THE HYDROLYSIS OF URIDINE CYCLIC PHOSPHONATE CATALYZED BY RIBONUCLEASE-A: IMPLICATIONS FOR THE MECHANISM OF ACTION OF THE ENZYME

AUTOR(ES)
RESUMO

Uridine 2′,3′-cyclic phosphonate (I) is slowly hydrolyzed by ribonuclease-A with k2 and Km values at pH6 that are respectively 1900 and 15 times smaller than the same parameters at the same pH for the related phosphate (II). Since the ratio of rate constants for hydroxide ion catalyzed hydrolysis is about 4, this result is consistent with, but does not prove a mechanism for the enzymic reaction that requires a pseudorotation.

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