Pj. Greasley et Mg. Gore, BOVINE INOSITOL MONOPHOSPHATASE - STUDIES ON THE BINDING INTERACTIONSWITH MAGNESIUM, LITHIUM AND PHOSPHATE IONS, FEBS letters, 331(1-2), 1993, pp. 114-118
Rapid equilibrium dialysis has been used to show that recombinant bovi
ne brain inositol monophosphatase binds one equivalent of P(i) per sub
unit of enzyme. P(i) is only bound in the presence of Mg2+ ions. The d
issociation constant for the equilibrium is approximately 50 muM. This
value of K(d) is independent of the concentration of the Mg2+ ions an
d of the presence or absence of Li+ ions. Lithium ions which inhibit t
he enzyme uncompetitively are not able to support the binding of the P
(i) to the enzyme. The observation that P(i) only binds in the presenc
e of Mg2+ ions supports similar conclusions made in experiments which
studied the protection of the enzyme from proteolytic degradation and
chemical modification.