Kinetic mechanisms of the nucleotide cofactor binding to the strong and weak nucleotide-binding site of the Escherichia coli PriA helicase. 2

Biochemistry

Volumn 45, Issue 23, 2006, Pages 7217-7236

  Lucius, Aaron L ^a   Jezewska, Maria J ^a   Roychowdhury, Anasuya ^a   Bujalowski, Wlodzimierz ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; ENZYME KINETICS; ESCHERICHIA COLI; FLUORESCENCE; MAGNESIUM PRINTING PLATES;

ALLOSTERIC CONTROL; ESCHERICHIA COLI PRIA HELICASE; NUCLEOTIDE COFACTOR; STOPPED FLOW TECHNIQUE;

ENZYMES;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; HELICASE; HELICASE PRIA; MAGNESIUM ION; NUCLEOTIDE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; MOLECULAR STABILITY; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; THERMODYNAMICS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BINDING SITES; DNA HELICASES; ESCHERICHIA COLI PROTEINS; KINETICS; SPECTROMETRY, FLUORESCENCE;

ESCHERICHIA COLI;

EID: 33745052089     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051827e     Document Type: Article

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