Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component

Gian Maria Rossolini; Maria Cristina Thaller; Renato Pezzi; Giuseppe Satta

Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component

Gian Maria Rossolini, Maria Cristina Thaller, Renato Pezzi, Giuseppe Satta

Fondazione Don Carlo Gnocchi Onlus

Research output: Contribution to journal › Article › peer-review

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

Keywords

Acid phosphatase
Escherichia coli

ASJC Scopus subject areas

Genetics
Molecular Biology
Applied Microbiology and Biotechnology
Microbiology

Cite this

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title = "Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component",

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.",

keywords = "Acid phosphatase, Escherichia coli",

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AU - Rossolini, Gian Maria

AU - Thaller, Maria Cristina

AU - Pezzi, Renato

AU - Satta, Giuseppe

PY - 1994/5/1

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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

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ER -

Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component

Abstract

Keywords

ASJC Scopus subject areas

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