Ca4 Æ calmodulin (Ca4 Æ CaM) inhibits the glycolytic enzyme phosphofructokinase, by preventing formation of its active tetramer. Fluorescence titrations show that the affinity of complex formation of Ca4 ÆCaM with the key 21-residue target peptide increases 1000-fold from pH 9.0 to 4.8, suggesting the involvement of histidine and carboxylic acid residues. 1H NMR pH titration indicates a marked increase in pKa of the peptide histidine on complex formation and HSQC spectra show related pH-dependent changes in the conformation of the complex. This unusually strong sensitivity of a CaM–target complex to pH suggests a potential functional role for Ca4 ÆCaM in regulation of the glycolytic pathway.

Interaction of calmodulin with the phosphofructokinase target sequence

GUERRINI, Remo;SALVADORI, Severo;
2004

Abstract

Ca4 Æ calmodulin (Ca4 Æ CaM) inhibits the glycolytic enzyme phosphofructokinase, by preventing formation of its active tetramer. Fluorescence titrations show that the affinity of complex formation of Ca4 ÆCaM with the key 21-residue target peptide increases 1000-fold from pH 9.0 to 4.8, suggesting the involvement of histidine and carboxylic acid residues. 1H NMR pH titration indicates a marked increase in pKa of the peptide histidine on complex formation and HSQC spectra show related pH-dependent changes in the conformation of the complex. This unusually strong sensitivity of a CaM–target complex to pH suggests a potential functional role for Ca4 ÆCaM in regulation of the glycolytic pathway.
2004
Martin, Sr; Biekofsky, Rr; Skinner, Ma; Guerrini, Remo; Salvadori, Severo; Feeney, J; Bayley, Pm
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11392/470785
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