Babinger, P. (2015).  YbiB from Escherichia coli, the defining member of the novel TrpD2 family of prokaryotic DNA-binding proteins. J .Biol.Chem. 290, 19527-19539.


2014 - 2013

Diermeier, S., Kolovos, P., Heizinger, L., Schwartz, U., Georgomanolis, T., Zirkel, A., Wedemann, G., Grosveld, F., Knoch, T. A., Merkl, R., Cook, P. R., Längst, G. & Papantonis, A. (2014). TNAα signalling primes chromatin for NF-kB binding and induces rapid and widespread nucleosome repositioning. Genome Biol. 15, 536.

Hauptmann, J., Kater, L., Löffler, P., Merkl, R.  & Meister, G. (2014). Generation of catalytic human Ago4 identifies structural elements important for RNA cleavage. RNA 20, 1532-1538.

Blaul, B., Steinbauer, R., Merkl. P., Merkl, R., Tschochner, H. & Ruther, J. (2014). Oleic acid is a precursor of linoleic acid and the male sex pheromone in Nasonia vitripennis. Insect. Biochem. Mol. Biol. 51, 33-40.

Janda, J. O., Popal, A., Bauer, J., Busch, M., Klocke, M., Spitzer, W., Keller, J. & Merkl, R. (2014). H2rs: deducing evolutionary and functionally important residue positions by means of an entropy and similarity based analysis of multiple sequence alignments. BMC Bioinformatics 15, 118.

Loedige, I., Stotz, M., Qamar, S., Kramer, K., Hennig, J., Schubert, T., Löffler, P., Merkl, R., Urlaub, H. & Meister, G. (2014). The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation. Genes Dev. 28, 749-764.

Busch, F., Rajendran, C., Mayans, O. Löffler, P., Merkl, R. & Sterner, R. (2014). TrpB2 Enzymes are O-Phospho-L-serine Dependent Tryptophan. Biochemistry 53, 6078-6083.

Peterhoff, D., Beer, B., Rajendran, C., Kumpula, E.P., Kapetaniou, E., Guldan, H., Wierenga, R.K., Sterner, R. & Babinger, P. (2014). A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization. Mol. Microbiol. 92, 885-899.

Sommer, B., Waege, I., Pöllmann, D., Seitz, T., Thomm, M., Sterner, R. & Hausner, W. (2014). Activation of a chimeric Rpb5/RpoH subunit using library selection. PLoS One 9, e87485.

Reisinger, B.,  Kuzmanovic, N., Löffler, P., Merkl, R., König, B. & Sterner, R. (2014). Expoiting protein symmetry to design light-controllable enzyme inhibitors. Angew. Chem. Int. Ed. 53, 595-598.

Reisinger, B.,  Sperl, J., Holinski, A., Schmid, V., Rajendran, C., Carstensen, L., Schlee, S., Blanquart, S., Merkl, R. & Sterner, R. (2014). Evidence for the existence of elaborate enzyme complexes in the paleoarchean era. J. Am. Chem. Soc. 136, 122-129.

Janda, J. O., Meier, A. & Merkl, R. (2013). CLIPS-4D: a classifier that distinguishes structurally and functionally important residue-positions based on sequence and 3D data. Bioinformatics 29, 3029-3035.

Sperl, J. M., Rohweder, B., Rajendran, C. & Sterner, R. (2013). Establishing catalytic activity on an artificial (βα)8-barrel protein designed from identical half-barrels. FEBS Lett.. 587, 2798-2805.

Meier, M.M., Rajendran, C., Malisi, C., Fox, N.G., Xu, C., Schlee, S., Barondeau, D.P. Hoecker, B., Sterner, R. & Raushel, F.M. (2013). Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template. J. Am. Chem. Soc. 135, 11670-11677.

Hauptmann, J., Dueck, A., Harlander, S., Pfaff, J., Merkl, R. & Meister, G. (2013). Turning catalytically inactive human Argonaute proteins into active slicer enzymes. Nat. Struct. Mol. Biol. 20, 814-817.

Schlee, S., Dietrich, S., Kurcon, T., Delaney, P., Goodey, N.M. & Sterner, R. (2013). Kinetic mechanism of indole-3-glycerol phosphate synthase. Biochemistry 52, 132-142.

2012 - 2011

List, F., Vega, M. C., Razeto, A., Haeger, M. C., Sterner, R. & Wilmanns, M. (2012). Catalysis uncoupling in a glutamine amidotransferase bienzyme by unblocking the glutaminase active site. Chem. Biol. 19, 1589-1599.

Reisinger, B.,  Bocola, M., List, F., Claren, J., Rajendran, C. & Sterner, R. (2012). A sugar isomerization reaction established on various (βα)8 -barrel scaffolds is based on substrate-assisted catalysis. Protein Eng. Des. Sel. 11, 751-760.

Carstensen, L., Sperl, J. M., Bocola, M., List, F., Schmid, F. X. & Sterner, R. (2012). Conservation of the folding mechanism between designed primordial (βα)8-barrel proteins and their modern descendant. J. Am. Chem. Soc. 134, 12786-12791.

Dietrich, S., Borst, N., Schlee, S., Schneider, D., Janda, J. O., Sterner, R. & Merkl, R. (2012). Experimental assessment of the importance of amino acid positions identified by an entropy-based correlation analysis of multiple sequence alignments. Biochemistry 51, 5633-5641.

Peterhoff, D., Zellner, H., Gudan, H., Merkl, R., Sterner, R. & Babinger, P. (2012).  Dimerization determines substrate specificity of a bacterial prenyltransferase. ChemBioChem 13, 1297-1303.

Evran, S., Telefoncu, A. & Sterner, R. (2012). Directed evolution of (βα)8-barrel enzymes: establishing phosphoribosylanthranilate isomerisation activity on the scaffold of the tryptophan synthase α-subunit. Protein Eng. Des. Sel. 25, 285-293.

Craig, D. B., Schwab, T. & Sterner, R. (2012). Random mutagenesis suggests that sequence errors are not a major cause of variation in the activity of individual

molecules of β-galactosidase. Biochem. Cell Biol. 90, 540-547.

Carstensen, L., Zoldák, G., Schmid, F. X. & Sterner, R. (2012). Folding mechanism of an extremely thermostable (βα)8-barrel enzyme: a high kinetic barrier protects the protein from denaturation. Biochemistry 51, 3420-3432.

List, F., Bocola, M., Haeger, M. C. & Sterner, R. (2012). Constitutively active glutaminase variants provide insights into the activation mechanism of anthranilate synthase. Biochemistry 51, 2812-2818.

Guldan, H., Matysik, F. M., Bocola, M., Sterner, R. & Babinger, P. (2011). Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria. Angew. Chem. Int. Ed. Engl. 50, 8188-8191.

Fischer, A., Seitz, T., Lochner, A., Sterner, R., Merkl, R. & Bocola, M. (2011). A fast and precise approach for computational saturation mutagenesis and its experimental validation by using an artificial (βα)8-barrel protein. ChemBioChem 12, 1544-1550.

Schwab, T. & Sterner, R. (2011). Stabilization of a metabolic enzyme by library selection in Thermus thermophilus. ChemBioChem  12, 1581-1588.


2010 - 2009

Ehrmann, A., Richter, K., Busch, F., Reimann, J., Albers, S.V. & Sterner, R. (2010). Ligand-inducted formation of a transient tryptophan synthase complex with αββ subunit stoichiometry. Biochemistry 49, 10842-10853.

 B Mandach, C. & Merkl R. (2010) Genes optimized by evolution for accurate and fast translation encode in Archaea and Bacteria a braod and characteristic spectrum of protein functions. MC Genomics 11, 617.

Seitz, T., Thoma, R., Schoch, G.A., Stihle, M., Benz, J., D'Arcy, B., Wiget, A., Ruf, A., Hennig, M. & Sterner, R. (2010). Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening. J. Mol. Biol. 403, 562-577.

Liebold, C., List, F., Kalbitzer, H.R., Sterner, R. & Brunner, E. (2010). The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy.  Protein Sci. 19, 1774-1782.

Richter, M., Bosnali, M., Carstensen, L., Seitz, T., Durchschlag, H., Blanquart, S., Merkl, R. & Sterner, R. (2010). Computational and experimental evidence for the evolution of a (βα)8-barrel protein from an ancestral quarter-barrel stabilised by disulfide bonds.  J. Mol. Biol. 398, 763-773.

Drzewiecki, K., Angelov, A., Ballschmiter, M. Tiefenbach, K.-J., Sterner, R. & Liebl, W. (2010) Hyperthermostable acetyl xylan esterase. Microbial Biotechnol. 3, 84-92.

Merkl R, Wiezer A. (2009) GO4genome: A prokaryotic phylogeny based on genome organization. J. Mol. Evol. 68, 550-562.

Schlee, S., Deuss, M., Bruning, M., Ivens, A., Schwab, T., Hellmann, N., Mayans, O. & Sterner, R. (2009). Activation of anthranilate phosphoribosyl transferase from Sulfolobus solfataricus by removal of Mg-inhibition and acceleration of product release. Biochemistry 48, 5199-5209.

Claren, J., Malisi, C., Höcker, B. & Sterner, R. (2009). Establishing wild-type levels of catalytic activity on natural and artificial (βα)8-barrel protein scaffolds.  Proc. Natl. Acad. Sci. USA 106, 3704-3709.

Xiang, D. F., Kolb, P., Meier, M. M., Fedorov, E. V., Fedorov, A. A., Sterner, R., Almo S. C., Shoichet, B. K. & Raushel, F. M. (2009). Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans: A close relative of phosphotriesterase in the amidohydrolase family. Biochemistry 48, 2237-2247.

Fischer, A., Enkler, N., Neudert, G., Bocola, M., Sterner, R. & Merkl, R. (2009). TransCent: Computational enzyme design by transferring active sites and considering constraints relevant for catalysis. BMC Bioinformatics 10, 54.

Höcker, B., Lochner, A., Seitz, T., Claren, J. & Sterner, R. (2009). High-resolution crystal structure of an artificial (βα)8-barrel protein designed from identical half-barrels.  Biochemistry 48, 1145-1147.

2008 - 2006

Guldan, H., Sterner, R. & Babinger, P. (2008). Identification and Characterization of a Bacterial Glycerol-1-phosphate Dehydrogenase: Ni2+ -Dependent AraM from Bacillus subtilis. Biochemistry 47, 7376-7384.

Merkl, R. & Zwick, M. (2008). H2r:Identification of evolutionary important residues by means of an entropy based analysis of multiple sequence alignments. BMC Bioinformatics 9, 151.

Reetz, M. T., Rentzsch, M., Pletsch, A., Taglieber, A., Hollmann, F., Mondière, R. J. G., Dickmann, N., Höcker, B., Cerrone, S., Haeger, M. C. & Sterner, R. (2008). A Robust Protein Host for Anchoring Chelating Ligands and Organocatalysts. ChemBioChem 9, 552-564.

Schwab, T., Skegro, D., Mayans, O. & Sterner, R. (2008). A rationally designed monomeric variant of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus is as active as the dimeric wild-type enzyme but less thermostable. J. Mol. Biol. 376, 506-516.

Seitz, T., Bocola, M., Claren, J. & Sterner, R. (2007). Stabilization of a (βα)8-Barrel Protein Designed from Identical Half Barrels. J. Mol. Biol. 372, 114-129.

Merkl, R. (2007). Modelling the evolution of the archeal tryptophan synthase. BMC Evol Biol. 7, 59.

Merkl, R. (2006). AMIGOS: a method for the inspection of genomic organisation or structure and its application to characterise conserved gene arrangements. In Silico Biol. 6, 281-306.

Waack, S., Keller, O., Asper, R., Brodag, T., Damm, C., Fricke, W. F., Surovcik, K., Meinicke, P. & Merkl, R. (2006). Score-based prediction of genomic islands in prokaryotic genomes using hidden Markov models. BMC Bioinformatics 7, 142.

Merkl, R. (2006). A comparative categorization of protein function encoded in bacterial or archeal genomic islands. J Mol Evol. 62, 1-14.

Leopoldseder, S., Hettwer, S. & Sterner, R. (2006). Evolution of Multi-Enzyme Complexes: The Case of Tryptophan Synthase. Biochemistry 45, 14111-14119.

Marino, M., Deuss, M., Svergun, D., Konarev, P., Sterner, R. & Mayans, O. (2006). Structural and Mutational Analysis of Substrate Complexation by Anthranilate Phosphoribosyltransferase from Sulfolobus solfataricus. J. Biol. Chem. 281, 21410-21421.

2005 - 2003

Schneider, B., Knöchel, T., Darimont, B., Hennig, M., Dietrich, S., Babinger, K., Kirschner, K. & Sterner, R. (2005). Role of the N-terminal Extension of the (βα)8-Barrel Enzyme Indole-3-Glycerol Phosphate Synthase for its Fold, Stability and Catalytic Activity. Biochemistry 44, 16405-16412.

Vega, C., Zou, P., Fernandez, F., Murphy, G., Sterner, R., Popov, A. & Wilmanns, M. (2005). Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA-synthetase-like subunit. Mol. Microbiol. 55, 675-686.

Wiezer, A. & Merkl, R. (2005). A comparative categorization of gene flux in diverse microbial species. Genomics 86, 462-475.

Höcker, B., Claren, J. & Sterner, R. (2004). Mimicking enzyme evolution by generating new (βα)8-barrels from (βα)4-half-barrels. Proc. Natl. Acad. Sci. USA 101, 16448-16453.

Thiemann, V., Dönges, C., Prowe, S., Sterner, R. & Antranikian, G. (2004). Characterisation of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii. Arch. Microbiol. 182, 226-235.

Leopoldseder, S., Claren, J., Jürgens, C. & Sterner, R. (2004). Interconverting the catalytic activities of (βα)8-barrel enzymes from different metabolic pathways: sequence requirements and molecular analysis. J. Mol. Biol. 337, 871-879.

Meinicke, P., Tech, M., Morgenstern, B. & Merkl, R. (2004). Oligo kernels for datamining on biological sequences: a case study on prokaryotic translation initiation sites. BMC Bioinformatics 5, 169.

Veith, B., Herzberg, C., Steckel, S., Feesche, J., Maurer, K. H., Ehrenreich, P., Bäumer, S., Henne, A., Liesegang, H., Merkl, R., Ehrenreich, A. & Gottschalk, G. (2004). The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential. J Mol Microbiol Biotechnol. 7, 204-211.

Merkl, R. (2004). SIGI: score-based identification of genomic islands. BMC Bioinformatics 5, 22.

Henne, A., Brüggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Lienard, T., Gohl, O., Martinez-Arias, R., Jacobi, C., Starkuviene, V., Schlenczeck, S., Dencker, S., Huber, R., Klenk, H. P., Kramer W., Merkl, R., Gottschalk, G., & Fritz, H.J.(2004). The genome sequence of the extreme thermophile Thermus thermophilus. Nat. Biotechnol. 22, 547-553.

Helmstaedt, K., Heinrich, G., Merkl, R. & Braus, G. H. (2004). Chorismate mutase of Thermus thermophilus is a monofunctional AroH class enzyme inhibited by tyrosine. Arch Microbiol. 181, 195-203.

Tech, M. & Merkl, R. (2003). YACOP: Enhanced gene prediction obtained by a combination of existing methods. In Silico Biol. 3, 441-451.

Merkl, R. (2003). A survey of codon and amino acid frequency bias in microbial genomes focusing on translational efficiency. J Mol Evol. 57, 453-466.

Wiezer, A. & Merkl, R. (2003). secureBLAST. In Silico Biol. 3, 405-409.

Bruggemann, H., Baumer, S., Fricke, W. F., Wiezer, A., Liesegang, H., Decker, I., Herzber, C., Martinez-Arias, R., Merkl, R., Henne, A. & Gottschalk, G. (2003). The genome sequence of Clostridium tetani, the causative agent of tetanus disease. Proc Natl Acad Sci U S A 100, 1316-1321.

2002 - 2000

Henn-Sax, M., Thoma, R., Schmidt, S., Hennig, M., Kirschner, K. & Sterner, R. (2002). Two (βα)8-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates. Biochemistry 41, 12032-12042.

Hettwer, S. & Sterner, R. (2002). A novel tryptophan synthase β-subunit from the hyperthermophile Thermotoga maritima: quaternary structure, steady-state kinetics, and putative physiological role. J. Biol. Chem. 277, 8194-8201.

Douangamath, A., Walker, M., Beismann-Driemeyer, S., Vega-Fernandez, M.C., Sterner, S. & Wilmanns, M. (2002). Structural evidence for ammonia tunnelling across the (βα)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure 10, 185-193.

Höcker, B., Schmidt, S. & Sterner, R. (2002). A common evolutionary origin of two elementary enzyme folds. FEBS letters 510, 133-135.

Larbig, K. D., Christmann, A., Johann, A., Klockgether, J., Hartsch, T., Merkl, R., Wiehlmann, L., Fritz, H. J. & Tümmler, B. (2002). Gene islands integrated into tRNA(Gly) genes confer genome diversity on a Pseudomonas aeruginosa clone. J Bacteriol. 184, 6665-6680.

Deppenmeier, U., Johann, A., Hartsch, T., Merkl, R., Schmitz, R. A., Martinez-Arias, R., Henne, A., Wiezer, A., Bäumer, S., Jacobi, C., Brüggemann, H., Lienard, T., Christmann, A., Bömeke, M., Steckel, S., Bhattacharyya, A., Lykidis, A., Overbeek, R., Klenk, H. P., Gunsalus, R. P., Fritz, H. J. & Gottschalk, G. (2002). The genome of Methanosarcina mazei: evidence for lateral gene transfer between bacteria and archaea. J Mol Microbiol Biotechnol. 4, 453-461.

Beismann-Driemeyer, S. & Sterner, R. (2001). Imidazole glycerol phosphate synthase from Thermotoga maritima: Quaternary structure, steady-state kinetics and reaction mechanism of the bi-enzyme complex. J. Biol. Chem. 276, 20387-20996.

Höcker, B., Beismann-Driemeyer, S., Hettwer, S., Lustig, A. & Sterner, R. (2001). Dissection of a (βα)8-barrel enzyme into two folded halves. Nat. Struct. Biol. 8, 32-36.

Lang, D., Thoma, R., Henn-Sax, M., Sterner, R. & Wilmanns, M. (2000). Structural evidence for evolution of the  β/α barrel scaffold by gene duplication and fusion. Science 289, 1546-1550.

Jürgens, C., Strom, A., Wegener, D., Hettwer, S., Wilmanns, M. & Sterner, R. (2000). Directed evolution of a (βα)8-barrel enzyme to catalyze related reactions in two different metabolic pathways. Proc. Natl. Acad. Sci. USA 97, 9925-9930.

Thoma, R., Hennig, M., Sterner, R. & Kirschner, K. (2000). Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure 8, 265-276.


Merkl, R. & Sterner, R. (2016). Ancestral protein reconstruction: techniques and applications. Biol. Chem. 397, 1-21.

List, F., Sterner, R. & Wilmanns, M. (2011). Related (βα)8-barrel proteins in histidine and tryptophan biosynthesis: a paradigm to study enzyme evolution. ChemBioChem 12, 1487-1494.

Sterner, R. & Brunner, E. The relationship between catalytic activity, structural flexibility and conformational stability as deduced from the analysis of mesophilic - thermophilic enzyme pairs and protein engineering studies. In: F. Robb et al., eds., Thermophiles - Biology and Technology at High Temperatures, CRC Press, Boca Raton, London, New York, pp. 25-38, 2008.

Sterner, R. & Höcker, B. (2005). Catalytic versatility , stability, and evolution of the (βα)8-barrel enzyme fold. Chemical Reviews 105, 4038-4055.

Jaenicke, R. & Sterner, R. Life at high temperatures. In: M. Dworkin et al., eds., The Procaryotes: An Evolving Electronic Resource for the Microbiological Community, 3rd edition (Latest update release 3.9, March 2002), New York, Springer-Verlag, 2000.

Sterner, R. & Liebl, W. (2001). Thermophilic Adaptation of Proteins. Crit. Rev. Biochem. Mol. Biol. 63, 39-106.

Sterner, R., Merz, A., Thoma, R. & Kirschner, K. (2001). Phosphoribosyl anthranilate isomerase and indoleglycerol phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima. Meth. Enzymol. 331, 270-280.

Sterner, R. (2001). 4Fe-4S ferredoxin from Thermotoga maritima. Meth. Enzymol. 334, 23-30.

Höcker, B., Jürgens, C., Wilmanns, M. & Sterner, R. (2001). Stability, catalytic versatility and evolution of the (βα)8-barrel fold. Curr. Opin. Biotechnol. 12, 376-381.

Henn-Sax, M., Höcker, B., Wilmanns, M. & Sterner, R. (2001). Divergent evolution of (βα)8-barrel enzymes. Biol. Chem. 382, 1315-1317.



Prof. Dr. Reinhard Sterner

Institute of  Biophysics and Physical Biochemistry
Room Nr. E3_1.313


University of Regensburg
Universitätsstrasse 31
93053 Regensburg

Postal Address:
University of Regensburg
93040 Regensburg

Claudia Pauer
Room Nr. E3_1.311
Phone +49-941-943 3004
Fax +49-941-943 2813

Our Department is located in the first floor of the new building WNE3.

  1. Fakultät für Biologie und Vorklinische Medizin
  2. Faculty Research

Biochemistry II



The (βα)8-barrel fold