title: Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions.
abstract: Treatment of a hyperthermophilic enzyme, alkaline phosphatase from Pyrococcus furiosus (PfuAP), with EDTA completely deactivated PfuAP, indicating that the presence of one or more divalent metal ions is essential for its catalytic activity. Subsequent addition of various divalent metal ions to the apoprotein recovered the enzymatic activity and, in particular, the addition of Co(II) resulted in an over 50-fold increase in activity compared with PfuAP before EDTA treatment. Intriguingly, PfuAP with Co(II) exhibited weaker stability toward heat treatment, suggesting that Co(2+) destabilizes the tertiary structure of PfuAP at high temperature.
authors: Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, 744 Motooka, Fukuoka, Japan.
authors: Kosuke
authors: K
authors: Minamihata
authors: Masahiro
authors: M
authors: Goto
authors: Noriho
authors: N
authors: Kamiya
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002413:Cations, Divalent / Q000737:chemistry; D002942:Circular Dichroism; D003035:Cobalt / Q000737:chemistry / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D006358:Hot Temperature; D020027:Pyrococcus furiosus / Q000187:drug effects* / Q000201:enzymology*
chemical_list: D019843:Archaeal Proteins; D002413:Cations, Divalent; D003035:Cobalt; D000469:Alkaline Phosphatase