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J. Biol. Chem., Vol. 260, Issue 18, 10019-10022, Aug, 1985
JE Foreman and WG Niehaus Jr
Mannitol-1-phosphate dehydrogenase (EC 1.1.1.17) has been purified from
Aspergillus parasiticus, a filamentous fungus which produces the polyketide
mycotoxin, versicolorin A. Its kinetic properties have been compared with
those of mannitol-1-phosphate dehydrogenase from the related
non-toxin-producing fungus, A. niger. Both enzymes are inhibited by
divalent transition metals, especially Zn2+ and Cd2+, but only the enzyme
from A. parasiticus exhibits inhibitor-induced cooperative binding of the
substrate, fructose-6 phosphate. Double reciprocal plots (1/v versus
1/Fru-6-P) are linear in the absence of Zn2+ but in the presence of Zn2+
are concave upward, with Hill coefficients of 1.5. The extent of
cooperativity is inversely related to ionic strength, disappearing at 100
mM KCl. The enzymes from both organisms are relatively stable to incubation
at 30 degrees C, but only the enzyme from A. parasiticus is rendered
thermally unstable by the addition of divalent transition metals. A model
is proposed to explain how binding of transition metal ions affects
substrate binding and thermal stability of the enzyme.
Zn2+-induced cooperativity of mannitol-1-phosphate dehydrogenase from Aspergillus parasiticus
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