Open AccessIdentification of the gene ( aphA ) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product
Author(s) -
Thaller Maria Cristina,
Schippa Serena,
Bonci Alessandra,
Cresti Stefania,
Rossolini Gian Maria
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10192.x
Subject(s) - phosphomonoesters , escherichia coli , biochemistry , phosphatase , open reading frame , phosphotransferase , biology , enzyme , cloning (programming) , acid phosphatase , gene product , microbiology and biotechnology , gene , chemistry , gene expression , peptide sequence , computer science , programming language , inorganic phosphate
An open reading frame located in the tyrB ‐ uvrA intergenic region of the Escherichia coli MG1655 chromosome was identified as encoding the class B acid phosphatase of this species on the basis of cloning and expression experiments. A protocol for purification of the enzyme (named AphA) was developed, and its properties were analyzed. The enzyme is a 100‐kDa homotetrameric protein which apparently requires a metal co‐factor for activity. Similarly to other bacterial class B acid phosphatases, it is able to dephosphorylate several organic phosphomonoesters as well as to catalyze the transfer of low‐energy phosphate groups from phosphomonoesters to hydroxyl groups of various organic compounds.