Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q96DG6 (Pseudomonas)
 76,258 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The transformation of inosine into 5'-inosine acid by Pseudomonas trifolii cells was studied. The synthesis of 5'-inosine acid can be performed by both live intact and dry cells. The effectiveness of inosine phosphorylation depends on the ratio of the inosine and phosphate donor concentrations and the amount of cells. The temperature and pH effect on activity of nucleoside phosphotransferase, phosphomonoesterase and 5'-nucleotidase has been studied. The influence of surface active substances and metal ions on the synthesis of 5'-inosine acid has been investigated. Optimal conditions for the inosine transformation by the above culture have been established.
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PMID:[Study of inosine transformation into 5'-inosinic acid by the culture of Pseudomonas trifoli]. 0 21

An alkaline phosphatase mutant of Pseudomonas aeruginosa exhibiting both regulatory and catalytic changes was isolated. Under repression conditions (i.e. high inorganic phosphate (Pi)) the mutant culture produced an alkaline phosphatase (APase) displaying significant activity against both beta-glycerol phosphate (betaGP) and p-nitrophenyl phosphate (pNPP), while the wild type displayed no activity directed towards these substrates under the same conditions. In vivo, the mutant enzyme's ratio of specific activities was 45:1 in favour of betaGP versus pNPP, whereas this ratio was reversed to 1:9 betaGP versus pNPP for the same enzyme isolated from mutant cells. In addition, the kinetic parameters and stability requirements for the mutant-derived enzyme was altered in comparison with those of the wild type. A study of lipopolysaccharide (LPS) preparations from both the mutant and wild type indicated the mutant to be deficient in the core region of its LPS. The authors propose that the modifications in the catalytic activity of the mutant enzyme, demonstrated in vivo, are due to a change in the enzyme's microenvironment.
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PMID:An alkaline phosphatase mutant of Pseudomonas aeruginosa. 1. Effects of regulatory, structural, and environmental shifts on enzyme function. 2 29

Since 1973 30 patients with urinary tract infections (UTI) or pyelonephritis have been treated with sisomicin, a new aminoglycoside, in a daily dose of 2 mg/kg for a period of seven to nine days. From a clinical point of view the result of treatment was good. Complete resolution was achieved in 17 patients, improvement in nine, and there was no effect in four patients. Thirty-five causative organisms (Escherichia coli = 23, Proteus sp. = 7, Klebsiella sp. = 3, Pseudomonas aeruginosa = 1, Citrobacter = 1) were isolated before treatment. Thirty of the organisms were eliminated during treatment, but seven reappeared during the follow-up period; five strains persisted. Side effects observed consisted of reversible increase of serum creatinine in four patients, excretion of granular casts in 14 patients, and a transient rise of alkaline phosphatase, SGOT and/or SGPT in five patients. No signs of ototoxicity or any other adverse reactions were found and local tolerance was good. In 20 patients blood samples for assay were obtained daily one hour after i. m. injection of 1.0 mg/kg. No evidence of drug accumulation in the serum was found: the mean serum concentrations one hour after injection remained between 3.4 and 3,9 microgram/ml during the entire treatment period. Sisomicin is a highly effective antibiotic for the treatment of UTI caused by gramnegative pathogens. On account of its potential toxicity however, it should be used, like other aminoglycosides, only in selected cases.
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PMID:[Efficacy, tolerance, and pharmacokinetics of sisomicin in urinary tract infections (author's transl)]. 10 44

Whole cells of Pseudomonas aeruginosa possess rhodanese activity. The enzyme can be released by rapidly resuspending the cells in cold Tris--HCl buffer. Approximately 95% of the rhodanese activity is released by cold shock. Release of the enzyme can be inhibited either by preincubating the cells with Mg2+ or by incorporating Mg2+ into the shocking buffer. The effect of Mg2+ can be reversed by washing the cells twice with buffer prior to cold shock. While rhodanese can be released from P. aeruginosa by cold shock, lactic dehydrogenase, a cytoplasmic enzyme, remains within the cell. Diazo-7-amino-1,3-napthalenedisulfonic acid, a compound which does not penetrate the cytoplasmic membrane, completely inactivated rhodanese and alkaline phosphatase, a periplasmic enzyme, whereas lactic dehydrogenase retained its full activity. These data suggest that rhodanese in P. aeruginosa, like alkaline phosphatase, is located distal to the cytoplasmic membrane in the periplasmic space. Electron micrographs also show that portions of the lipopolysaccharide outer membrane are shed from the cell during cold shock, while cells preincubated with Mg2+ did not release segments of their outer membrane.
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PMID:Release of rhodanese from Pseudomonas aeruginosa by cold shock and its localization within the cell. 11 Apr 32

The conditions necessary for the secretion of phospholipase C (phosphatidylcholine cholinephosphohydrolase) by Pseudomonas aeruginosa were studied. Enzyme secretion by washed cell suspensions required a carbon source and ammonium, potassium, and calcium ions. The calcium requirement could be substituted by magnesium and strontium but not by copper, manganese, cobalt, or zinc. During growth in liquid medium, cells secreted phospholipase C during late logarithmic and early stationary phases. Secretion was repressed by the addition of inorganic phosphate but not by organic phosphates, glucose, or sodium succinate. Studies with tetracycline indicated that de novo protein synthesis was necessary for the secretion of phospholipase C and that the exoenzyme was not released from a preformed periplasmic pool. Similarly, extraction of actively secreting cells with 0.2 M MgCl2 at pH 8.4 solubilized large quantities of the periplasmic enzyme alkaline phosphatase but insignificant amounts of phospholipase C. Bacteria continued to secrete enzyme for nearly 45 min after the addition of inorganic phosphate or rifampin.
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PMID:Secretion of phospholipase C by Pseudomonas aeruginosa. 11 87

Pseudomonas aeruginosa (ATCC 9027) releases four periplasm-located enzymes, i.e., ribonuclease (EC 3.1.4.22; EC 3.1.4.23), alkaline phosphatase (EC 3.1.3.1), cyclic-2', 3'-phosphodiesterase (EC 3.1.4.d), and 5'-nucleotidase (EC 3.1.3.5) into the medium during growth. Ribonuclease and alkaline phosphatase are classed as enzymes which are readily extracted by osmotic shock and spheroplast formation whereas cyclic-2',3'-phosphodiesterase and 5'-nucleotidase are classed as enzymes which are not readily extracted by these procedures. In view of the relative ease of extraction of the former enzymes it is suggested that the lattter enzymes, cyclic-2',3'-phosphodiesterase and 5'-nucleotidase, are bound and located in the periplasm in a manner different to ribonuclease and alkaline phosphatase.
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PMID:The release and characterization of some periplasm-located enzymes of Pseudomona aeruginosa. 18 95

The activity of phosphohydrolase (acid, alkaline, pyrophosphatase) was studied in two strains of Pseudomonas maltophilia: VCM-B-591 and SSE-B-715. The activity of these enzyme systems in these strains was found to be much higher than in other Pseudomonas species, viz. Ps. aeruginosa VCM-B-889, Ps. fluorescens VCM-B-553, Ps. geniculata SSE-B-338, and in E. coli B. The phosphohydrolase activity of Ps. maltophilia varied depending on the growth phase of the culture. The highest activity of acid phosphatase was registered in the middle of the exponential phase for the strain VCM-B-591 and at the beginning of this phase for the strain SSE-B-715. The activity of alkaline phosphatase was maximal, for both of the strains VCM-B-591 and SSE-B-715, at the beginning of the logarithimic growth phase. The pyrophosphatase activity of the two strains had "two peaks" at the beginning and by the end of the logarithmic phase of growth. Incubation of Ps. maltophilia cells in media without orthophosphate did not result in an increase of their phosphohydrolase activity.
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PMID:[Phosphohydrolase activity of Pseudomonas maltophilia]. 23 Nov 88

Ninety-one strains of Pseudomonas pseudomallei were tested in the API 20E system and in equivalent conventional tests. Except for utilisation of citrate there was good correlation between API and conventional tests. Seven-digit profiles were constructed from each strain after 48 hours' incubation, and numerical codes 2 006 727, 2 206 706, 2 206 707, and 2 206 727 accounted for 77% of strains tested. API 20 E, in combination with tests for heat stability of alkaline phosphatase, resistance to colistin and gentamicin, oxidative attack only of glucose, and acid from maltose, was found to provide a simple method for positive identification of all strains of this organism in two days.
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PMID:Identification of Pseudomonas pseudomallei in the clinical laboratory. 38 28

We report the development and testing of an enzyme-linked immunosorbent assay with excellent sensitivity for the detection of Haemophilus influenzae type b (HI(b)) antigen in clinical specimens from patients with HI(b) meningitis. The assay, an indirect sandwich technique, uses polystyrene balls as a solid phase and an alkaline phosphatase-labeled goat anti-rabbit globulin conjugate. Specimens are incubated with polystyrene balls armed with burro anti-HI(b) antiserum, and recognition antibody is visualized by addition of alkaline phosphatase-labeled anti-globulin, together with the enzyme substrate p-nitrophenyl phosphate. Concentrations of antigen are determined from standard curves prepared by using purified HI(b) capsular antigen polyribophosphate. The assay reproducibly detects polyribophosphate at concentrations between 1 and 5 ng/ml. Cross-reactions have not as yet been encountered in simulated and authentic clinical specimens containing other species including Escherichia coli, Klebsiella pneumoniae, group B Streptococcus, Pseudomonas aeruginosa, Streptococcus pneumoniae, Staphylococcus aureus, Neisseria meningitidis, and Listeria monocytogenes. In preliminary tests with 11 spinal fluid specimens, 2 serum specimens, and 5 urine specimens from patients with culture-proved HI(b) meningitis, antigen was detected in all specimens in concentrations ranging from 1 to 7,000 ng/ml. Antigen was not detected in any of 62 clinical specimens which were culture negative for HI(b), including 11 spinal fluid specimens from patients with bacterial meningitis caused by microorganisms other than HI(b). The enzyme-linked immunosorbent assay technique described here is considerably simpler than radioimmunoassay and, based on concurrent tests with 14 positive clinical specimens, may be more sensitive than counterimmunoelectrophoresis. It seems, therefore, to hold considerable promise for clinical use in rapid detection of systemic HI(b) infections.
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PMID:Indirect sandwich enzyme-linked immunosorbent assay for rapid detection of Haemophilus influenzae type b infection. 39 14

Mutants of Pseudomonas aeruginosa strain PAKS-I which are defective in the formation of extracellular protease activity have been characterized. The mutants produced between approximately 1 and 25% of the protease activity of the wild type and no strains completely lacking extracellular protease were found, even after repeated mutagen treatment. Most mutants also had changed activities of extracellular staphylolytic enzyme, lipase and lecithinase. Four of 13 mutants were unable to release alkaline phosphatase and staphylolytic enzyme into the medium in contrast to the wild type. Serotype, phage type and biochemical reactions were essentially unchanged. The results indicate that some of the mutations affected the cell envelope structure of function leading to decreased ability to release extracellular proteins, and that other mutations possibly affected a common regulatory mechanism for extracellular enzymes.
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PMID:Protease-deficient mutants of Pseudomonas aeruginosa: pleiotropic changes in activity of other extracellular enzymes. 41 77


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