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. 1993 Dec;25(12):1969-74.
doi: 10.1016/0020-711x(88)90333-3.

Regulation of rat-kidney cortex fructose-1,6-bisphosphatase activity. II. Effects of adenine nucleotides

M M Sola  1 , F J Oliver, R Salto, M Gutiérrez, A M Vargas
Affiliations

Regulation of rat-kidney cortex fructose-1,6-bisphosphatase activity. II. Effects of adenine nucleotides

M M Sola et al. Int J Biochem. 1993 Dec.

Abstract

1. The native rat-kidney cortex Fructose-1,6-bisphosphatase is differentially regulated by adenine nucleotides in the presence of divalent cations. 2. Binding of AMP and ADP to the enzyme is co-operative. The inhibition by both nucleotides show an uncompetitive mechanism AMP being the most efficient inhibitor. 3. Mg2+ decreases the inhibition produced by AMP and ADP by enhancing their I0.5 and completely annulates the inhibitory effect of ATP. 4. In the presence of Mn2+ ADP behaves as an inhibitor but no inhibition is evident with AMP, suggesting the existence of different allosteric sites for each nucleotide.

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