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Enzyme Research

Reports from RIKEN add new data to research in enzyme research

Published in Health Business Week, February 8th, 2008

"Monufunctional histidinol phosphate phosphatase from Thermus thermophilus HB8, which catalyzes the dephosphorylation Of L-histidinol phosphate, belongs to the PHP family, together with the PHP domain of bacterial DNA polymerase III and family X DNA polymerase. We have determined the structures of the complex with a sulfate ion, the complex with a phosphate ion, and the unliganded form at 1.6, 2.1, and 1.8 A resolution, respectively," scientists in Sayo, Japan report.

"The enzyme exists as a tetramer, and the subunit consists of a distorted W(X)7 barrel with one linker and one C-terminal tail. Three metal sites located on the C-terminal side of the barrel are occupied...

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