Nitrogen and Sulphur at the Active Centre of Carboxypeptidase A

Abstract

A SERIES of metallocarboxypeptidases has been prepared by the substitution of manganese, cobalt, nickel, copper, cadmium, or mercury for zinc, the element present in and essential to the enzymatic activity of native carboxypeptidase A 1. The stability constants, peptidase and esterase activities of these derivatives have been studied and compared1–3. Zinc is bound to the single sulphydryl group of the apoenzyme4–6, as is cobalt as evidenced by its exchange with zinc and by the spectral changes which accompany its binding2,6. It has been suggested that a sulphur and a nitrogen atom of carboxypeptidase, together with a metal atom, constitute the active centre of the enzyme, their interaction being required for activity5.

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References

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    Vallee, B. L., Fed. Proc. (in the press).

  2. 2

    Coleman, J. E., and Vallee, B. L., J. Biol. Chem., 235, 390 (1960).

  3. 3

    Coleman, J. E., and Vallee, B. L. (in preparation).

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    Vallee, B. L., Coombs, T. L., and Hoch, F. L., Abst. Papers 138th Meeting Amer. Chem. Soc. (Washington, 1960).

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    Vallee, B. L., Coombs, T. L., and Hoch, F. L., J. Biol. Chem., 235, P.C., 45 (1960).

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    Williams, R. J. P., Nature, 188, 322 (1960).

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    Bjerrum, J., Schwarzenback, G., and Sillen, L. G., Stability Constants I-II (Chem. Soc., London, 1957).

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VALLEE, B., WILLIAMS, R. & COLEMAN, J. Nitrogen and Sulphur at the Active Centre of Carboxypeptidase A . Nature 190, 633–634 (1961). https://doi.org/10.1038/190633a0

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