A conserved negatively charged cluster in the active site of creatine kinase is critical for enzymatic activity.

@article{Eder2000ACN,
  title={A conserved negatively charged cluster in the active site of creatine kinase is critical for enzymatic activity.},
  author={Michael Eder and Michael Stolz and Theo Wallimann and Uwe Schlattner},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 35},
  pages={27094-9}
}
Creatine kinase catalyzes the reversible transphosphorylation of creatine by MgATP. From the sequence homology and the molecular structure of creatine kinase isoenzymes, we have identified several highly conserved residues with a potential function in the active site: a negatively charged cluster (Glu(226), Glu(227), Asp(228)) and a serine (Ser(280)). Mutant proteins E226Q, E226L, E227Q, E227L, D228N, and S280A/S280D of human sarcomeric mitochondrial creatine kinase were generated by in vitro… CONTINUE READING