Zu Hauptinhalt springen
Startseite UR

Wird geladen...



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

Research

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.
 

Projects


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.

Team-Leaders

Alumni

Dr. Silke Beissmann-Driemeier

Jan 1998 - Jan 2001

Vera Röhlich

Juli 2000 - Juni 2001

Dr. Martina Henn-Sax

Sept 1998 - Dez 2001

Dr. Andreas Ivens

 Jan 2000 - Juni 2002

Dr. Stefan Hettwer

Apr 1998 - Sept 2002

Dr. Satoshi Akanuma

Juli 2001 - Feb 2003

Dr. Birte Höcker

Nov 1998 - Juni 2003

Dr. Manal Bosnali

Okt 2002 - März 2004

Natalie Heuer

Okt 2002 - März 2004

Simona Jansen

Juli 2000 - April 2004

Iris Lambeck

Dez 2003 - Dez 2004

Dr. Catharina Dönges

März 2000 - Jan 2005

Susanne Marquardt

April 2004 - März 2005

Birgit Schwarz

Dez 2003 - April 2005

Dr. Michaela Häger

Feb 2001 - Juni 2005

Dr. Karin Babinger

Juni 2005 - Okt 2005

Dr. Sonja Leopoldseder

2001 -  Jan 2006

Christian Bolz

Jan 2006 - Nov 2006

Maximilian Plank

Juni 2006 - Aug 2007

Lorella Ungar

Jan 2004 - Aug 2007

Matthias Zwick

Sep 2006 - Dez 2007

Dr. Markus Richter

Mai 2004 - Aug 2008

Dr. Jörg Claren

Nov 2004 - Dez 2008

Ulrike Eßlinger

Juni 2008 - Mai 2009

Daniel Roderer

Sep 2008 - Aug 2009

Bettina Sommer

Feb 2009 - Nov 2009

Dr. Felix List

Nov 2004 - März 2010

Dr. Alexander Ehrmann

Okt 2005 - Aug 2010

Dr. Tobias Seitz

April 2006 - Sept 2010

Nadine Borst

Jan 2010 - Sept 2010

Dr. Thomas Schwab

Jan 2006 - Dez 2010

Dr. Susanne Dietrich

Okt 2005 - Dez 2010

Dr. Harald Guldan

Feb 2007 - Juni 2011

Dr. Marco Bocola

Okt 2006 - Juli 2011

Dr. Hermann Zellner

April 2007 - Okt 2011

Barbara Beer

Mai 2011 - Mai 2012

Dr. Daniel Schneider

Dez 2006 - Mai 2012

Dr. Linn Carstensen

Okt 2008 - Juni 2012

Veronika Schmid

Jan 2012 - Sept 2012

Bastian Groitl

Jan 2012 - Sept 2012

Dr. Monika Meier

Feb 2008 - Jan 2013

Dr. Dietmar Birzer

März 2009 - Aug 2013

Dr. Josef Sperl

Aug 2009 - Aug 2013

Dr. David Peterhoff

Aug 2009 - Okt 2013

Dr. Bernd Reisinger

Aug 2009 - Juli 2014

Dr. Florian Busch

Jan 2010 - Aug 2015

Dr. Alexandra Holinski

Nov 2011 - Apr 2017
Dr. Patrick Löffler

Dez 2012 - Mai 2017

Dr. Maximilian Plach

Aug 2012 - Mai 2017

Dr. Wolfgang Kaiser

Jan 2013 - Sept 2017

Dr. Bettina Rohweder

Nov 2010 - März 2019

Publications

2019

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, 330

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

2018

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

2017

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

2016

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

2015

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

2014

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

2013

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

2012

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

2011

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

2010

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

2009

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

2008

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

2007

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

2006

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

2005

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

2004

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

2003

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).
secureBLAST.
In Silico Biol. (Gedrukt) 3, 405-9

2002

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

2001

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

2000

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

contact


Prof. Dr. Reinhard Sterner

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

Address:

University of Regensburg
Universitätsstrasse 31
93053 Regensburg

Postal Address:
University of Regensburg
93040 Regensburg

Secretary:
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

 

Hisa

The (βα)8-barrel fold