Histidine 265 is important for covalent catalysis by vaccinia topoisomerase and is conserved in all eukaryotic type I enzymes

Journal of Biological Chemistry

Volumn 272, Issue 7, 1997, Pages 3891-3896

  Petersen, Birgitte Ø ^a   Shuman, Stewart ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA TOPOISOMERASE; DOUBLE STRANDED DNA; HISTIDINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; COVALENT BOND; ENZYME BINDING; ENZYME MECHANISM; EUKARYOTE; PRIORITY JOURNAL; PROTEIN METABOLISM; VACCINIA VIRUS;

AMINO ACID SEQUENCE; ASPARAGINE; BASE SEQUENCE; CATALYSIS; CONSERVED SEQUENCE; DNA; DNA TOPOISOMERASES, TYPE I; GLUTAMINE; HISTIDINE; HYDROLYSIS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; VACCINIA VIRUS;

EID: 0031058037     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.7.3891     Document Type: Article

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