Literature DB >> 8081499

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

M C Thaller1, F Berlutti, S Schippa, G Lombardi, G M Rossolini.   

Abstract

Phosphatase activities were investigated in Morganella morganii, which is one of the few enterobacterial species producing high-level phosphate-irrepressible 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 2-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, P(i), 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% to the PhoN nonspecific acid phosphatase of Salmonella typhimurium, and 37.8% 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.

Entities:  

Mesh:

Substances:

Year:  1994        PMID: 8081499     DOI: 10.1099/00221287-140-6-1341

Source DB:  PubMed          Journal:  Microbiology        ISSN: 1350-0872            Impact factor:   2.777


  19 in total

1.  X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.

Authors:  K Ishikawa; Y Mihara; K Gondoh; E Suzuki; Y Asano
Journal:  EMBO J       Date:  2000-06-01       Impact factor: 11.598

2.  Isolation, cloning, and expression of an acid phosphatase containing phosphotyrosyl phosphatase activity from Prevotella intermedia.

Authors:  X Chen; T Ansai; S Awano; T Iida; S Barik; T Takehara
Journal:  J Bacteriol       Date:  1999-11       Impact factor: 3.490

3.  Identification of a novel phosphatase sequence motif.

Authors:  J Stukey; G M Carman
Journal:  Protein Sci       Date:  1997-02       Impact factor: 6.725

4.  Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily.

Authors:  M C Thaller; S Schippa; G M Rossolini
Journal:  Protein Sci       Date:  1998-07       Impact factor: 6.725

5.  An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.

Authors:  A F Neuwald
Journal:  Protein Sci       Date:  1997-08       Impact factor: 6.725

6.  From phosphatases to vanadium peroxidases: a similar architecture of the active site.

Authors:  W Hemrika; R Renirie; H L Dekker; P Barnett; R Wever
Journal:  Proc Natl Acad Sci U S A       Date:  1997-03-18       Impact factor: 11.205

7.  Phosphorylation of nucleosides by the mutated acid phosphatase from Morganella morganii.

Authors:  Y Mihara; T Utagawa; H Yamada; Y Asano
Journal:  Appl Environ Microbiol       Date:  2000-07       Impact factor: 4.792

8.  Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile.

Authors:  G M Rossolini; N Franceschini; M L Riccio; P S Mercuri; M Perilli; M Galleni; J M Frere; G Amicosante
Journal:  Biochem J       Date:  1998-05-15       Impact factor: 3.857

9.  Identification and characterization of phoN-Sf, a gene on the large plasmid of Shigella flexneri 2a encoding a nonspecific phosphatase.

Authors:  K I Uchiya; M Tohsuji; T Nikai; H Sugihara; C Sasakawa
Journal:  J Bacteriol       Date:  1996-08       Impact factor: 3.490

10.  Expression of the virulence plasmid-carried apyrase gene (apy) of enteroinvasive Escherichia coli and Shigella flexneri is under the control of H-NS and the VirF and VirB regulatory cascade.

Authors:  F Berlutti; M Casalino; C Zagaglia; P A Fradiani; P Visca; M Nicoletti
Journal:  Infect Immun       Date:  1998-10       Impact factor: 3.441

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.