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Peter Macheroux

Open Positions
Open Position 4: Biochemical and physiological role of berberine bridge enzymes in Arabidopsis thaliana
Open Position 5: Biochemical and structural characterisation of members of the berberine bridge enzyme family
» »  Application info

Projects
Barbara Steiner: Structural and biochemical characterization of berberine bridge enzymes from Arabidopsis thaliana
Eveline Brodl: Structure-Function Relationships in Enzymes
Stefan  Etzl: Structural and biochemical characterization of light-activated cyclases
Shalinee Jha: Characterization of DPPIII knockout mice
Marina Toplak: Functional roles of the berberine bridge enzyme family in Arabidopsis thaliana
Geoffrey Gourinchas: Structure Function Studies of Photoactivated Diguanylate Cyclases
Emilia Strandback: Biochemical characterization of naturally occurring variants of NAD(P)H:quinone oxidoreductase 1

Closed projects
Silvia Wallner: Flavin-dependent plant oxidases
Sonja Sollner: Function and mechanism of Lot6p from Saccharomyces cerevisiae, a flavin-dependent quinone reductase
Andreas Winkler: Structure-Function studies on berberine bridging enzyme (BBE) from the California poppy (Eschscholzia californica)
Alexandra Binter: Enzymes of Nikkomycin Biosynthesis
Venugopal Gudipati: Structural and functional characterisation of the proteasomal complex with quinone reductase
Bastian Daniel: Expression and characterisation of novel archaeal, bacterial and eukaroytic flavoproteins
Chaitanya R  Tabib: Biochemistry and microbiology of photobacterial bioluminescence
Chanakan Tongsook: Exploration of the function of uncharacterized human proteins
Peter Augustin: Heterologous expression, purification and characterization of human flavoproteins

Further Information
Curriculum Vitae (47 kB)
Publication List (external Link)
Collaborators (56 kB)
Grants (51 kB)

 







Peter Macheroux
Institute of Biochemistry
Technische Universität Graz
Petersgasse 12/2
8010 Graz

e-Mail: peter.macheroux@tugraz.at
phone: +43 316 873 6450
fax: +43 316 873 6952
web: http://www.biochemistry.tugraz.at

Structure-Function Relationships in Enzymes

The focus of P. Macheroux’s research is to understand the functional role of amino acids in the active sites of enzymes with regard to substrate recognition and stereo- and regiospecificity of the chemical transformation. In addition, he is interested in substrate-triggered conformational changes and how enzymes utilize cofactors (flavin, NADPH, zinc) to achieve catalysis. He employs a multidisciplinary approach encompassing kinetic, thermodynamic, spectroscopic and structural techniques and the generation of variant enzymes in order to probe their functional role in substrate recognition and catalysis. He collaborates with partners in academia and industry to develop inhibitors for enzymes, which can yield important new insights into enzyme mechanisms and can be useful as potential lead compounds in the design of new drugs.

Laboratory know-how and infrastructure

The methods established in our laboratory comprise kinetic (stopped-flow and rapid quench analysis of enzymatic reactions), thermodynamic (isothermal titration microcalorimetry) and spectroscopic (fluorescence, circular dichroism and UV/Vis absorbance) methods. We also make frequent use of MALDI-TOF and ESI mass spectrometry. Protein purification techniques (chromatography and electrophoresis) are routine methods in our laboratory. Molecular biology methods are routinely used to clone and express target proteins in suitable host organisms.


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