Trans Cooperativity by a Split DNA Recombinase: The Central and Catalytic Domains of Bacteriophage Lambda Integrase Cooperate in Cleaving DNA Substrates When the Two Domains Are not Covalently Linked

Journal of Molecular Biology

Volumn 370, Issue 2, 2007, Pages 303-314

  Subramaniam, Srisunder ^a   Kamadurai, Hari B ^a   Foster, Mark P ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

lambda integrase; NMR; single turnover kinetics; suicide substrate; tyrosine recombinase

Indexed keywords

DNA; INTEGRASE; LAMBDA INTEGRASE; RECOMBINASE; UNCLASSIFIED DRUG; VIRUS ENZYME;

ARTICLE; BACTERIOPHAGE LAMBDA; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; COVALENT BOND; DNA BINDING; DNA CLEAVAGE; DNA SEQUENCE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENE MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; TRANSACTIVATION;

ENTEROBACTERIA PHAGE LAMBDA;

EID: 34249712504     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.024     Document Type: Article

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