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Institute for Biophysics and physical Biochemistry

Biochemistry II




Busch M.R., Drexler L., Mahato D.R., Hiefinger C., Osuna S., Sterner R. (2023)
Retracing the Rapid Evolution of an Herbicide-Degrading Enzyme by Protein Engineering
ACS Catal. 13, 15558-15571

Busch M., Rajendran C., Sterner R. (2023)
Structural and Functional Characterization of the Ureidoacrylate Amidohydrolase RutB from Escherichia coli
Biochemistry 62, 863-872

Kinateder* T., Drexler* L., Straub K., Merkl R., Sterner R. (2023)
Experimental and computational analysis of the ancestry of an evolutionary young enzyme from histidine biosynthesis
Protein Sci. 32, e4536

Hiefinger* C., Mandl* S., Wieland* M., Kneuttinger A. (2023)
Chapter Eight - Rational design, production and in vitro analysis of photoxenoproteins
In Methods in Enzymology: Integrated Methods in Protein Biochemistry: PartC edited by A. K. Shukla, 247-288 

*contributed equally


Bhagat A.K., Schlee S., Straub K., Nazet J., Luckner P., Bruckmann A., Sterner R. (2022)
Photoswitching of Feedback Inhibition by Tryptophan in Anthranilate Synthase
ACS Synth. Biol. 11, 2846–2856

Kneuttinger A.C. (2022)
A guide to designing photocontrol in proteins: methods, strategies and applications
Biol. Chem. 403, 573-613

Kropp C., Bruckmann A., Babinger P. (2022)
Controlling Enzymatic Activity by Modulating the Oligomerization State via Chemical Rescue and Optical Control
ChemBioChem 23, e202100490


Kneuttinger A.C., Sterner R. (2021)
The Structure of Carbamoylphosphate Synthetase Unravels Central
Functional Features of a Key Metabolic Multienzyme Complex

Biochemistry 60, 3422–3423

Maria-Solano M.A., Kinateder T., Iglesias-Fernández J., Sterner R., Osuna S.  (2021)
In silico identification and experimental validation of distal activity-enhancing mutations in tryptophan synthase.
ACS Catal. 11, 13733–13743

Nazet J., Lang E., Merkl R.  (2021)
Rosetta:MSF:NN: Boosting performance of multi-state computational protein design with a neural network.
PLoS ONE 16, e025669

Heizinger L., Merkl R.  (2021)
Evidence for the preferential reuse of sub-domain motifs in primordial protein folds.
Proteins 89, 1167–1179

Wurm J.P., Sung S., Kneuttinger A.C., Hupfeld E., Sterner E., Wilmanns M., Sprangers R.  (2021)
Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
Nat. Commun. 12, 2748

Schmitz S., Ertelt M., Merkl R., Meiler J. (2021)
Rosetta design with co-evolutionary information retains protein function.
PLoS Comput Biol. 17, e1008568

Kropp C., Straub K., Linde M., Babinger P. (2021) 
Hexamerization and thermostability emerged very early during geranylgeranylglyceryl phosphate synthase evolution.
Protein Sci. 30, 583-596

Hertle R., Nazet J., Semmelmann F., Schlee S., Funke F., Merkl R., Sterner R. (2021).
Reprogramming the Specificity of a Protein Interface by Computational and Data-Driven Design.
Structure 29, 292-304

Simeth N.A., Kinateder T., Rajendran C., Nazet J., Merkl R., Sterner R., König B., Kneuttinger A.C. (2021).
Towards Photochromic Azobenzene-Based Inhibitors for Tryptophan Synthase.
Chem. - Eur. J. 27, 2439-2451


Hasler D., Meduri R., Bak M., Lehmann G., Heizinger L., Wang X., Li Z., Sement F., Bruckmann A., Dock-Bregeon A., Merkl R., Kalb R., Grauer E., Kunstmann E., Zavolan M., Liu M., Fischer U., Meister G. (2020).
The Alazami syndrome-associated protein LARP7 guides U6 small nuclear RNA modification and contributes to splicing robustness.
Mol Cell 77, 1014-1031

Norris A., Busch F.,  Schupfner M., Sterner R., Wysocki V. (2020).
Quaternary structure of the tryptophan synthase α-subunit homolog BX1 from Zea mays.
J Am Soc Mass Spectrom 31, 227-233

Esch R., Merkl R. (2020).
Conserved genomic neighborhood is a strong but no perfect indicator for a direct interaction of microbial gene products.
BMC Bioinformatics 21, 5

Kneuttinger A., Rajendran C., Simeth N., Bruckmann A., König B., Sterner R. (2020).
Significance of the protein interface configuration for allostery in imidazole glycerol phosphate synthase.                                                                                           Biochemistry 59, 2729-2742

Schupfner M., Straub K., Busch F.,  Merkl R., Sterner R. (2020).
Analysis of allosteric communication in a multienzyme complex by ancestral sequence reconstruction.
Proc. Natl. Acad. Sci. U.S.A. 117, 346-354


Kneuttinger A.C., Straub K., Bittner P., Simeth N.A., Bruckmann A., Busch F., Rajendran, C., Hupfeld E., Wysocki V.H., Horinek D., König B., Merkl R., Sterner R. (2019).
Light-Regulation of enzyme allostery through photo-responsive unnatural amino acids.
Cell Chem. Biol. 26, 1501-1514

Kneuttinger A.C., Zwisele S., Straub K., Bruckmann A., Busch F., Kinateder T., Gaim B., Wysocki V.H., Merkl R., Sterner R. (2019).
Light-Regulation of Tryptophan synthase by combining protein design and enzymology.
Int. J. Mol. Sci. 20, (20)

Rohweder B., Lehmann G., Eichner N., Polen T., Rajendran C., Ruperti F., Linde M., Treiber T., Jung O., Dettmer K., Meister G., Bott M., Gronwald W., Sterner R. (2019).
Library selection with a randomized repertoire of (βα)8-barrel enzymes results in unexpected induction of gene expression.                                                         Biochemistry 58, 4207-4217

Straub K., Linde M., Kropp C., Blanquart S., Babinger P., Merkl R. (2019).
Sequence selection by FitSS4ASR alleviates ancestral sequence reconstruction as exemplified for geranylgeranylglyceryl phosphate synthase.
Biol. Chem. 400, 367-381

Schlee S., Straub K., Schwab T., Kinateder T., Merkl R., Sterner R. (2019).
Prediction of quaternary structure by analysis of hot spot residues in protein-protein interfaces: the case of anthranilate phosphoribosyltransferases.
Proteins 87, 815-825

Semmelmann F., Kabeya N., Malcicka M., Bruckmann A., Broschwitz B., Straub K., Merkl R., Monroig O., Sterner R., Ruther J., Ellers J. (2019).
Functional characterisation of two delta 12-desaturases demonstrates targeted production of linoleic acid as pheromone precursor in Nasonia.                            J.Exp.Biol. 222, (Pt 10)

Semmelmann F., Hupfeld E., Heizinger L., Merkl R., Sterner R. (2019).
A fold-independent interface residue is crucial for complex formation and allosteric signaling in class I glutamine amidotransferases.                                    Biochemistry 58, 2584-2588

Semmelmann F., Straub K., Nazet J., Rajendran C., Merkl R., Sterner R. (2019).
Mapping the allosteric communication networt of aminodeoxychorismate synthase.
 J. Mol. Biol. 431, 2718-2728

Schupfner M., Busch F., Wysocki V., Sterner R. (2019).
Generation of a stand-alone tryptophan synthase α-subunit by mimicking an evolutionary blueprint.
Chembiochem 20, 2747-2751

Semmelmann F., Hofferberth J., Ruther J., Sterner R. (2019).
Mapping key amino acid residues for the epimerase efficiency and stereospecificity of the sex pheromone biosynthetic short-chain dehydrogenases/reductases of Nasonia.
Sci Rep 9, (1)

Straub K., Merkl R. (2019).
Ancestral sequence reconstruction as a tool for the elucidation of a stepwise evolutionary adaptation.
Methods Mol. Biol.  1851, 171-182

Plössl K., Straub K., Schmid V., Strunz F., Wild J., Merkl R., Weber B.H.F., Friedrich U. (2019).
Identification of the retinoschisin-binding site on the retinal Na/K-ATPase.
PLos One  14, (5)

Schwartz U., Németh A., Diermeier S., Exler J.H., Hansch S., Maldonado R., Heizinger L.,  Merkl R., Längst G. (2019).
Characterizing the nuclease accessibility of DNA in human cells to map higher order structures of chromatin.
Nucleic Acids Res. 47, 1239-1254

Hoffmeister H., Fuchs A., Strobl L., Sprenger F., Gröbner-Ferreira R., Michaelis S., Hoffmann P., Nazet J., Merkl R., Längst G. (2019).
Elucidation of the functional roles of the Q and I motifs in the human chromatin-remodeling enzyme BRG1.
J. Biol. Chem. 294, 3294-3310

Ziegler C., Graf J., Faderl S., Schedlbauer J., Strieder N., Förstl B., Spang R., Bruckmann A., Merkl R., Hombach S., Kretz M. (2019).
The long non-coding RNA LINC00941 and SPRR5 are novel regulators of human epidermal homeostasis.
EMBO Rep. 20, (2)


Pfab A., Bruckmann A., Nazet J., Merkl R., Grasser K.D. (2018).
The Adaptor Protein ENY2 Is a Component of the Deubiquitination Module of the Arabidopsis SAGA Transcriptional Co-activator Complex but not of the TREX-2 Complex.
J. Mol. Biol. 430, 1479-1494

Schwartz U., Németh A., Diermeier S., Exler J.H., Hansch S., Maldonado R., Heizinger L., Merkl R., Längst G. (2018).
Characterizing the nuclease accessibility of DNA in human cells to map higher order structures of chromatin.
Nucleic Acids Res. 47, 1239-1254

Schlee S., Klein T., Schumacher M., Nazet J., Merkl R., Steinhoff H., Sterner R. (2018).
Relationship of Catalysis and Active Site Loop Dynamics in the (βα)8-Barrel Enzyme Indole-3-glycerol Phosphate Synthase.
Biochemistry 57, 3265-3277

Claren J., Schwab T., Sterner R. (2018).
Library Generation and Auxotrophic Selection Assays in Escherichia coli and Thermus thermophilus.
Methods Mol. Biol. 1685, 333-345

Plössl K., Schmid V., Straub K., Schmid C., Ammon M., Merkl R., Weber B.H.F., Friedrich U. (2018).
Pathomechanism of mutated and secreted retinoschisin in X-linked juvenile retinoschisis.
Exp. Eye Res. 177, 23-34

Linde M., Heyn K., Merkl R., Sterner R., Babinger P. (2018).
Hexamerization of Geranylgeranylglyceryl Phosphate Synthase Ensures Structural Integrity and Catalytic Activity at High Temperatures.
Biochemistry 57, 2335-2348

Kneuttinger A.C., Winter M., Simeth N.A., Heyn K., Merkl R., König B., Sterner R. (2018).
Artificial Light Regulation of an Allosteric Bienzyme Complex by a Photosensitive Ligand.
Chembiochem 19, 1750-1757

Fleming J.R., Schupfner M., Busch F., Baslé A., Ehrmann A., Sterner R., Mayans O. (2018).
Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms for the Enzymatic Channeling of Indole.
J. Mol. Biol. 430, 5066-5079

Rohweder B., Semmelmann F., Endres C., Sterner R. (2018).
Standardized cloning vectors for protein production and generation of large gene libraries in Escherichia coli.
BioTechniques 64, 24-26


Löffler P., Schmitz S., Hupfeld E., Sterner R., Merkl R. (2017).
Rosetta:MSF: a modular framework for multi-state computational protein design.
PLoS Comput. Biol. 13, e1005600

Plach M.G., Semmelmann F., Busch F., Busch M., Heizinger L., Wysocki V.H., Merkl R., Sterner R. (2017).
Evolutionary diversification of protein-protein interactions by interface add-ons.
Proc. Natl. Acad. Sci. U.S.A. 114, E8333-E8342

Sterner R., Höcker B., Kolmar H. (2017).
Highlight issue: protein design.
Biol. Chem. 398, 1-2

Simeth N.A., Kneuttinger A.C., Sterner R., König B. (2017).
Photochromic coenzyme Q derivatives: switching redox potentials with light.
Chem Sci 8, 6474-6483

Antranikian G., Suleiman M., Schäfers C., Adams M.W.W., Bartolucci S., Blamey J.M., Birkeland N., Bonch-Osmolovskaya E., da Costa M.S., Cowan D., Danson M., Forterre P., Kelly R., Ishino Y., Littlechild J., Moracci M., Noll K., Oshima T., Robb F., Rossi M., Santos H., Schönheit P., Sterner R., Thauer R., Thomm M., Wiegel J., Stetter K.O. (2017).
Diversity of bacteria and archaea from two shallow marine hydrothermal vents from Vulcano Island.
Extremophiles 21, 733-742

Holinski A., Heyn K., Merkl R., Sterner R. (2017).
Combining ancestral sequence reconstruction with protein design to identify an interface hotspot in a key metabolic enzyme complex.
Proteins 85, 312-321


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, 709-15

Ruther J., Hagström Å.K., Brandstetter B., Hofferberth 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

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

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


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, 19527-39

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, 864-76

Plach M.G., Löffler P., Merkl R., Sterner R. (2015).
Conversion of anthranilate synthase into isochorismate synthase: implications for the evolution of chorismate-utilizing enzymes.
Angew. Chem. Int. Ed. Engl. 54, 11270-4

Woriedh M., Merkl R., Dresselhaus T. (2015).
Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells.
J. Exp. Bot. 66, 5205-16

Ece S., Evran S., Janda J., Merkl R., Sterner R. (2015).
Improving thermal and detergent stability of Bacillus stearothermophilus neopullulanase by rational enzyme design.
Protein Eng. Des. Sel. 28, 147-51


Peterhoff D., Beer B., Rajendran C., Kumpula E., 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, 885-99

Janda J., 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., Längst G., 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, 749-64

Busch F., Rajendran C., Mayans O., Löffler P., Merkl R., Sterner R. (2014).
TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases.
Biochemistry 53, 6078-83

Reisinger B., Kuzmanovic N., Löffler P., Merkl R., König B., Sterner R. (2014).
Exploiting protein symmetry to design light-controllable enzyme inhibitors.
Angew. Chem. Int. Ed. Engl. 53, 595-8

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

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

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, 122-9

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, 1532-8


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, 2798-805

Schlee S., Dietrich S., Kurćon T., Delaney P., Goodey N.M., Sterner R. (2013).
Kinetic mechanism of indole-3-glycerol phosphate synthase.
Biochemistry 52, 132-42

Meier M.M., Rajendran C., Malisi C., Fox N.G., Xu C., Schlee S., Barondeau D.P., Höcker B., Sterner R., Raushel F.M. (2013).
Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template.
J. Am. Chem. Soc. 135, 11670-7


Peterhoff D., Zellner H., Guldan H., Merkl R., Sterner R., Babinger P. (2012).
Dimerization determines substrate specificity of a bacterial prenyltransferase.
Chembiochem 13, 1297-303

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, 2812-8

List F., Vega M.C., Razeto A., Häger M.C., Sterner R., Wilmanns M. (2012).
Catalysis uncoupling in a glutamine amidotransferase bienzyme by unblocking the glutaminase active site.
Chem. Biol. 19, 1589-99

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, 285-93

Kropinski A.M., Van den Bossche A., Lavigne R., Noben J., Babinger P., Schmitt R. (2012).
Genome and proteome analysis of 7-7-1, a flagellotropic phage infecting Agrobacterium sp H13-3.
Virol. J. 9, 102

Dietrich S., Borst N., Schlee S., Schneider D., Janda J., 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, 5633-41

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, 540-7

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, 12786-91

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. 25, 751-60

Carstensen L., Zoldák G., Schmid F., Sterner R. (2012).
Folding mechanism of an extremely thermostable (βα)(8)-barrel enzyme: a high kinetic barrier protects the protein from denaturation.
Biochemistry 51, 3420-32


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, 1544-50

Guldan H., Matysik F., 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, 8188-91

Schwab T., Sterner R. (2011).
Stabilization of a metabolic enzyme by library selection in Thermus thermophilus.
Chembiochem 12, 1581-8

Fink F., Hochrein J., Wolowski V., Merkl R., Gronwald W. (2011).
PROCOS: computational analysis of protein-protein complexes.
J Comput Chem 32, 2575-86

Sterner R. (2011).
Directed evolution: a powerful approach to optimising and understanding enzymes.
Chembiochem 12, 1439-40

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, 1487-94


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, 1774-82

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 (beta alpha)8-barrel protein from an ancestral quarter-barrel stabilised by disulfide bonds.
J. Mol. Biol. 398, 763-73

Ehrmann A., Richter K., Busch F., Reimann J., Albers S., Sterner R. (2010).
Ligand-induced formation of a transient tryptophan synthase complex with αββ subunit stoichiometry.
Biochemistry 49, 10842-53

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


Xiang D.F., Kolb P., Fedorov A.A., Meier M.M., Fedorov L.V., Nguyen T.T., 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 superfamily.
Biochemistry 48, 2237-47

Claren J., Malisi C., Höcker B., Sterner R. (2009).
Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds.
Proc. Natl. Acad. Sci. U.S.A. 106, 3704-9

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

Schlee S., Deuss M., Bruning M., Ivens A., Schwab T., Hellmann N., Mayans O., Sterner R. (2009).
Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release .
Biochemistry 48, 5199-209

Höcker B., Lochner A., Seitz T., Claren J., Sterner R. (2009).
High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels.
Biochemistry 48, 1145-7


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, 506-16

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, 552-64

Burghardt T., Saller M., Gürster S., Müller D., Meyer C., Jahn U., Hochmuth E., Deutzmann R., Siedler F., Babinger P., Wirth R., Huber H., Rachel R. (2008).
Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus hospitalis: the major cytosolic and membrane proteins.
Arch. Microbiol. 190, 379-94

Guldan H., Sterner R., Babinger P. (2008).
Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.
Biochemistry 47, 7376-84

Sterner R., Merkl R., Raushel F.M. (2008).
Computational design of enzymes.
Chem. Biol. 15, 421-3


Seitz T., Bocola M., Claren J., Sterner R. (2007).
Stabilisation of a (betaalpha)8-barrel protein designed from identical half barrels.
J. Mol. Biol. 372, 114-29

Babinger P., Völkl R., Cakstina I., Maftei A., Schmitt R. (2007).
Maintenance DNA methyltransferase (Met1) and silencing of CpG-methylated foreign DNA in Volvox carteri.
Plant Mol. Biol. 63, 325-36


Marino M., Deuss M., Svergun D.I., Konarev P.V., Sterner R., Mayans O. (2006).
Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.
J. Biol. Chem. 281, 21410-21

Leopoldseder S., Hettwer S., Sterner R. (2006).
Evolution of multi-enzyme complexes: the case of tryptophan synthase.
Biochemistry 45, 14111-9


Vega M.C., Zou P., Fernandez F.J., Murphy G.E., 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, 675-86

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 (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity.
Biochemistry 44, 16405-12

Sterner R., Höcker B. (2005).
Catalytic versatility, stability, and evolution of the (betaalpha)8-barrel enzyme fold.
Chem. Rev. 105, 4038-55


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

Höcker B., Claren J., Sterner R. (2004).
Mimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels.
Proc. Natl. Acad. Sci. U.S.A. 101, 16448-53

Leopoldseder S., Claren J., Jürgens C., Sterner R. (2004).
Interconverting the catalytic activities of (betaalpha)(8)-barrel enzymes from different metabolic pathways: sequence requirements and molecular analysis.
J. Mol. Biol. 337, 871-9

Sterner R., Schmid F.X. (2004).
Biochemistry. De novo design of an enzyme.
Science 304, 1916-7

Thiemann V., Dönges C., Prowe S.G., Sterner R., Antranikian G. (2004).
Characterisation of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii.
Arch. Microbiol. 182, 226-35

Jakobiak T., Mages W., Scharf B., Babinger P., Stark K., Schmitt R. (2004).
The bacterial paromomycin resistance gene, aphH, as a dominant selectable marker in Volvox carteri.
Protist 155, 381-93


Tech M., Merkl R. (2003).
YACOP: Enhanced gene prediction obtained by a combination of existing methods.
In Silico Biol. (Gedrukt) 3, 441-51

Jaenicke R., Sterner R. (2003).
Protein design at the crossroads of biotechnology, chemistry, theory, and evolution.
Angew. Chem. Int. Ed. Engl. 42, 140-2

Wiezer A., Merkl R. (2003).
In Silico Biol. (Gedrukt) 3, 405-9


Hettwer S., Sterner R. (2002).
A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role.
J. Biol. Chem. 277, 8194-201

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., Gunsalus R.P., Fritz H., Gottschalk G. (2002).
The genome of Methanosarcina mazei: evidence for lateral gene transfer between bacteria and archaea.
J. Mol. Microbiol. Biotechnol. 4, 453-61

Henn-Sax M., Thoma R., Schmidt S., Hennig M., Kirschner K., Sterner R. (2002).
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates.
Biochemistry 41, 12032-42

Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., Sterner R., Wilmanns M. (2002).
Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex.
Structure 10, 185-93

Höcker B., Schmidt S., Sterner R. (2002).
A common evolutionary origin of two elementary enzyme folds.
FEBS Lett. 510, 133-5


Babinger P., Kobl I., Mages W., Schmitt R. (2001).
A link between DNA methylation and epigenetic silencing in transgenic Volvox carteri.
Nucleic Acids Res. 29, 1261-71

Sterner R., Merz A., Thoma R., Kirschner K. (2001).
Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima.
Meth. Enzymol. 331, 270-80

Beismann-Driemeyer S., Sterner R. (2001).
Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex.
J. Biol. Chem. 276, 20387-96

Höcker B., Beismann-Driemeyer S., Hettwer S., Lustig A., Sterner R. (2001).
Dissection of a (betaalpha)8-barrel enzyme into two folded halves.
Nat. Struct. Biol. 8, 32-6

Sterner R. (2001).
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 (beta alpha)(8)-barrel fold.
Curr. Opin. Biotechnol. 12, 376-81

Henn-Sax M., Höcker B., Wilmanns M., Sterner R. (2001).
Divergent evolution of (betaalpha)8-barrel enzymes.
Biol. Chem. 382, 1315-20

Sterner R., Liebl W. (2001).
Thermophilic adaptation of proteins.
Crit. Rev. Biochem. Mol. Biol. 36, 39-106


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, 265-76

Jürgens C., Strom A., Wegener D., Hettwer S., Wilmanns M., Sterner R. (2000).
Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.
Proc. Natl. Acad. Sci. U.S.A. 97, 9925-30

Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M. (2000).
Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion.
Science 289, 1546-50

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

Biochemistry II

The (βα)8-barrel fold