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 |
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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 |
Keywords
- Acid phosphatase
- Escherichia coli
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Applied Microbiology and Biotechnology
- Microbiology