Thermostability of manganese- and iron-superoxide dismutases from escherichia coli is determined by the characteristic position of a glutamine residue

European Journal of Biochemistry

Volumn 269, Issue 21, 2002, Pages 5137-5148

  Hunter, Thérèse ^a   Bannister, Joe V ^a,b   Hunter, Gary J ^a  

^a UNIVERSITY OF MALTA   (Malta)

^b CRANFIELD UNIVERSITY   (United Kingdom)

Author keywords

Metal specificity; Site directed mutagenesis; Superoxide dismutase; Thermostability

Indexed keywords

BACTERIAL ENZYME; GLUTAMINE; IRON; ISOENZYME; MANGANESE; METAL; SUPEROXIDE DISMUTASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PHYSICAL CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; WILD TYPE;

ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; GLUTAMINE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; IRON; MANGANESE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDANTS; OXIDATIVE STRESS; PARAQUAT; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SODIUM AZIDE; SUPEROXIDE DISMUTASE; TEMPERATURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036428548     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03200.x     Document Type: Article

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