Name:

Jiří Damborský

Affiliation:

Loschmidt Laboratories, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic

E-mail:

jiri@chemi.muni.cz

Web:

http://loschmidt.chemi.muni.cz/peg

Research:

structure-function relationships, evolution and engineering of dehalogenating enzymes

Short CV:

1994-1996 visiting scholar with J. Hermens, Utrecht University, The Netherlands; G. Sayler, University of Tennessee, USA; D. Hardman, University of Kent at Canterbury, UK and D. B. Janssen, Groningen University, The Netherlands
 
1997 Ph.D. with M. Němec, Masaryk University, Czech Republic; visiting scientist with P. Adriaens, University of Michigan, USA and M. Sjostroem, Umea University, Sweden
 
since 2003 Josef Loschmidt Professor of Chemistry at Faculty of Science, Masaryk University, Czech Republic
 

Awards:

1997 Young Microbiologist of the Year from the Czechoslovak Microbiological Society
 
1998 Award BIOTECH from the Czech Society for Biochemistry and Molecular Biology
 
2003 Alfred Bader Prize for Bioorganic Chemistry from the Czech Chemical Society
 

Editorship:

2001-2003 Environmental Toxicology and Chemistry, Member of Editorial Board
 
since 2003 Central European Journal of Chemistry, Editor
 
since 2003 FEMS Microbiology Reviews, Editor
 
since 2005 Biotechnology Journal, Member of Editorial Board
 

Publications:

Trantírek, L., Hynková, K., Nagata, Y., Murzin, A., Ansorgová, A., Sklenář, V., Damborský, J. Reaction Mechanism and Stereochemistry of γ-Hexachlorocyclohexane Dehydrochlorinase LinA. J. Biol. Chem. 276: 7734-7740 (2001).
 
Damborský, J., Prokop, M., Koča, J. TRITON: Graphic Software for Rational Engineering of Enzymes. Trends Biochem. Sci. 26: 71-73 (2001).
 
Prokop, Z., Monincová, M., Chaloupková, R., Klvaňa, M., Janssen, D.B., Nagata, Y., Damborský, J. Catalytic Mechanism of the Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26. J. Biol. Chem. 278: 45094-45100 (2003).
 
Chaloupková, R., Sýkorová, J., Prokop, Z., Jesenská, A., Monincová, M., Pavlová, M., Nagata, Y., Damborský, J. Modification of Activity and Specificity of Haloalkane Dehalogenase from Sphingomonas paucimobilis UT26 by Engineering of its Entrance Tunnel. J. Biol. Chem. 278: 52622-52628 (2003).
 
Oakley, A., Klvaňa, M., Otyepka, M., Nagata, Y., Wilce, M.C.J., Damborský, J. Crystal Structure of Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 Å Resolution. Biochemistry 43: 870-878 (2004).
 

Research interest:

Haloalkane dehalogenases are bacterial enzymes cleaving the carbon-halogen bond of the halogenated aliphatic compounds by a hydrolytic mechanism. These enzymes have become an important model system for investigation of fundamental principles of enzymatic catalysis, but also have potential use in detoxification of subsurface pollutants, recovery of industrial side products and biosensing. Modification of the substrate specificity and activity of these enzymes is required for optimisation of their catalytic properties. Our project focuses on the study of molecular mechanisms of enzymatic catalysis, structure-function relationships and engineering of haloalkane dehalogenases. The major objectives are: (i) to clone, isolate and characterise new dehalogenating enzymes, (ii) to understand the structural determinants of their catalytic activity and substrate specificity, (iii) to uncover molecular events leading to evolution of enzymes with novel substrate specificities, (iv) to design mutant proteins with modified catalytic properties using computer modelling techniques, (v) to construct these mutants using DNA-recombinant technologies and (vi) to characterise them structurally and functionally. The project will lead to the development of new theoretical approaches for computer-assisted protein design and construction of biocatalysts with modified catalytic properties.