PMID:15148399
| Citation |
Yang, K and Metcalf, WW (2004) A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase. Proc. Natl. Acad. Sci. U.S.A. 101:7919-24 |
|---|---|
| Abstract |
Genetic analysis indicates that Escherichia coli possesses two independent pathways for oxidation of phosphite (Pt) to phosphate. One pathway depends on the 14-gene phn operon, which encodes the enzyme C-P lyase. The other pathway depends on the phoA locus, which encodes bacterial alkaline phosphatase (BAP). Transposon mutagenesis studies strongly suggest that BAP is the only enzyme involved in the phoA-dependent pathway. This conclusion is supported by purification and biochemical characterization of the Pt-oxidizing enzyme, which was proven to be BAP by N terminus protein sequencing. Highly purified BAP catalyzed Pt oxidation with specific activities of 62-242 milliunits/mg and phosphate ester hydrolysis with specific activities of 41-61 units/mg. Surprisingly, BAP catalyzes the oxidation of Pt to phosphate and molecular H2. Thus, BAP is a unique Pt-dependent, H2-evolving hydrogenase. This reaction is unprecedented in both P and H biochemistry, and it is likely to involve direct transfer of hydride from the substrate to water-derived protons. |
| Links |
PubMed PMC419532 Online version:10.1073/pnas.0400664101 |
| Keywords |
Alkaline Phosphatase/isolation & purification; Alkaline Phosphatase/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Hydrogen/metabolism; Hydrogenase/metabolism; Hydrolysis; Mutation/genetics; Oxidation-Reduction; Phosphates/metabolism; Phosphites/metabolism; Protons |
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This paper demonstrates that PhoA is a phosphite-dependent, H2-evolving hydrogenase. The reaction is unusual and is likely to involve direct transfer of hydride from the substrate to water-derived protons.
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