Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo- and exonucleolytic cleavage

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 1, 1999, Pages 38-43

  Garforth, S J ^a   Ceska, T A ^a   Suck, D ^a   Sayers, J R ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ENDONUCLEASE; EXONUCLEASE; LYSINE; SINGLE STRANDED DNA;

ARTICLE; BACTERIOPHAGE T5; BINDING SITE; DNA REPLICATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROLYSIS; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DNA; DNA-BINDING PROTEINS; ENDODEOXYRIBONUCLEASES; EXODEOXYRIBONUCLEASE V; EXODEOXYRIBONUCLEASES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; LYSINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; T-PHAGES;

MAMMALIA;

EID: 0033524487     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.1.38     Document Type: Article

References (33)