Glycine in the conserved motif III modulates the thermostability and oxidative stress resistance of peptide deformylase in Mycobacterium tuberculosis

FEMS Microbiology Letters

Volumn 320, Issue 1, 2011, Pages 40-47

  Narayanan, Sai Shyam ^a   Sokkar, Pandian ^b   Ramachandran, Murugesan ^b   Nampoothiri, Kesavan Madhavan ^a  

^a REGIONAL RESEARCH LABORATORY CSIR   (India)

^b MADURAI KAMARAJ UNIVERSITY   (India)

Author keywords

Mycobacterium tuberculosis; Oxidative stress stability; Peptide deformylase; Site directed mutagenesis; Thermostability

Indexed keywords

GLYCINE; HYDROGEN PEROXIDE; PEPTIDE DEFORMYLASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN MOTIF 3; PROTEIN PURIFICATION; RESIDUE ANALYSIS; THERMOSTABILITY;

AMIDOHYDROLASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CONSERVED SEQUENCE; ENZYME STABILITY; GLYCINE; KINETICS; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; OXIDATIVE STRESS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS;

EID: 79957918284     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02289.x     Document Type: Article

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