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. 1973 Mar;70(3):661–664. doi: 10.1073/pnas.70.3.661

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

S Pontremoli 1,2, E Melloni 1,2, A De Flora 1,2, B L Horecker 1,2
PMCID: PMC433329  PMID: 4351799

Abstract

Removal of the NH2-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 NH2-terminus. Thus, the tryptophan-containing peptide appears to determine the functional properties of the native enzyme.

Keywords: rabbit, subtilisin, allosteric, tryptophan fluorescence

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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