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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Martin SR,Biekofsky RR,Skinner MA,Guerrini R,Salvadori S,Feeney J,Bayley PMdoi
10.1016/j.febslet.2004.10.023keywords:
subject
Has Abstractpub_date
2004-11-05 00:00:00pages
284-8issue
1-2eissn
0014-5793issn
1873-3468pii
S0014579304012578journal_volume
577pub_type
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