Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 167-173 |
| Number of pages | 7 |
| Journal | FEMS Microbiology Letters |
| Volume | 118 |
| Issue number | 1-2 |
| Publication status | Published - May 1 1994 |
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Keywords
- Acid phosphatase
- Escherichia coli
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Applied Microbiology and Biotechnology
- Microbiology
Cite this
Rossolini, G. M., Thaller, M. C., Pezzi, R., & Satta, G. (1994). Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component. FEMS Microbiology Letters, 118(1-2), 167-173.