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Specificity of Creatine Phosphokinase

Abstract

SOME of the properties of the enzyme creatine phosphokinase have recently been described1; but no experiments were reported on the activity of the enzyme with substrates other than adenosine tri-phosphate, adenosine diphosphate, phosphocreatine and creatine. Such experiments are in progress and will be reported in due course. A recent publication by Armstrong2, in which it was shown that the administration of N-ethylglycocyamine (negmine) was followed by the urinary excretion of N-ethyl-glycocyamidine (negmidine), suggested that a phosphorylation reaction may have been involved. It was therefore of interest to determine whether negmine could be phosphorylated by the creatine phosphokinase system.

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References

  1. Ennor, A. H., and Rosenberg, H., Biochem. J., 57, 203 (1954).

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  2. Armstrong, M. D., Fed. Proc., 12, 170 (1953).

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  3. Ennor, A. H., and Rosenberg, H. (unpublished observations).

  4. Lipmann, F., “Adv. in Enzymol.”, 1, 99 (1941).

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  5. Borsook, H., and Dubnoff, J. W., J. Biol. Chem., 168, 493 (1947).

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ENNOR, A., ROSENBERG, H. & ARMSTRONG, M. Specificity of Creatine Phosphokinase. Nature 175, 120 (1955). https://doi.org/10.1038/175120a0

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