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Journal of Bacteriology, November 2005, p. 7543-7545, Vol. 187, No. 21
0021-9193/05/$08.00+0     doi:10.1128/JB.187.21.7543-7545.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Replacement of Tyrosine 181 by Phenylalanine in Gentisate 1,2-Dioxygenase I from Pseudomonas alcaligenes NCIMB 9867 Enhances Catalytic Activities

Chew Ling Tan,1 Chew Chieng Yeo,3 Hoon Eng Khoo,4 and Chit Laa Poh1,2*

Programme in Environmental Microbiology, Department of Microbiology, Faculty of Medicine, National University of Singapore, 5 Science Drive 2, Singapore 117597, Singapore,1 School of Biomedical Science, Curtin University of Technology, Bentley, Western Australia 6102, Australia,2 Department of Biotechnology, Malaysia University of Science and Technology, Block C, Dataran Usahawan Kelana, 17 Jalan SS7/26, 47301 Petaling Jaya, Malaysia,3 Department of Biochemistry, Faculty of Medicine, National University of Singapore, 5 Science Drive 2, Singapore 117597, Singapore4

Received 10 May 2005/ Accepted 6 August 2005

xlnE, encoding gentisate 1,2-dioxygenase (EC 1.13.11.4), from Pseudomonas alcaligenes (P25X) was mutagenized by site-directed mutagenesis. The mutant enzyme, Y181F, demonstrated 4-, 3-, 6-, and 16-fold increases in relative activity towards gentisate and 3-fluoro-, 4-methyl-, and 3-methylgentisate, respectively. The specific mutation conferred a 13-fold higher catalytic efficiency (kcat/Km) on Y181F towards 3-methylgentisate than that of the wild-type enzyme.

* Corresponding author. Present address: Programme in Environmental Microbiology, Department of Microbiology, Yong Loo Lin School of Medicine, National University of Singapore, 5 Science Drive 2, Singapore 117597. Phone: (65) 6874-3674. Fax: (65) 6776-6872. E-mail: micpohcl{at}nus.edu.sg.

Journal of Bacteriology, November 2005, p. 7543-7545, Vol. 187, No. 21
0021-9193/05/$08.00+0     doi:10.1128/JB.187.21.7543-7545.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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