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

Mark Harris | Zendy; D. A. Usher | Zendy; Hans Albrecht | Zendy; Gordon H. Jones | Zendy; J. G. Moffatt | Zendy

Open Access

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

Author(s) -

Mark Harris,

D. A. Usher,

Hans Albrecht,

Gordon H. Jones,

J. G. Moffatt

Publication year - 1969

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.63.2.246

Subject(s) - phosphonate , hydrolysis , pseudorotation , chemistry , ribonuclease , catalysis , enzyme , uridine , stereochemistry , reaction rate constant , medicinal chemistry , mechanism of action , organic chemistry , biochemistry , kinetics , rna , molecule , physics , quantum mechanics , in vitro , gene

Uridine 2',3'-cyclic phosphonate (I) is slowly hydrolyzed by ribonuclease-A with k(2) and K(m) 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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