Distinct Metal Ion Requirements for the Phosphomonoesterase and
Phosphodiesterase Activities of Calf Intestinal Alkaline Phosphatase

Igunnu, Adedoyin; Osalaye, Dunsin S; Olorunsogo, Olufunso O; Malomo, Sylvia O; Olorunniji, Femi J

Distinct Metal Ion Requirements for the Phosphomonoesterase and Phosphodiesterase Activities of Calf Intestinal Alkaline Phosphatase

Adedoyin Igunnu¹, Dunsin S Osalaye², Olufunso O Olorunsogo², Sylvia O Malomo^{**, 1}, Femi J Olorunniji^{*, 1, 3}

¹ Department of Biochemistry, Faculty of Science, University of Ilorin, Ilorin, Nigeria

² Department of Biochemistry, College of Basic Medical Sciences, University of Ibadan, Ibadan, Nigeria

³ Institute of Molecular Cell and Systems Biology, University of Glasgow, Bower Building, Glasgow G12 8QQ, Scotland, UK

Article Information

Identifiers and Pagination:

Year: 2011
Volume: 5
First Page: 67
Last Page: 72
Publisher ID: TOBIOCJ-5-67
DOI: 10.2174/1874091X01105010067

Article History:

Received Date: 26/9/2011
Revision Received Date: 28/10/2011
Acceptance Date: 30/10/2011
Electronic publication date: 30/12/2011
Collection year: 2011

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© Igunnu et al.; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http: //creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

^* Address correspondence to these authors at the Institute of Molecular Cell and Systems Biology, University of Glasgow, Bower Building, Glasgow G12 8QQ, Scotland, UK; Tel: +441413303331; E-mail: Femi.Olorunniji@glasgow.ac.uk^** Department of Biochemistry, Faculty of Science, University of Ilorin, Ilorin, Nigeria; Tel: +2348033736997; E-mail: somalomo@unilorin.edu.ng

The roles of Mg²⁺ and Zn²⁺ ions in promoting phosphoryl transfer catalysed by alkaline phosphatase are yet to be fully characterised. We investigated the divalent metal ion requirements for the monoesterase and diesterase activities of calf intestinal alkaline phosphatase. The synergistic effect of Mg²⁺ and Zn²⁺ in promoting the hydrolysis of para-nitrophenyl phosphate (monoesterase reaction) by alkaline phosphatase is not observed in the hydrolysis of the diesterase substrate, bis-para-nitrophenyl phosphate. Indeed, the diesterase reaction is inhibited by concentrations of Mg²⁺ that were optimal for the monoesterase reaction. This study reveals that the substrate specificities of alkaline phosphatases and related bimetalloenzymes are subject to regulation by changes in the nature and availability of cofactors, and the different cofactor requirements of the monoesterase and diesterase reactions of mammalian alkaline phosphatases could have significance for the biological functions of the enzymes.

Keywords: Alkaline phosphatase, phosphodiester hydrolysis, metal ion cofactors.

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RESEARCH ARTICLE

Distinct Metal Ion Requirements for the Phosphomonoesterase and Phosphodiesterase Activities of Calf Intestinal Alkaline Phosphatase

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Abstract

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