Interaction of calmodulin with the phosphofructokinase target sequence | Zendy

Martin Stephen R. | Zendy; Biekofsky Rodolfo R. | Zendy; Skinner Murray A. | Zendy; Guerrini Remo | Zendy; Salvadori Severo | Zendy; Feeney James | Zendy; Bayley Peter M. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

Interaction of calmodulin with the phosphofructokinase target sequence

Author(s) -

Martin Stephen R.,

Biekofsky Rodolfo R.,

Skinner Murray A.,

Guerrini Remo,

Salvadori Severo,

Feeney James,

Bayley Peter M.

Publication year - 2004

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2004.10.023

Subject(s) - tetramer , calmodulin , phosphofructokinase , histidine , chemistry , titration , glycolysis , peptide , biochemistry , peptide sequence , heteronuclear single quantum coherence spectroscopy , stereochemistry , target peptide , enzyme , biophysics , nuclear magnetic resonance spectroscopy , biology , inorganic chemistry , gene

Ca 4 · calmodulin (Ca 4 · CaM) inhibits the glycolytic enzyme phosphofructokinase, by preventing formation of its active tetramer. Fluorescence titrations show that the affinity of complex formation of Ca 4 · 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. 1 H NMR pH titration indicates a marked increase in p K a 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 Ca 4 · CaM in regulation of the glycolytic pathway.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research