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Journal of Bacteriology, December 2005, p. 8216-8220, Vol. 187, No. 23
0021-9193/05/$08.00+0     doi:10.1128/JB.187.23.8216-8220.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Identification of Regions Involved in Enzymatic Stability of Peptide Deformylase of Mycobacterium tuberculosis

Rahul Saxena and Pradip K. Chakraborti*

Institute of Microbial Technology, Sector 39A, Chandigarh 160 036, India

Received 2 May 2005/ Accepted 2 September 2005

Sequence analysis of peptide deformylase of Mycobacterium tuberculosis revealed the presence of insertions (residues 74 to 85) and an unusually long carboxy-terminal end (residues 182 to 197). Our results with deletion mutants indicated the contribution of these regions in maintaining enzymatic stability. Furthermore, we showed that the region spanning the insertions was responsible for maintaining resistance to oxidizing agents, like H2O2.

* Corresponding author. Mailing address: Institute of Microbial Technology, Sector 39A, Chandigarh 160 036, India. Phone: 91 172 2695215, ext. 452. Fax: 91 172 2690585. E-mail address: pradip{at}imtech.res.in.

Journal of Bacteriology, December 2005, p. 8216-8220, Vol. 187, No. 23
0021-9193/05/$08.00+0     doi:10.1128/JB.187.23.8216-8220.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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