Changes in the membrane bound alkaline phosphate of glucose and lactate grown vegetative cells of Bacillus subtilis SB15

Ghosh, Arati; Ghosh, B. K.

doi:10.1016/0006-291x(72)90298-7

Cited by 22 publications

(19 citation statements)

References 10 publications

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“…This indicates that the antigenic structures of IAPase and CAPase appeared di¡erent, and further suggests that these two proteins of S. marcescens are immunologically distinct enzyme species. Unlike the two types of APases reported from B. subtilis [10,18,22], the APases described in this study were distinct in their growth requirements, electrophoretic mobilities [3], chromatographic behavior, biochemical as well as immunological properties and therefore, were di¡erent isodynamic enzymes which probably arose from an independent genetic origin.…”

Section: Immunological Identitycontrasting

confidence: 59%

Evidence on the presence of two distinct alkaline phosphatases in Serratia marcescens

Bhatti¹

2000

FEMS Microbiology Letters

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Certain strains of Serratia marcescens synthesized two different types of alkaline phosphatase (APase), constitutive (CAPase) and inducible (IAPase) APases, in low phosphate medium. Synthesis of the IAPase was repressed in the presence of high phosphate. Purification and separation of these electrophoretically distinct APases was achieved by using fractional (NH 4 ) 2 SO 4 precipitation, adsorption on a DEAE-cellulose column and elution of enzymes by a linear sodium chloride gradient. Starch gel electrophoresis of certain fractions revealed the separation of not only IAPase from CAPase but its separation into four distinct isozymes. CAPase gave maximum enzyme activity around pH 9.5, whereas for IAPase a broad range of enzyme activity was found between pH 8.5 and 10.5. Reversible inactivation at low pH occurred for IAPase but very little with CAPase. CAPase was more thermolabile than IAPase at 95³C. The two APases were found to be distinct in their kinetic as well as immunological properties, suggesting two distinct enzyme species.

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Section: Immunological Identitycontrasting

confidence: 59%

Evidence on the presence of two distinct alkaline phosphatases in Serratia marcescens

Bhatti¹

2000

FEMS Microbiology Letters

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“…Members of this family are found in many bacteria and in eukaryotes such as human, mouse, Drosophila and Saccharomyces cerevisiae (Millan, 1986; Yang et al ., 2000; Narisawa et al ., 2003; Song, 2006). In Gram negative bacteria these enzymes are located in the periplasmic space (Torriani, 1990) while in Gram positive bacteria they are membrane bound (Ghosh et al ., 1977). PhoA from Gram negative E. coli and the PhoA homologue, PhoZ from Gram positive Enterococcus faecalis are well‐documented examples of alkaline phosphatases secreted via the ‘sec’ protein secretion pathway (Angelini et al ., 2001; Rosch and Caparon, 2004).…”

Section: Introductionmentioning

confidence: 99%

Genetic and biochemical properties of an alkaline phosphatase PhoX family protein found in many bacteria

Zaheer

Morton

Proudfoot

et al. 2009

Environmental Microbiology

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We report on the biochemical, phylogenetic and genetic regulation of PhoX, the major alkaline phosphatase protein from the soil bacterium Sinorhizobium meliloti. The protein is shown to be a member of a recently identified family of PhoX alkaline phosphatase proteins that is distinct from the well-characterized PhoA family. The mature S. meliloti PhoX protein is located in the periplasm and lacks a 76-amino-acid N-terminal Tat signal peptide. Its phosphatase activity was stimulated by Ca(+2) and was optimal at pH 9-11. Except for phytic acid and phosphatidic acid, the enzyme was active against a wide range of phosphorylated substrates (77 nucleotides, phosphorylated carbohydrates and amino acids) and thus exhibited low substrate specificity for C-O-P bonds. No C-P bond substrate was dephosphorylated while the protein was active with two of six phosphoramidate substrates (N-P bond) tested. Sinorhizobium meliloti phoX was induced when cells were starved for phosphorous and the induction was dependent on the PhoB-regulatory protein. We demonstrate by in vitro analysis that PhoB protein binds to two tandem 22 nt PhoB binding sites located 64-21 nt upstream from the phoX transcription start site. Analysis of 95 PhoX orthologues from diverse bacteria revealed two distinct phylogenetic groups of PhoX proteins. The two groups differed in having a conserved glycine (PhoX-I) or asparagine (PhoX-II) next to their putative catalytic Ca(+2) binding site. Analysis of the phoX promoter regions from many of these bacteria also revealed the presence of PhoB binding sites. Alkaline phosphatase proteins of either the PhoX or PhoA family (but rarely both) are found in many bacteria, thus it appears that these are functionally equivalent.

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“…The enzyme is a relatively nonspecific phosphomonoesterase that catalyses the removal of phosphate groups from a variety of small organic molecules as well as large biomolecules such as DNA and protein. In Gram negative bacteria the enzyme is located in the periplasmic space (Torriani, 1990) while in Gram positive bacteria this enzyme is membrane bound (Ghosh et al, 1977). In the cyanobacterium Synechococcus strain PCC 7942, the enzyme is periplasmic but remains bound to the cell wall or cytoplasmic membranes (Ray et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Identification of the gene for the monomeric alkaline phosphatase of Vibrio cholerae serogroup O1 strain

Majumdar

Ghatak

Ghosh

2005

Gene

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Changes in the membrane bound alkaline phosphate of glucose and lactate grown vegetative cells of Bacillus subtilis SB15

Cited by 22 publications

References 10 publications

Evidence on the presence of two distinct alkaline phosphatases in Serratia marcescens

Evidence on the presence of two distinct alkaline phosphatases in Serratia marcescens

Genetic and biochemical properties of an alkaline phosphatase PhoX family protein found in many bacteria

Identification of the gene for the monomeric alkaline phosphatase of Vibrio cholerae serogroup O1 strain

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