Nitrogen and Sulphur at the Active Centre of Carboxypeptidase A

Details Nitrogen and Sulphur at the Active Centre of Carboxypeptidase A Nitrogen and Sulphur at the Active Centre of Carboxypeptidase A

May 1961

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1961natur.190..633v&link_type=abstract

Nature, Volume 190, Issue 4776, pp. 633-634 (1961).

Computer Science

Scientific paper

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 A1. 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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