Switching catalytic reaction conducted in pore void of mesoporous material by redox gate control.

A molecular gate attached on the pore outlet of a mesoporous material, which is opened and closed by redox system of thiol groups, effectively switched the progress of a catalytic reaction promoted by the acidic site in the pore void.

Heterologous expression and catalytic properties of the C-terminal domain of starfish cdc25 dual-specificity phosphatase, a cell cycle regulator.

The 3'-terminal region of starfish Asterina pectinifera cdc25 cDNA encoding the C-terminal catalytic domain was overexpressed in Escherichia coli. The C-terminal domain consisted of 226 amino acid residues containing the signature motif HCxxxxxR, a motif highly conserved among protein tyrosine and dual-specificity phosphatases, and showed phosphatase activity toward p-nitrophenyl phosphate. The enzyme activity was strongly inhibited by SH inhibitors.