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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hiraga, Sota (Osaka University, Osaka, Japan). Regulation of synthesis of alkaline phosphatase by deoxyribonucleic acid synthesis in a constitutive mutant of Bacillus subtilis. J. Bacteriol. 91:2192-2199. 1966.-It was found that synthesis of alkaline phosphatase (APase) correlated with deoxyribonucleic acid (DNA) synthesis in a partially constitutive mutant of Bacillus subtilis. When cultures of the mutant were made to undergo synchronous growth by germination of spores in an excess-phosphate medium, synthesis of APase was repressed at the beginning of DNA synthesis. If the initiation of DNA synthesis was inhibited by thymine starvation, the repression of APase was not observed. When DNA synthesis, previously initiated, was inhibited by thymine or uracil starvation, or by addition of mitomycin C, the repression was partially released at a later stage. In contrast, this correlation between repression and DNA synthesis was not observed in a repressible strain.
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PMID:Regulation of synthesis of alkaline phosphatase by deoxyribonucleic acid synthesis in a constitutive mutant of Bacillus subtilis. 495 12

Hou, Cynthia I. (University of British Columbia, Vancouver, B.C., Canada), Audrey F. Gronlund, and J. J. R. Campbell. Influence of phosphate starvation on cultures of Pseudomonas aeruginosa. J. Bacteriol. 92:851-855. 1966.-The changes occurring in Pseudomonas aeruginosa during phosphate starvation in a phosphate-deficient medium were assessed by measuring alterations in optical density, viable-cell count, chemical composition, and ribosome patterns. After a 24-hr period of starvation, optical density, protein, and deoxyribonucleic acid per milliliter of culture increased, whereas ribonucleic acid decreased. Extensive ribosomal degradation was apparent from sucrose density gradient centrifugation patterns. The induction of an alkaline phosphomonoesterase during phosphate starvation was observed. A linear response of phosphate-starved cells to low levels of phosphate supplied exogenously was evident from optical-density measurements, and a threshold requirement for phosphate analogous to the "energy of maintenance" was not detected.
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PMID:Influence of phosphate starvation on cultures of Pseudomonas aeruginosa. 495 48

1. The purification of the ;vegetative' alkaline phosphatase of Bacillus subtilis 168 was simplified by ionic elution of the enzyme from intact cells. 2. The enzyme has a molecular weight of about 70000 and treatment of the enzyme with 10mm-hydrochloric acid or 6.0m-guanidine hydrochloride, beta-mercaptoethanol (0.1m) gives rise to enzymically inactive subunits. 3. The amino acid composition of the enzyme was determined. The N-terminal residue determined by the DNS chloride method is glycine. 4. The properties of this enzyme were compared with the ;sporulation' alkaline phosphatase of the same strain. 5. Although the ;sporulation' enzyme differs from the ;vegetative' enzyme in its physiology of appearance and apparent mRNA stability, an examination of properties of the enzymes revealed no differences. 6. The enzyme from both cell forms is bound to the particulate fraction of cell extracts, but can be solubilized by high concentrations of magnesium chloride; removal of the magnesium chloride, by dialysis, results in precipitation of both enzymes. Both enzymes can be removed from intact cells by ionic elution. 7. The ;vegetative' and ;sporulation' enzymes have identical pH optima, K(m) and K(i) values and electrophoretic mobilities in cellulose acetate. 8. Their half-life is 28min at 65 degrees C and their Q(10) is 1.25. 9. The molecular size determined by gel filtration on Sephadex G-100 is about 69000. 10. ;Vegetative' and ;sporulation' forms gave precipitin lines that were continuous and non-spurred when tested against antiserum prepared against the ;vegetative' enzyme. 11. The ;sporulation' alkaline phosphatase appears to be associated with stage II of sporulation and appears to be induced by something specifically concerned in sporulation and not by phosphate starvation.
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PMID:Sporulation in Bacillus subtilis 168. Comparison of alkaline phosphatase from sporulating and vegetative cells. 500 77

The physiological and genetic controls operating on phosphate-regulated promoters were studied in greater detail. This was done by defining the control for three phosphate-regulated genes: phoA, psiE, and psiO. Each is highly inducible by phosphate starvation. Individually, these phosphate-starvation-inducible, psi, genes at the same time show common and differing features in their molecular control. The phoA gene, encoding alkaline phosphatase, is specifically induced by phosphate starvation. It is negatively controlled by phoR as well as by the phosphate-specific transport (PST) system in Escherichia coli. phoA induction is positively controlled by the phoB, M, and R products; it is unaffected by the cAMP and CAP system. The psiE and psiO genes were studied by using strains with lacZ fused to their respective promoters. psiE-lacZ is induced by phosphate-, carbon- or nitrogen-limited growth. Genetically, psiE-lacZ induction is partially phoB and phoR-dependent. However, its expression is phoM-independent. This implies that phoB/phoR coupled control differs from phoB/phoM coupled control. Repression of psiE-lacZ is substantially altered in only some PST mutants, such as phoT. In addition, psiE-lacZ is negatively controlled by the cAMP and CAP system. psiO-lacZ is induced by phosphate-, carbon- or nitrogen-limited growth or by anaerobiosis. Its expression is unaffected by any pho mutation that has been previously described. A cell density-dependent induction of psiO-lacZ is observed in lon mutants. Also, psiO-lacZ is negatively controlled by the cAMP-CAP system. In summary, these results demonstrate that co-ordinately regulated promoters can have some common regulatory elements while, at the same time, not sharing other controlling factors.
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PMID:Overlapping and separate controls on the phosphate regulon in Escherichia coli K12. 630 24

phoB is a positive regulatory gene for phoA, which codes for alkaline phosphatase, as well as for other genes belonging to the phosphate (pho) regulon whose expression is inducible by phosphate limitation in Escherichia coli. A hybrid plasmid that contains a phoB-lacZ fused gene was constructed in vitro. This plasmid enabled us to study phoB gene expression by measuring the beta-galactosidase level in the cells. The plasmid was introduced into various regulatory mutants related to the phosphate regulon, and phoB gene expression in these strains was studied under limited and excess phosphate conditions. It was found that the regulation of phoB expression was very similar to that of phoA expression. Expression of both genes was induced by phosphate starvation. Both genes were constitutively expressed in phoR, phoS, phoT and phoU mutants and were not expressed in a phoR-phoM double mutant. The implications of these findings for the regulatory mechanism of the pho regulon are discussed.
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PMID:Regulation of the pho regulon in Escherichia coli K-12. Genetic and physiological regulation of the positive regulatory gene phoB. 631 Jan 21

The phoB gene, which encodes a positive control factor for a number of phosphate-regulated genes in Escherichia coli, was cloned into multicopy plasmid pBR322. A phoB-cat fusion that expressed chloramphenicol transacetylase from the phoB promoter was constructed. Studies of the expression of the phoB-cat fusion showed that the pattern of regulation of the phoB gene was similar to that of the phoA gene, the structural gene for alkaline phosphatase. The phoB gene was derepressed under conditions of phosphate starvation, was constitutively expressed in a phoR background, and required the phoM gene product for expression in a phoR strain. Finally, a functional phoB product was required for its own synthesis. Our results indicate either that phoA gene expression responds directly to the concentration of the phoB gene product in cells or that the phoA and phoB controlling elements are quite similar.
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PMID:Analysis of regulation of phoB expression using a phoB-cat fusion. 631 14

The alkaline phosphatase of Plectonema boryanum shows a considerable increase in activity following placement of the cells in a phosphate free medium. Five days of phosphate starvation result in a 14-fold increase of alkaline phosphatase activity. Growth in the presence of inhibitors of transcription and translation indicate that the synthesis of the enzyme is de novo. Orthophosphate causes an immediate inhibition of enzyme activity. Enzyme was extracted from P. boryanum with lysozyme or polymyxin B treatment in order to make comparative studies of cell bound and cell free enzyme. Of several enzyme specific inhibitors tested, mercuric chloride was the most effective. Temperature studies showed that the cell bound enzyme was most active at 40 degrees C while the cell free enzyme was most active at 70 degrees C. The pH optimum was 9 for the cell free enzyme, and 8.8 for the cell bound. The enzyme was tested to determine if it could hydrolyse a number of different organic compounds. It hydrolysed p-nitrophenol phosphate 100%, fructose-6-phosphate 45%, beta-glycerol phosphate 25% and other compounds to a lesser degree. Of seventeen other Cyanobacteria tested for alkaline phosphatase, all were positive, and of these eleven were inducible for the enzyme. Ten of the isolates released some of the enzyme into the culture medium. Michaelis constants for the enzyme were also determined.
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PMID:Physiological aspects of alkaline phosphatase in selected cyanobacteria. 679 13

The localization of alkaline phosphomonoesterase (EC 3.1.3.1) was studied in two Pseudomonas species: P. maltophilia VKM B-591 and P. aeruginosa VKM B-889. The former species is characterized by constitutive synthesis of alkaline phosphatase, and its level is not regulated by orthophosphate in the medium. The enzyme of the latter species is orthophosphate-repressible. The two species differ also in the localization of the enzyme in the cell. Under the conditions of derepression (the absence of inorganic phosphate from the medium), the enzyme of the repressible strain of P. aeruginosa is actively synthesized on the membranes and secreted into the medium. Most of the enzyme activity (80--90%) is found in the cultural broth 4 h after phosphorus starvation. In P. maltophilia, 90% of the synthesized enzyme is found in the membrane fraction irrespective of the incubation time under the same conditions. Apparently, a correlation exists between the regulation of alkaline phosphatase synthesis and the localization of the enzyme. It is likely that in P. aeruginosa, just as in E. coli, alkaline phosphatase is synthesized on polysomes attached to the membrane, with the subsequent translocation of the enzyme to the site of its localization. P. maltophilia appears to have a defect in one of its membrane component responsible for the regulation of the synthesis and the secretion of the enzyme in the cell.
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PMID:[Relationship of Pseudomonas maltophilia alkaline phosphatase to its membranes]. 679 9

Studies were made on memory of the rhythmic change in activity of duodenal alkaline phosphatase in rats. During starvation, the peak enzyme activity decreased gradually disappearing in 4 days. The peak activity of duodenal alkaline phosphatase was retained by feeding starch diet for 4 days instead of starvation for 4 days, but not by feeding casein diet for the same period. Starvation for one day after feeding casein diet for 4 days resulted in disappearance of the peak activity. However, the peak activity was still retained after one day of starvation after 4 days on starch diet. Therefore, starch feeding appears to be important in the memory of the rhythmic change in activity of duodenal alkaline phosphatase.
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PMID:Memory of the rhythmic change in activity of duodenal alkaline phosphatase in rats. 686 51

A new form of alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) has been identified in the yeast Saccharomyces cerevisiae. Utilizing either synthetic or natural substrates, the enzyme exhibited a broad pH activity curve with maximum activity between 8.5 and 9.0. The enzyme was nonspecific with respect to substrate, attacking a variety of compounds containing phosphomonoester linkages, but has no detectable activity against polyphosphate, pyrophosphate or phosphodiester linkages. The enzyme exhibited an apparent Km of 0.25 mM with respect to p-nitrophenyl phosphate, 0.38 mM with respect to alpha-naphthyl phosphate, and 1.0 mM with respect to 5'AMP. The enzyme is regulated in a constitutive manner and its activity does not increase during phosphate starvation or sporulation, as does the repressible alkaline phosphatase. The enzyme is tightly bound to a particulate fraction of the cell, tentatively identified as the tonoplast membrane. It is not solubilized by treatment with high concentrations of NaCl, KH2PO4 or chaotropic agents. Triton X-100 (0.1%) solubilizes 12% of the particulate activity. This enzyme is differentiated from the other alkaline phosphatases found in yeast by its chromatographic elution DEAE-cellulose, kinetic parameters, heat stability and pH stability, as well as its particulate nature. This particulate alkaline phosphatase was found in every strain examined. It has a significantly lower specific activity in the phoH mutant and a higher activity in the acid phosphatase constitutive mutant A137.
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PMID:A particulate form of alkaline phosphatase in the yeast, Saccharomyces cerevisiae. 701 3


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