Schenk, Gerhard and Korsinczky, Michael L.J. and Hume, David A. and Hamilton, Susan E. and de Jersey, John (2000) Purple acid phosphatases from bacteria: similarities to mammalian and plant enzymes. Gene, 255. pp. 419-424. ISSN 0378-1119

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Abstract

Mammalian and plant purple acid phosphatases have similar active site structures despite low sequence identity (<20%). Although no bacterial enzyme has been purified, a sequence database search revealed that genes that could encode potential purple acid phosphatases may be restricted to a small number of organisms (i.e. myco- and cyanobacteria). Analysis of their deduced amino acid sequences and predicted secondary structures indicates that the cyanobacterial enzyme is similar to both the mammalian and the recently discovered low-molecular-weight plant purple acid phosphatases, while the mycobacterial enzyme is homologous to the fungal and high-molecular-weight plant purple acid phosphatases. Homology models indicate that both bacterial proteins appear to be similar to mammalian purple acid phosphatases in the immediate vicinity of the active site. It is likely that these enzymes act as Fenton-type catalysts in order to prevent damage caused by reactive oxygen species generated by invaded host cells (M. tuberculosis) or by the light-harvesting complex (Synechocystis sp.). © 2000 Elsevier Science B.V. All rights reserved.

Item Type:	Article
Keywords:	Binuclear metal centre; Cyanobacteria; Fenton-type catalysis; Mycobacteria; Phosphate metabolism; Purple acid phosphatase;
Academic Unit:	Faculty of Science and Engineering > Chemistry
Item ID:	3745
Depositing User:	Gary Schenk
Date Deposited:	07 Jun 2012 15:13
Journal or Publication Title:	Gene
Publisher:	Elsevier
Refereed:	Yes
URI:	Publisher
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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