Conversion of Neutral to Alkaline Liver Fructose 1,6-Bisphosphatase: Changes in Molecular Properties of the Enzyme | Zendy

S. Pontremoli | Zendy; E. Melloni | Zendy; Antonio De Flora | Zendy; B.L. Horecker | Zendy

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Conversion of Neutral to Alkaline Liver Fructose 1,6-Bisphosphatase: Changes in Molecular Properties of the Enzyme

Author(s) -

S. Pontremoli,

E. Melloni,

Antonio De Flora,

B.L. Horecker

Publication year - 1973

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.70.3.661

Subject(s) - fructose 1,6 bisphosphatase , tryptophan , allosteric regulation , chemistry , enzyme , biochemistry , urea , fructose , residue (chemistry) , peptide , enzyme assay , amino acid

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.

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