Identification of tegions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosis

Saxena, Rahul ; Chakraborti, Pradip K. (2005) Identification of tegions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosis Journal of Bacteriology, 187 (23). pp. 8216-8220. ISSN 0021-9193

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Official URL: http://jb.asm.org/cgi/content/abstract/187/23/8216

Related URL: http://dx.doi.org/10.1128/JB.187.23.8216-8220.2005

Abstract

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.

Item Type:Article
Source:Copyright of this article belongs to American Society for Microbiology.
ID Code:60372
Deposited On:08 Sep 2011 14:37
Last Modified:08 Sep 2011 14:37

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