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Enzyme Research
Researchers from RIKEN describe findings in enzyme research
May 16th, 2008
According to recent research published in the Journal of Molecular Biology, "Nonstandard nucleotide triphosphate pyrophosphatase (NTPase) can efficiently hydrolyze nonstandard purine nucleotides in the presence of divalent cations. The crystal structures of the NTPase from Pyrococcus horikoshii OT3 (PhNTPase) have been determined in two unliganded forms and in three liganded forms with inosine 5'-monophosphate (IMP), ITP and Mn, which visualize the recognition of these ligands unambiguously." "The overall structure of PhNTPase is similar to that of previously reported crystal structures of the NTPase from Methanococcus jannaschii and the human ITPase. They share...
Source: Health Business Week (2008-05-16)
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