Romas Kazlauskas (born 1956) studied chemistry at the Massachuetts Institute of Technology (Ph.D) and Harvard University (postdoc with George Whitesides). He worked at General Electric Company (1985-88) and McGill University, Montreal, Canada (1988-2003) and is currently a professor in Biochemistry, Molecular Biology and Biophysics at the University of Minnesota, Twin Cities. He is an expert in enantioselective organic synthesis using enzymes.
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Romas J. Kazlauskas
Professor, BMBB
 
Ph.D., MIT (1982)
Postdoc: Harvard U.
visiting prof.: Stuttgart U. ('95-'96), KTH Stockholm ('02-'03)
 
Contact Information:
 
Office: 174A Gortner Lab
 
Phone: (612) 624-5904
Email: rjk@umn.edu
 
Laboratory: 174 Gortner Lab
Phone: (612) 624-5960

Publications

Research Group

 

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Romas J. Kazlauskas [ Back ]

 
  Romas J. Kazlauskas
Research Interests
 
Stereoselective Enzymatic Reactions

 

What's new?
• Kazlauskas to collaborate on a World Class University project at Seoul National University on "Biorefining Aromatic Feedstocks from Lignin"

• J. Gorke, Ph.D. student supervised by F. Srienc (Chem. Eng.) and R. Kazlauskas won a Kenneth G. Hancock Memorial Award for outstanding student contributions to green chemistry.

• Kazlauskas joins international advisory board for new European journal ChemCatChem, which covers homogeneous, heterogeneous and biocatalysis. The journal launches in Fall 2009.

Research Description

Biocatalysis uses enzymes for synthesis of drugs, chemical intermediates & biofuels. Enzymes are nature’s catalysts evolved for efficient biochemistry. Applying these enzymes to current chemical problems minimizes pollution and the use of toxic and non-selective chemical reagents. Some examples of current research:

• How to efficiently produce peroxycarboxylic acids with enzymes? A solution would be a green contribution to organic synthesis and could be used to make the next generation of biofuels (remove lignin from lignocellulosic biomass).

• How do acyl transferases exclude water from their active sites? An understanding would provide insight into antibiotic synthesis and new methods to make esters and biodegradable polyesters.

• How do enzymes evolve to catalyze a new reaction? An understanding will help understand why enzymes are such efficient catalysts and create new catalysts for synthesis, including catalysts that could catalyze reactions not found in biochemistry.

Research may involve travel to collaborating laboratories in Greifswald, Germany or Nara, Japan. Students can join NIH Training Grants in Chemical Biology or in Biotechnology.


Selected Publications

Q. Jing, K. Okrasa, R. J. Kazlauskas. "Stereoselective hydrogenation of olefins using rhodium-substituted carbonic anhydrase - a new reductase" Chem. Eur. J. 2009, 15, 1370-1376. more...

Q. Jing, K. Okrasa, R. J. Kazlauskas, "Manganese-substituted a-carbonic anhydrase as an enantioselective peroxidase" Topics Organometall. Chem. 2008. more...

C.K. Savile, R. J. Kazauskas, "Protease-catalyzed resolutions using the 3-(3-pyridine) propionyl anchor group: p-toluenesulfonamide" in Practical Methods in Biocatalysis and Biotransformations, Whittall, J.; P., Eds., 2008, submitted.

K. Okrasa, R. J. Kazlauskas, “Manganese carbonic anhydrase as an enantioselective epoxidation of olefins with hydrogen peroxide” Chem. Eur. J. 2006, 11, 1587-1596. more...

C. K. Savile, V. P. Magloire, R. J. Kazlauskas, “Subtilisin-catalyzed resolution of N-acyl arylsulfinamides” J. Am. Chem. Soc. 2005, 127, 2104-2113. more...

S. Park, K. Morley, G. P. Horsman, M. Holmquist, K. Hult, R. J. Kazlauskas, “Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than random mutagenesis” Chem. Biol., 2005, 12, 45-54. more...

U. T. Bornscheuer, R. J. Kazlauskas, “Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways” Angew. Chem. Intl. Ed. 2004, 43, 6032-6040. more...

S. Park, R. J. Kazlauskas “Biocatalysis in ionic liquids – advantages beyond green technology” Curr. Opin. Biotechnol. 2003, 14, 432-437. more...

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