Cleavage experiments with deoxythymidine 3',5'-bis-(p-nitrophenyl phosphate) suggest that the homing endonuclease I-PpoI follows the same mechanism of phosphodiester bond hydrolysis as the non-specific Serratia nuclease

FEBS Letters

Volumn 443, Issue 2, 1999, Pages 209-214

  Friedhoff, Peter ^a   Franke, Ingo ^a   Krause, Kurt L ^b   Pingoud, Alfred ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b UNIVERSITY OF HOUSTON   (United States)

Author keywords

Acid base catalysis; Active site; DNA entry nuclease; DNase; Homology; Sequence alignment

Indexed keywords

DEOXYRIBONUCLEASE I; NUCLEASE; ORGANOPHOSPHATE;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SERRATIA;

AMINO ACID SEQUENCE; DNA; ENDODEOXYRIBONUCLEASES; ENDORIBONUCLEASES; ESTERS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; INTRONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; THYMIDINE;

SERRATIA;

EID: 0033065134     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01660-3     Document Type: Article

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