PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21831832-3	2011	Our spectroscopy and transient kinetics results on human dUTPase mutants combined with previous structural studies indicate that (i) H-bond interactions between the gamma-phosphate and the P-loop-like motif V promote the catalytically competent conformation of the reaction center at the alpha-phosphate group; (ii) these interactions accelerate the chemical step of the kinetic cycle and that (iii) hydrolysis occurs very slowly or not at all in the absence of the gamma-phosphate--motif V interactions, i.e., in dUDP, dUDP.BeFx, or in the motif V-deleted mutant.	Phosphates	171-180	Deoxyuridine triphosphatase	Drosophila melanogaster	57-64