Role of AMP deaminase reaction in the control of fructose 1,6-bisphosphatase activity in yeast.
The physiological role of the inhibition of AMP deaminase (EC 3.5.4.6) by Pi was analyzed using permeabilized yeast cells. (a) Fructose 1,6-bisphosphatase (EC 3.1.3.11) was inhibited only a little by AMP, which was readily degraded by AMP deaminase under the in situ conditions. (b) The addition of Pi, which showed no direct effect on fructose 1,6-bisphosphatase, effectively enhanced the inhibition of the enzyme by AMP increased through the inhibition of AMP deaminase. (c) Pi activated phosphofructokinase (EC 2.7.1.11) and inhibited AMP deaminase activity. AMP deaminase reaction can act as a control system of fructose 1,6-bisphosphatase activity and gluconeogenesis/glycolysis reaction through the change in the AMP level. Pi may contribute to the stimulation of glycolysis through the inhibition of fructose 1,6-bisphosphatase by the increase in AMP in addition to the direct activation of phosphofructokinase.
Yoshino
M
M
Murakami
K
K
D000659:AMP Deaminase / Q000378:metabolism*; D000249:Adenosine Monophosphate / Q000378:metabolism; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D009709:Nucleotide Deaminases / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D010710:Phosphates; D000249:Adenosine Monophosphate; D006597:Fructose-Bisphosphatase; D009709:Nucleotide Deaminases; D000659:AMP Deaminase