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- Title
Interaction of calmodulin with the phosphofructokinase target sequence
- Authors
Martin, Stephen R.; Biekofsky, Rodolfo R.; Skinner, Murray A.; Guerrini, Remo; Salvadori, Severo; Feeney, James; Bayley, Peter M.
- Abstract
Ca4 · calmodulin (Ca4 · CaM) inhibits the glycolytic enzyme phosphofructokinase, by preventing formation of its active tetramer. Fluorescence titrations show that the affinity of complex formation of Ca4 · CaM 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 · CaM in regulation of the glycolytic pathway.
- Subjects
CALMODULIN; CALCIUM-binding proteins; PHOSPHOFRUCTOKINASE 1; TETRAMERS (Oligomers)
- Publication
FEBS Letters, 2004, Vol 577, Issue 1/2, p284
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2004.10.023