Mechanism of NTP hydrolysis by the Escherichia coli primary replicative helicase DnaB protein. 2. Nucleotide and nucleic acid specificities

Biochemistry

Volumn 48, Issue 29, 2009, Pages 6730-6746

  Roychowdhury, Anasuya ^a   Szymanski, Michal R ^a   Jezewska, Maria J ^a   Bujalowski, Wlodzimierz ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC EFFECT; ALLOSTERIC SIGNAL; BASE COMPOSITION; BIMOLECULAR ASSOCIATION; CHEMICAL HYDROLYSIS; COFACTOR; COFACTORS; CONFORMATIONAL TRANSITIONS; DNA-BINDING; DNAB HELICASE; DNAB PROTEIN; ENERGY TRANSDUCTION; HELICASE; HYDROLYSIS RATE; KINETIC MECHANISM; PRODUCT COMPLEX; PURINE NUCLEOTIDES; RAPID QUENCH; SINGLE-STRANDED DNA (SS-DNA); TEMPERATURE EFFECTS;

BINDING ENERGY; DNA; ENZYMES; ESCHERICHIA COLI; GENES; NUCLEIC ACIDS; NUCLEOTIDES; OLIGOMERS; THERMAL EFFECTS;

HYDROLYSIS;

ADENOSINE TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE; DNAB HELICASE; NUCLEOSIDE TRIPHOSPHATE; PURINE; PYRIMIDINE;

ARTICLE; BINDING SITE; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DNA BINDING; ENZYME MECHANISM; ESCHERICHIA COLI; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN NUCLEIC ACID INTERACTION; TEMPERATURE SENSITIVITY; THERMODYNAMICS;

DNAB HELICASES; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; NUCLEOTIDES; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 67651211844     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9000529     Document Type: Article

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