title: Identification of regions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosis.
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 H(2)O(2).
authors.affiliation: Institute of Microbial Technology, Chandigarh, India.
authors.forename: Rahul
authors.initials: R
authors.lastname: Saxena
authors.forename: Pradip K
authors.initials: PK
authors.lastname: Chakraborti
mesh_terms: D000581:Amidohydrolases / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D004795:Enzyme Stability / Q000235:genetics; D016680:Genome, Bacterial; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment
chemical_list: D000581:Amidohydrolases; C084507:peptide deformylase