The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli

Biochemistry

Volumn 36, Issue 16, 1997, Pages 4925-4933

  Hunter, Therese ^a   Ikebukuro, Kazunori ^b   Bannister, William H ^a   Bannister, Joe V ^a,c   Hunter, Gary J ^a  

^a UNIVERSITY OF MALTA   (Malta)

^b UNIVERSITY OF TOKYO   (Japan)

^c CRANFIELD UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; SODIUM AZIDE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; DATA ANALYSIS; DNA DETERMINATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; HYDROGEN BOND; OLIGONUCLEOTIDE PROBE; OXIDATIVE STRESS; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CYSTEINE; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; RESTRICTION MAPPING; SERINE; STRUCTURE-ACTIVITY RELATIONSHIP; SUPEROXIDE DISMUTASE; TYROSINE;

ESCHERICHIA COLI;

EID: 0030888269     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9629541     Document Type: Article

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