Temperature and metal ions-dependent activity of the family I inorganic pyrophosphatase from the swine roundworm Ascaris suum.
Temperature dependence, heat stability and metal ions-dependent activity were examined on the Family I inorganic pyrophosphatase (PPase) recently identified from Ascaris suum. Recombinant A. suum PPase (rAsPPase) showed an optimal activity at 55 degrees C. The rAsPPase was heat stable at 40 degrees C in the absence of added Mg(2+) and at 50 degrees C in its presence. The enzyme required divalent metal ions for its activity. The preferences for the metal ions (5 mM concentration) were in the order: Mg(2+)> Co(2+)> Cu(2+)> Fe(2+)> Zn(2+)> Mn(2+). On the contrary, enzyme activity was inhibited by Ca(2+). These findings suggest that catalytic features of AsPPase are consistent with the Family I PPases reported from a wide range of organisms.
Islam
Khyrul M
KM
National Institute of Animal Health, National Agricultural Research Organization, Tsukuba, Ibaraki, Japan.
Miyoshi
Takeharu
T
Isobe
Takashi
T
Kasuga-Aoki
Harue
H
Arakawa
Takeshi
T
Matsumoto
Yasunobu
Y
Yokomizo
Yuichi
Y
Tsuji
Naotoshi
N
Tsuji
Naotoshi
N
D000818:Animals; D017165:Ascaris suum / Q000201:enzymology*; D002118:Calcium / Q000378:metabolism; D043564:Inorganic Pyrophosphatase / Q000378:metabolism*; D007700:Kinetics; D019216:Metals, Heavy / Q000378:metabolism*; D013696:Temperature
D019216:Metals, Heavy; D043564:Inorganic Pyrophosphatase; D002118:Calcium