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.
Rossolini
G M
GM
Dipertimento di Biologia Molecolare, Università di Siena, Italy.
Thaller
M C
MC
Pezzi
R
R
Satta
G
G
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