Mechanistic study of CuZn-SOD from Ipomoea carnea mutated at dimer interface: Enhancement of peroxidase activity upon monomerization

Biochimie

Volumn 97, Issue 1, 2014, Pages 181-193

  Mishra, Panchanand ^a   Dixit, Anshuman ^a   Ray, Mamata ^a   Sabat, Surendra Chandra ^a  

^a INSTITUTE OF LIFE SCIENCES   (India)

Author keywords

Dimeric interface mutation; MD simulation; Peroxidase activity; Superoxide dismutase activity

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; DIETHYLDITHIOCARBAMIC ACID; DIMER; HYDROGEN PEROXIDE; LEUCINE; LYSINE; MONOMER; PEROXIDASE; PHENYLGLYOXAL;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; HIGH TEMPERATURE; IPOMOEA; IPOMOEA CARNEA; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; SITE DIRECTED MUTAGENESIS;

IPOMOEA CARNEA;

CATALYTIC DOMAIN; DITIOCARB; ESCHERICHIA COLI; GENE EXPRESSION; HYDROGEN PEROXIDE; IPOMOEA; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PEROXIDASE; PHENYLGLYOXAL; PLANT PROTEINS; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SUPEROXIDE DISMUTASE;

EID: 84891864443     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2013.10.014     Document Type: Article

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