Conversion of neutral to alkaline liver fructose 1,6-bisphosphatase: changes in molecular properties of the enzyme.
Removal of the NH(2)-terminal region of fructose 1,6-bisphosphatase from rabbit liver by digestion with subtillisin, or changes in conformation in this region of the protein produced by exposure to low concentrations of urea, result in similar changes in catalytic and allosteric properties of the enzyme. These changes include shift of the pH optimum to more alkaline pH, and loss of sensitivity to inhibition by AMP. The conformation changes are monitored by changes in the fluorescence of the single tryptophan residue, which is located near the NH(2)-terminus. Thus, the tryptophan-containing peptide appears to determine the functional properties of the native enzyme.
D000249:Adenosine Monophosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases; D000818:Animals; D002384:Catalysis; D006597:Fructose-Bisphosphatase; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism; D006598:Hexosediphosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D008968:Molecular Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013381:Subtilisins; D014364:Tryptophan / Q000032:analysis; D014508:Urea
D000596:Amino Acids; D006598:Hexosediphosphates; D000249:Adenosine Monophosphate; D014364:Tryptophan; D014508:Urea; D006597:Fructose-Bisphosphatase; D000626:Aminopeptidases; D013381:Subtilisins; D005634:Fructose-Bisphosphate Aldolase