Catalytic significance of the specificity of divalent cations as KS* and kcat* cofactors for secreted phospholipase A2.

@article{Yu1998CatalyticSO,
  title={Catalytic significance of the specificity of divalent cations as KS* and kcat* cofactors for secreted phospholipase A2.},
  author={B. Z. Yu and J. Rogers and G. Nicol and K. Theopold and K. Seshadri and S. Vishweshwara and M. Jain},
  journal={Biochemistry},
  year={1998},
  volume={37 36},
  pages={
          12576-87
        }
}
Calcium is required for the substrate binding and for the chemical step of the interfacial catalytic turnover cycle of pancreatic phospholipase A2 (PLA2), but not for the binding of the enzyme to the interface. The role of calcium and other divalent cations (C) is analyzed for the effect on the substrate binding and kcat* for the chemical step. The cofactor role of 3d-cations(II) (C) for the hydrolysis of dimyristoylphosphatidylmethanol (DMPM) vesicles is characterized as an equilibrium… Expand
Allosteric effect of amphiphile binding to phospholipase A(2).
Structure, function and interfacial allosterism in phospholipase A2: insight from the anion-assisted dimer.
  • B. Bahnson
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 2005
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