Acid and alkaline phosphatases of <i>Capnocytophaga</i> species. I. Production and cytological localization of the enzymes

Poirier, T.; Holt, Stanley C.

doi:10.1139/m83-210

Cited by 23 publications

(14 citation statements)

References 40 publications

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“…Based on a functional search against all ORFs in the whole genome of C. perfringens strain 13, CPE0201 is believed to represent the only gene to encode an NSAP. Generally, acid phosphatases of Gram-positive bacteria are bound to the cell surface (Okabayashi et al, 1974) or cytoplasmic membrane (Poirier & Holt, 1983). CPE0201 appears to be the only surface-associated acid phosphatase of C. perfringens.…”

Section: Discussionmentioning

confidence: 99%

Genetic and biochemical analysis of a class C non-specific acid phosphatase (NSAP) of Clostridium perfringens

et al. 2010

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Clostridium perfringens, a Gram-positive anaerobe, is a human pathogen that causes gas gangrene in muscle tissues. Its ability to grow and survive in the host is believed to be due to the production of numerous enzymes that enable the organism to obtain essential nutrients from the host. In this study, CPE0201, a putative acid phosphatase gene deduced by genome analysis, was shown to encode a non-specific acid phosphatase in C. perfringens. Multiple alignments of the amino acid sequence showed that CPE0201 shares two signature motifs that belong to a class C acid phosphatase family. Expression of CPE0201 was shown to be positively regulated by the global VirR/VirS-VR-RNA regulatory cascade at the transcriptional level. To determine the acid phosphatase activity of the CPE0201-encoded protein, cloning, expression, purification and several biochemical characterizations were carried out. The optimum pH for activity of the CPE0201 enzyme was 4.8, and its V max and K m were 3.08 nmol ml−1 min−1 and 2.84 mM, respectively, with p-nitrophenyl phosphate (PNPP) as substrate. A CPE0201 mutant did not grow in a minimal medium containing PNPP, while it showed normal growth when Na2HPO4 was added to the medium. The enzyme appears to be associated with the surface of the cell, where it may function to acquire inorganic phosphate from organic phosphomonoesters in acidic conditions, which could play an important role in the survival and growth of C. perfringens in the host tissue.

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Section: Discussionmentioning

confidence: 99%

Genetic and biochemical analysis of a class C non-specific acid phosphatase (NSAP) of Clostridium perfringens

et al. 2010

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“…Such a phosphateirrepressible enzyme is rare but not exceptional. Two other bacteria, Capnocytophaga and Bacteroides ruminicola, synthesize constitutive and phosphate-irrepressible alkaline phosphatase (Poirier & Holt, 1983;Cheng & Costerton, 1973). Another special feature of the 2. mobilis alkaline phosphatase is its low specific activity, which is at least 8.4 times lower than that in E. coli after derepression.…”

Section: Discussionmentioning

confidence: 99%

Phosphate-irrepressible Alkaline Phosphatase of Zymomonas mobilis

Michel

Baratti

1989

Microbiology

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The phosphate regulation and subcellular location of the hydrolytic enzyme alkaline phosphatase were investigated in the Gram-negative bacterium Zymomoms mobilk. The biosynthesis of alkaline phosphatase was not derepressed at a low phosphate concentration as is generally observed in other micro-organisms, nor was it repressed by high phosphate concentrations in the medium. The enzyme level was rather constant during the growth phases in batch culture, at a value at least 8-4-fold lower than that observed in Escherichia coli. The alkaline phosphatase of Z. mobilis was found associated with the membrane fraction after cell disruption, osmotic shock treatment or spheroplast formation. This is a rather unusual location, since most of the alkaline phosphatases from Gram-negative bacteria have been shown to be periplasmic enzymes. Activity staining on polyacrylamide gels after two-dimensional electrophoresis revealed two isoforms of alkaline phosphatase, each of approximate molecular mass 56 kDa. These two forms belong to a group including the more basic envelope proteins of 2. mobilis. Our results indicate that the enzyme from 2. mobiZis differs markedly from typical alkaline phosphatases of other Gram-negative bacteria.

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“…Capnoqtophaga gingiualis has been shown to produce a range of hydrolytic enzymes (Shibata e t a/., 1992;Poirier & Holt, 1983;Nakamura & Slots, 1982). The saccharolytic glpcosidase enzymes include a-and p-glucosidases, N-acetylglucosaminidase and a-and P-galactosidases (Spratt, 1994).…”

Section: Introductionmentioning

confidence: 99%

“…Enzymes which contribute to proteolytic activity include try pin-like protease and aminopeptidase (Shibata e t al., 1992; Spratt e t a/,, 1995). Phosphatase activity is also apparent (Poirier & Holt, 1983). C.gingivalis has been reported to ferment glucose and other sugars (Socransky e t a/., 1979).…”

Section: Introductionmentioning

confidence: 99%

Capnocytophaga gingivalis: effects of glucose concentration on growth and hydrolytic enzyme production

Spratt¹,

Greenman²,

Schaffer³

1996

Microbiology

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In chemostat culture, the microaerophilic, CO, requiring, gingival-plaqueassociated bacterium Capnocytophaga gingivalis responded to the addition of glucose (1-6 g I-') by doubling its growth rate and increasing its biomass yield fivefold. The data suggest that the glucose is catabolized by a fully aerobic route. Rather than repressing hydrolytic enzymes which might be associated with pathogenic properties, glucose enhanced the specific activity of aminopeptidase, trypsin-like protease, acid and alkaline phosphatase and aglucosidase in comparison with a control culture grown in a tryptonekhiamin medium. Thus, the supply of glucose could be of importance in maximizing the pathogenic potential of this organism. Keywords

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Acid and alkaline phosphatases of Capnocytophaga species. I. Production and cytological localization of the enzymes

Cited by 23 publications

References 40 publications

Genetic and biochemical analysis of a class C non-specific acid phosphatase (NSAP) of Clostridium perfringens

Genetic and biochemical analysis of a class C non-specific acid phosphatase (NSAP) of Clostridium perfringens

Phosphate-irrepressible Alkaline Phosphatase of Zymomonas mobilis

Capnocytophaga gingivalis: effects of glucose concentration on growth and hydrolytic enzyme production

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