Evidence that the alkaline P-nitrophenylphosphate phosphatase from Halobacterium halobium is a manganese-containing enzyme
Author:
Publisher
Elsevier BV
Subject
Biochemistry
Reference28 articles.
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2. Purification and some properties of an atypical alkaline p-nitrophenylphosphate phosphatase activity from Halobacterium halobium;Bonet;Int. J. Biochem.,1991
3. Alkaline p-nitrophenylphosphate activity from Halobacterium halobium. Selective activation by manganese and effect of other divalent cations;Bonet;Int. J. Biochem.,1992
4. Bovine kidney alkaline phosphatase. Purification, subunit structure, and metalloenzyme properties;Cathala;J. biol. Chem.,1975
5. Characterization of a phosphotyrosil-protein phosphatase activity associated with a phosphoseryl-protein phosphatase of Mr = 95000 from bovine heart;Chernoff;J. biol. Chem.,1983
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1. Manganese;Comprehensive Coordination Chemistry II;2003
2. Properties of Halophilic Proteins;Cellular Origin, Life in Extreme Habitats and Astrobiology;2003
3. Stability of an extreme halophilic alkaline phosphatase from Halobacterium salinarium in non-conventional medium;Journal of Biotechnology;2001-05
4. Kinetic regulation of an alkalinep-nitrophenylphosphate phosphatase fromHalobacterium salinarumin low water system by Mn2+and monovalent cations;FEMS Microbiology Letters;2001-05
5. Structure and function of manganese-containing biomolecules;Perspectives on Bioinorganic Chemistry;1996
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