Open AccessIdentification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa‐polypeptide component
Author(s) -
Rossolini Gian Maria,
Thaller Maria Cristina,
Pezzi Renato,
Satta Giuseppe
Publication year - 1994
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.1574-6968.1994.tb06821.x
Subject(s) - periplasmic space , escherichia coli , biochemistry , enzyme , acid phosphatase , phosphatase , chemistry , phosphate , hydrolysis , biology , gene
An acid phosphatase containing a 27‐kDa polypeptide component has been identified in Escherichia coli by means of a zymogram technique. The enzyme is secreted in the periplasmic space and is able to hydrolyze several organic phosphate esters, but not diesters, showing preferential activity on p ‐nitrophenyl phosphate and other phenolic phosphate esters. Production of the enzyme apparently occurs only in cells growing on carbon sources other than glucose.