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
Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component. / Rossolini, Gian Maria; Thaller, Maria Cristina; Pezzi, Renato; Satta, Giuseppe.
In: FEMS Microbiology Letters, Vol. 118, No. 1-2, 01.05.1994, p. 167-173.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component
AU - Rossolini, Gian Maria
AU - Thaller, Maria Cristina
AU - Pezzi, Renato
AU - Satta, Giuseppe
PY - 1994/5/1
Y1 - 1994/5/1
N2 - 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.
AB - 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.
KW - Acid phosphatase
KW - Escherichia coli
UR - http://www.scopus.com/inward/record.url?scp=0028277528&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028277528&partnerID=8YFLogxK
M3 - Article
C2 - 8013875
AN - SCOPUS:0028277528
VL - 118
SP - 167
EP - 173
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1-2
ER -