Effect of Zn(II) and Mg(II) on phosphohydrolytic activity of rat matrix-induced alkaline phosphatase.
Rat matrix-induced alkaline phosphatase is an enzyme which requires magnesium and zinc ions for its maximal activity. Two Zn(II) ions and one Mg(II) ion are bound to each subunit of native dimeric enzyme. The presence of magnesium ion (10-100 microM) or zinc ion (7-20 nM) alone is sufficient to stimulate apoenzyme activity. However maximal activity (264 U/mg) requires the presence of both ions. Binding of Zn(II) ions to the Mg(II) binding site causes a strong inhibition of the apoenzyme while the binding of Mg(II) on Zn(II) binding site is not sufficient to stimulate PNPPase activity of the apoenzyme. Binding of both ions to the enzyme molecule did not change the apparent dissociation constant for PNPP hydrolysis.
Ciancaglini
P
P
Pizauro
J M
JM
Grecchi
M J
MJ
Curti
C
C
Leone
F A
FA
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D001857:Bone Matrix / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology*; D051381:Rats; D015032:Zinc / Q000494:pharmacology*
D000469:Alkaline Phosphatase; D008274:Magnesium; D015032:Zinc