Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component.
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.
Dipertimento di Biologia Molecolare, Università di Siena, Italy.
G M
GM
Rossolini
M C
MC
Thaller
R
R
Pezzi
G
G
Satta
D000135:Acid Phosphatase / Q000737:chemistry* / Q000378:metabolism*; D003470:Culture Media; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D005947:Glucose; D005990:Glycerol; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013379:Substrate Specificity
D003470:Culture Media; D000135:Acid Phosphatase; D005947:Glucose; D005990:Glycerol