Amino-acids imitate the EDTA activation on the fructose-1,6-bisphosphatase of mantle tissue from the sea mussel (Mytilus galloprovincialis Lmk).
In the absence of AMP and Fru-2,6-P2, several amino-acids such as histidine, lysine, alanine, aspartic acid, and other molecules, as reduced glutathione or citrate, activate FBPase-1 from Mytilus galloprovincialis mantle. AMP decreases Vmax and Km for Fru-1,6-P2 both in the absence and in the presence of activators; but the addition of Fru-2,6-P2 decreases the affinity of the enzyme by its substrate. Na+ acts as a inhibitor reducing both Vmax and Km. The Km value is lower than the physiological level of Fru-1,6-P2, suggesting that the enzyme is operative but its activity is very reduced.
Barcia
R
R
Departamento de Bioquímica e Bioloxia Molecular, Universidade de Santiago de Compostela, Facultade de Veterinaria, Lugo, Spain.
Ramos-Martínez
J I
JI
D000249:Adenosine Monophosphate / Q000494:pharmacology; D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D049872:Bivalvia / Q000201:enzymology*; D002850:Chromatography, Gel; D004492:Edetic Acid / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005635:Fructosediphosphates / Q000494:pharmacology; D012964:Sodium / Q000494:pharmacology; D013053:Spectrophotometry
D000596:Amino Acids; D005635:Fructosediphosphates; D000249:Adenosine Monophosphate; C027652:fructose 2,6-diphosphate; D004492:Edetic Acid; D012964:Sodium; D006597:Fructose-Bisphosphatase