Issue 9, 1994

‘Active’ conformation of the inositol monophosphatase substrates adenosine 2′-phosphate and inositol phosphate: role of the ribofuranosyl O-atom and inositol O-atoms in chelating a second magnesium ion

Abstract

A high energy conformation, in which the adenine moiety of adenosine 2′-phosphate occupies a C-1′-axial ribofuranosyl position, is stabilised through the chelation of a second (additional) Mg2+ ion by the 2′-and furanose ring O-atoms; with inositol 1-phosphate as the substrate, the 1- and 6-O-atoms chelate the second Mg2+ ion and for both substrates a different (buried) Mg2+ ion interacts directly with the phosphate moiety.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1994, 1139-1141

‘Active’ conformation of the inositol monophosphatase substrates adenosine 2′-phosphate and inositol phosphate: role of the ribofuranosyl O-atom and inositol O-atoms in chelating a second magnesium ion

A. G. Cole and D. Gani, J. Chem. Soc., Chem. Commun., 1994, 1139 DOI: 10.1039/C39940001139

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements