Multiple transients in the pre-steady-state of nucleoside hydrolase reveal complex substrate binding, product base release, and two apparent rates of chemistry

Biochemistry

Volumn 45, Issue 30, 2006, Pages 9307-9318

  Vandemeulebroucke, An ^a   Versées, Wim ^a   Steyaert, Jan ^a   Barlow, John N ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; ENZYME INHIBITION; FLUORESCENCE; MONOMERS; PH EFFECTS; SPECTROSCOPIC ANALYSIS; SUBSTRATES;

ABSORBANCE SPECTROSCOPY; NUCLEOSIDE HYDROLASE; SUBSTRATE BINDING; TRANSIENT KINETICS;

ENZYME KINETICS;

NUCLEOSIDASE;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING AFFINITY; CHEMICAL ANALYSIS; COMPLEX FORMATION; DNA REPAIR; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; MUTAGENESIS; PRIORITY JOURNAL; STEADY STATE; TRYPANOSOMA VIVAX;

ANIMALS; BINDING SITES; GUANINE; HYDROGEN-ION CONCENTRATION; INOSINE; KINETICS; MODELS, CHEMICAL; N-GLYCOSYL HYDROLASES; PROTOZOAN PROTEINS; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; TRYPANOSOMA VIVAX;

TRYPANOSOMA VIVAX;

EID: 33746635945     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060666r     Document Type: Article

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