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Journal of Bacteriology, September 2006, p. 6179-6183, Vol. 188, No. 17
0021-9193/06/$08.00+0     doi:10.1128/JB.00259-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Probing the Substrate Specificity of Aminopyrrolnitrin Oxygenase (PrnD) by Mutational Analysis

Jung-Kul Lee,1,6 Ee-Lui Ang,1 and Huimin Zhao1,2,3,4,5*

Departments of Chemical and Biomolecular Engineering,1 Chemistry,2 Bioengineering,3 Institute for Genomic Biology,4 Center for Biophysics and Computational Biology, University of Illinois, 600 South Mathews Avenue, Urbana, Illinois 61801,5 Department of Chemical Engineering, Konkuk University, 1 Hwayang-Dong, Gwangjin-Gu, Seoul, Korea, 143-7016

Received 19 February 2006/ Accepted 12 May 2006

Molecular modeling and mutational analysis (site-directed mutagenesis and saturation mutagenesis) were used to probe the molecular determinants of the substrate specificity of aminopyrrolnitrin oxygenase (PrnD) from Pseudomonas fluorescens Pf-5. There are 17 putative substrate-contacting residues, and mutations at two of the positions, positions 312 and 277, could modulate the enzyme substrate specificity separately or in combination. Interestingly, several of the mutants obtained exhibited higher catalytic efficiency (approximately two- to sevenfold higher) with the physiological substrate aminopyrrolnitrin than the wild-type enzyme exhibited.

* Corresponding author. Mailing address: Department of Chemical and Biomolecular Engineering, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801. Phone: (217) 333-2233. Fax: (217) 333-0750. E-mail: zhao5{at}uiuc.edu.

Journal of Bacteriology, September 2006, p. 6179-6183, Vol. 188, No. 17
0021-9193/06/$08.00+0     doi:10.1128/JB.00259-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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