Unusually wide co-factor tolerance in a metalloenzyme; divalent metal ions modulate edno-exonuclease activity in T5 exonuclease

Nucleic Acids Research

Volumn 29, Issue 13, 2001, Pages 2772-2779

  Garforth, Scott J ^a,b   Patel, Dipak ^a   Feng, Min ^a   Sayers, Jon R ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; COPPER ION; DOUBLE STRANDED DNA; ENDONUCLEASE; ENZYME; EXONUCLEASE; IRON; MAGNESIUM ION; MANGANESE; METAL ION; METALLOENZYME; NICKEL; PLASMID DNA; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BACTERIOPHAGE T5; BIOCHEMISTRY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

BASE SEQUENCE; BINDING SITES; CATALYSIS; CATIONS, DIVALENT; COENZYMES; ENDODEOXYRIBONUCLEASES; ENZYME ACTIVATION; EXODEOXYRIBONUCLEASES; KINETICS; MERCURY COMPOUNDS; METALS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PLASMIDS; POTASSIUM CHLORIDE; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; T-PHAGES;

ESCHERICHIA COLI; NEGIBACTERIA; T5 BACTERIOPHAGE; UNIDENTIFIED BACTERIOPHAGE;

EID: 0035394137     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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