[HTML][HTML] Definition of optimal substrate recognition motifs of Ca2+-calmodulin-dependent protein kinases IV and II reveals shared and distinctive features
RR White, YG Kwon, M Taing, DS Lawrence… - Journal of Biological …, 1998 - ASBMB
The substrate recognition determinants of Ca 2+-calmodulin-dependent protein kinase
(CaMK) IV and CaMKIIα were investigated using peptide substrates modeled on the amino
acid sequence encompassing Ser-9 of synapsin I. For both kinases, hydrophobic residues
(Leu or Phe) at the− 5 position, are well tolerated, whereas non-hydrophobic residues (Arg,
Ala, or Asp) decreaseV max/K m by 55-to> 4000-fold. At the− 3 position, substitution of Ala
for Arg leads to decreases of 99-and 343-fold inV max/K m for CaMKIV and CaMKIIα …
(CaMK) IV and CaMKIIα were investigated using peptide substrates modeled on the amino
acid sequence encompassing Ser-9 of synapsin I. For both kinases, hydrophobic residues
(Leu or Phe) at the− 5 position, are well tolerated, whereas non-hydrophobic residues (Arg,
Ala, or Asp) decreaseV max/K m by 55-to> 4000-fold. At the− 3 position, substitution of Ala
for Arg leads to decreases of 99-and 343-fold inV max/K m for CaMKIV and CaMKIIα …