Phosphatase activities were investigated in Morganella morganii, which is one of the few enterobacterial species producing high-level phosphateirrepressible acid phosphatase activity (HPAP phenotype), and the gene encoding the major phosphate-irrepressible acid phosphatase was cloned, sequenced, and its product characterized. Using p-nitrophenyl phosphate as substrate, Morganella produced a major phosphate-irrepressible acid phosphatase (named PhoC) which is associated with the HPAP phenotype, a minor phosphate-irrepressible acid phosphatase, and a phosphate-repressible alkaline phosphatase. The presence of the PhoC activity prevented induction of alkaline phosphatase when a PhoC-hydrolysable organic phosphate ester, such as glycerol &phosphate, was the sole phosphate source. PhoC is a secreted nonspecific acid phosphatase apparently composed of four 25 kDa polypeptide subunits. The enzyme is resistant to EDTA, Pi# fluoride and tartrate. The M. morganii PhoC showed 84.6% amino acid sequence identity to the PhoN nonspecific acid phosphatase of Providencia stuartii, 45.3 O/O to the PhoN nonspecific acid phosphatase of Salmonella typhimurium, and 3708% to the principal acid phosphatase (PhoC) of Zymomonas mobilis. Comparison of sequence data and of regulation of these enzymes suggested a different phylogeny of members of this gene family within the Enterobacteriaceae.

Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii / Thaller, Mc; Berlutti, Francesca; Schippa, Serena; Lombardi, G; Rossolini, Gm. - In: MICROBIOLOGY. - ISSN 1350-0872. - 140 ( Pt 6):(1994), pp. 1341-1350..

Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii.

BERLUTTI, Francesca;SCHIPPA, Serena;
1994

Abstract

Phosphatase activities were investigated in Morganella morganii, which is one of the few enterobacterial species producing high-level phosphateirrepressible acid phosphatase activity (HPAP phenotype), and the gene encoding the major phosphate-irrepressible acid phosphatase was cloned, sequenced, and its product characterized. Using p-nitrophenyl phosphate as substrate, Morganella produced a major phosphate-irrepressible acid phosphatase (named PhoC) which is associated with the HPAP phenotype, a minor phosphate-irrepressible acid phosphatase, and a phosphate-repressible alkaline phosphatase. The presence of the PhoC activity prevented induction of alkaline phosphatase when a PhoC-hydrolysable organic phosphate ester, such as glycerol &phosphate, was the sole phosphate source. PhoC is a secreted nonspecific acid phosphatase apparently composed of four 25 kDa polypeptide subunits. The enzyme is resistant to EDTA, Pi# fluoride and tartrate. The M. morganii PhoC showed 84.6% amino acid sequence identity to the PhoN nonspecific acid phosphatase of Providencia stuartii, 45.3 O/O to the PhoN nonspecific acid phosphatase of Salmonella typhimurium, and 3708% to the principal acid phosphatase (PhoC) of Zymomonas mobilis. Comparison of sequence data and of regulation of these enzymes suggested a different phylogeny of members of this gene family within the Enterobacteriaceae.
1994
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Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii / Thaller, Mc; Berlutti, Francesca; Schippa, Serena; Lombardi, G; Rossolini, Gm. - In: MICROBIOLOGY. - ISSN 1350-0872. - 140 ( Pt 6):(1994), pp. 1341-1350..
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/121794
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