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Purple acid phosphatases from bacteria: similarities to mammalian and plant enzymes
Schenk, Gerhard; Korsinczky, Michael L.J.; Hume, David A.; Hamilton, Susan E.; de Jersey, John
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.
Keyword(s): Chemistry; Binuclear metal centre; Cyanobacteria; Fenton-type catalysis; Mycobacteria; Phosphate metabolism; Purple acid phosphatase
Publication Date:
2000
Type: Journal article
Peer-Reviewed: Yes
Institution: Maynooth University
Citation(s): 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
Publisher(s): Elsevier
File Format(s): application/pdf
Related Link(s): http://mural.maynoothuniversity.ie/3745/1/GS_Purple_Acid.pdf
First Indexed: 2020-01-31 06:06:41 Last Updated: 2020-04-02 07:26:30