2b8j

Structural highlights

Function

[APHA_ECOLI] Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity.^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Acid phosphatase

References

1. ↑ Thaller MC, Schippa S, Bonci A, Cresti S, Rossolini GM. Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product. FEMS Microbiol Lett. 1997 Jan 15;146(2):191-8. PMID:9011040
2. ↑ Passariello C, Forleo C, Micheli V, Schippa S, Leone R, Mangani S, Thaller MC, Rossolini GM. Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655. Biochim Biophys Acta. 2006 Jan;1764(1):13-9. Epub 2005 Nov 2. PMID:16297670 doi:http://dx.doi.org/10.1016/j.bbapap.2005.08.028
3. ↑ Calderone V, Forleo C, Benvenuti M, Thaller MC, Rossolini GM, Mangani S. A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases. J Mol Biol. 2006 Jan 27;355(4):708-21. Epub 2005 Nov 10. PMID:16330049 doi:http://dx.doi.org/10.1016/j.jmb.2005.10.068