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Fructose-l,6-bisphosphatase

Ekdahl, E. N., and Ekman, P. (1984). The effect of fructose-2,6-bisphosphate and AMP on the activity of phosphorylated and unphosphorylated fructose-l,6-bisphosphatase from rat liver. FEES Lett. 167, 203-209. [Pg.259]

The enzyme from various sources is tetrameric. There is some confusion about the number of sites for zinc on each subunit, but probably there are three, giving a total of 12 Zn bound per molecule. The role of Zn appears to be one of modulation of activity. Binding of Zn to the first two sets of binding sites results in reduced catalytic activity. The third set of sites (of lowest affinity) appears to be the sites for the activating cation Mg ". Thus Zn can act as a negative regulator of fructose-l,6-bisphosphatase, and also as an activator when it binds to the third set of sites. [Pg.613]

See other pages where Fructose-l,6-bisphosphatase is mentioned: [Pg.748]    [Pg.646]    [Pg.72]    [Pg.146]    [Pg.69]    [Pg.332]    [Pg.332]    [Pg.259]    [Pg.479]    [Pg.646]    [Pg.407]    [Pg.683]    [Pg.386]    [Pg.249]    [Pg.154]    [Pg.2967]    [Pg.78]    [Pg.386]   
See also in sourсe #XX -- [ Pg.156 , Pg.166 ]



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