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

An immunological study of anthranilate synthetase (ASase) has been initiated using quantitative precipitation, enzyme neutralization, and immunodiffusion methods. Cross-reactivity of anthranilate synthetase-anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase (ASase-PRTase) from Escherichia coli, Klebsiella aerogenes, and Salmonella typhimurium and ASase from Serratia marcescens and Pseudomonas putida was detected with antibodies to ?E. coli trypsin-treated ASase. Cross-reactivity of antigens was also obtained with S. marcescens anti-ASase. Indices of dissimilarity verified the overall structural similarity of ASase-PRTase from E. coli, K. aerogenes, and S. typhimurium and the divergence from S. marcescens ASase. Further divergence of these enzymes from ASase in B. subtilis and P. putida was apparent. Precipitation of ASase components I and II (ASase CoI and ASase CoII) was obtained using anti-ASase or antiserum fractionated to contain component-specific antibodies. Anti-ASase inhibited enzyme activity to binding to determinants on both subunits. Anti-ASase CoI inhibited the ammonia-dependent reaction and interfered with amide transfer from glutaminyl-ASase CoII. Anti-ASase CoII inhibited the glutamine reaction by blocking amide transfer. Enzyme neutralization experiments indicate more conservation of determinants at the active site region of ASase CoII compared to ASase CoI in the enterobacteria. A particulate form of ASase-PRTase in E. coli, K. aerogenes, and S. typhimurium could be distinguished by quantitative precipitation and immunodiffusion.
 ...
PMID:Immunological study of anthranilate synthetase. 5 Mar 16

Pseudomonas aeruginosa strain P15 produces not only pyocin R1 and phage PS10, but also a substance having a flexuous rod structure, the nature of which is so far unknown. A variant strain (P15--40) was obtained which produced these flexuous particles more effectively than the original strain, and the particles were purified to homogeneity and investigated. Several strains of P. aeruginosa were found to be killed by the particles. It was concluded that the flexuous rod-like particles are not related to pyocin R1 or phage PS10, but represent a new pyocin, which we have designated as pyocin F1. Pyocin F1 showed a different action spectrum and a different pattern on SDS-polyacrylamide gel electrophoresis from either pyocin R1 or phage PS10. The killing activity of pyocin F1 was of single-hit type. The activity was not affected by anti-R1, anti-R1-core or anti-PS10, or by DNase, RNase, pronase or trypsin, but was completely destroyed by treatment at 70 degrees C for 10 min. Some cofactor was required for the adsorption of this pyocin on sensitive bacteria. Another flexuous bacteriocin was also found and named pyocin F2.
 ...
PMID:Biochemical properties of a new flexuous bacteriocin, pyocin F1, produced by Pseudomonas aeruginosa. 10 91

The effect of the iron content of the medium on the yields of extracellular products by seven distinct strains of Pseudomonas aeruginosa was examined. All strains showed at least an 85% decrease in toxin A yields when grown in medium containing 5.0 mug of iron per ml (high iron) as compared to 0.05 mug/ml (low iron), whereas bacterial growth increased approximately twofold. During the course of examining extracellular products produced by P. aeruginosa, we found many strains that produced an extracellular factor which agglutinated erythrocytes. This hemagglutinin was nondialyzable, heat stable, and resistant to Pronase and trypsin. The effect of iron on extracellular yields of hemagglutinin was strain dependent; four of seven strains showed decreases in hemagglutinin yields in high-iron medium. Similarly, the effect of increasing the iron concentration of the growth medium on yields of total extracellular proteases or on elastase was strain dependent. The amount of total extracellular protein was decreased by at least 31% in the high-iron medium for all strains of P. aeruginosa examined. Detailed studies on one strain (WR-9) showed that, in the presence of increasing amounts of iron in the medium, the extracellular yields of toxin A, protease, and hemagglutinin were decreased in a similar manner. In addition, the kinetics of release of these extracellular products were similar at a given iron concentration. Thus it appears that the yields of other extracellular products of P. aeruginosa besides toxin A are influenced by the concentration of iron in the growth medium.
 ...
PMID:Influence of iron on yields of extracellular products in Pseudomonas aeruginosa cultures. 10 50

The present study indicates that crystalline elastase of Pseudomonas aeruginosa is a very potent inactivator of human plasma alpha 1-proteinase inhibitor, the enzyme (E) inactivated the inhibitor (I) almost completely within 1 h at 25 degrees C at a molar ratio of E/I = 1:100. The crystalline P. aeruginosa protease also inactivated the inhibitor, but 100-fold less. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the alpha 1-proteinase inhibitor inactivated by the elastase and protease showed decreases in molecular weight of approximately 5,000 and 10,000, respectively. Regeneration of trypsin was negligible even when bovine trypsin-alpha 1-proteinase inhibitor complex (E/I = 1.0) was treated with the elastase. The affinity of alpha 1-proteinase inhibitor to trypsin was much higher than that to elastase. It was suggested that, assuming the pseudomonal proteases are produced and can inactivate alpha 1-proteinase inhibitor in vivo during pseudomonal diseases, the loss of alpha 1-proteinase inhibitor activity may permit the endogenous serine proteases to cause tissue destruction.
 ...
PMID:Protease and elastase of Pseudomonas aeruginosa: inactivation of human plasma alpha 1-proteinase inhibitor. 11 Jun 91

A noncovalent complex of the apoprotein (1-104) and cyanogen bromide heme fragment containing residues 1 to 65, (1-65) H, has been prepared from horse heart cytochrome c. Conditions under which the redundant portions of the ferrous complex can be removed by limited trypsin digestion have been devised. The complementing fragments have been isolated from the derived complexes and four apofragments and one heme fragment have been identified in the amino acid sequence of cytochrome c. They are (39-104), (40-104), (54-104), (56-104), and (1-53)H. The formation of an ordered ferric complex composed of one heme fragment and one apofragment for the cases (1-53)H (39-104), (1-53)H-(40-104), (1-53)H-(54-104), and (1-53)H-(56-104) has been demonstrated by the quenching of the tryptophan 59 fluorescence and the regain of biological activity in a cytochrome b2 assay. The apparent dissociation constant has been estimated as less than 3 X 10(-7) M in all the aforementioned cases. Thus, the region (between residues 38 and 57) of the amino acid sequence permissible for cleavage without disruption of the ordered structure indicated by the present in vitro experiments corresponds to that (between residues 38 and 57) evolutionally deleted in the three-dimensional structure of Pseudomonas aeruginosa cytochrome c551 discovered by Dickerson et al. (Dickerson, R.E., Timkovich, R., and Almassy, R.J. (1976) J. Mol. Biol. 100, 473-491).
 ...
PMID:Formation of a biologically active, ordered complex from two overlapping fragments of cytochrome c. 19 Feb 31

The amino acid sequence of a 51-residue tryptic peptide of citraconylated [1-14C]carboxamidomethyl-labeled Escherichia coli GMP synthetase was determined by sequenator analyses of the intact peptide and fragments obtained by cleavage of the peptide with cyanogen bromide, trypsin, and Staphylcoccus aureus strain V8 protease. The cysteine residue of this peptide fragment is essential for glutamine-dependent GMP synthesis activity and is implicated in formation of a hypothetical covalent glutamyl-enzyme intermediate. There is essentially cysteine-containing regions of two other glutamine amidotransferases, Pseudomonas putida anthranilate synthetase Component II and chicken liver formylglycinamide ribonucleotide amidotransferase. There is, however, a cluster of amino acids with "antipathy" for helix formation and a "nonessential" cysteine of anthranilate synthetase Component II.
 ...
PMID:Amino acid sequence of a peptide containing an essential cysteine residue of Escherichia coli GMP synthetase. 21 34

Pyocin inhibition of Neisseria gonorrhoeae and its feasibility as a gonococcal typing scheme were examined. Mitomycin C-induced pyocin lysates of Pseudomonas aeruginosa were able to selectively inhibit the growth of gonococcal strains. The particles associated with the inhibitory activity were non-dialyzable, heat labile, Pronase sensitive, trypsin resistant, and of large molecular weight by membrane and gel filtration techniques. The inhibitory activity was shown to be specific by absorption with sensitive and insensitive strains of N. gonorrhoeae and P. aeruginosa. Partial purification of pyocin lysates by ammonium sulfate precipitation followed by ultracentrifugation revealed phagelike particles consistent with high-molecular-weight R-type pyocines. These particles were associated with increased inhibitory activity and could be seen associated with the gonococcal cell surface. One hundred and six gonococcal strains could be differentiated on the basis of their sensitivity of 23 pyocin extracts. Thirty different patterns of pyocin inhibition were seen. Isolates from different body sites from the same patient could generally be identified as being similar strains. Strains isolated from known consorts had the same patterns. In general, agreement between pyocin typing and available epidemiological information was good.
 ...
PMID:Pyocin sensitivity of Neisseria gonorrhoeae and its feasibility as an epidemiological tool. 40 41

Susceptibility testing by the broth dilution method showed that all the gram-positive but only some of the gram-negative bacteria tested were susceptible to the antitumor antibiotic, macromomycin (MCR; NSC 170105). The minimal inhibitory concentration for the susceptible organisms was less than 3 mug/ml. The action of MCR was bactericidal; however, at very high concentrations (50 mug/ml and above) some organisms occasionally escaped death. None of the escaped organisms was resistant to MCR. In combination with other commonly used antibiotics, MCR displayed partial synergy for Pseudomonas aeruginosa (from a minimal inhibitory concentration of >100 to 12.5 mug/ml with 100 mug of chloramphenicol per ml) and for Bacillus pumilus and Staphylococcus aureus (from 1.6 to 0.4 mug/ml and below) with polymyxin B. As with mammalian cells, (125)I-labeled MCR was irreversibly bound to both gram-positive and -negative bacteria. Treatment with trypsin of the (125)I-labeled MCR-exposed cells did not release the bound MCR or reverse its lethal effect. When in solution in a protective buffer at 4 degrees C, MCR was stable for up to 45 days; at 37 degrees C, however, 25% of its bactericidal activity was lost in 72 h. Loss of activity was enhanced 16-fold in the presence of both heated and unheated pooled human sera. Urine had no effect on the activity of MCR.
 ...
PMID:Bactericidal activity of macromomycin, a antitumor antibiotic. 40 34

The isoelectric points of three proteases (I, II and III), separated from culture supernatants of Pseudomonas aeruginosa strain PAKS-I by isoelectric focusing, were 8.5, 6.6 and 4.5 respectively. Collagenase activity was not detected. More than 75% of the extracellular protease activity of this strain was due to protease II. This enzyme also possessed elastase activity. When purified by ammonium sulphate precipitation, isoelectric focusing and gel chromatography, protease II showed one band on disc electrophoresis and one band on conventional immunoelectrophoresis. The pH optimum, stability and effect of inhibitors and substrate concentration were examined. The molecular weight was 23000 +/- 5000. Protease II was lethal for mice when injected intraperitoneally at a high dose (minimum lethal dose 0.1 mg). Dermonecrosis and subcutaneous haemorrhages were produced in new-born mice upon subcutaneous injection of 10 microgram protease II. A sensitive test for cytotoxicity showed no evidence of cytoplasmic membrane damage to HeLa cells or human diploid embryonic lung fibroblasts by protease II. Morphological changes similar to those produced by trypsin were found.
 ...
PMID:Purification and properties of a protease with elastase activity from Pseudomonas aeruginosa. 41 76

Factors that promote oropharyngeal colonization of seriously ill patients with gram-negative bacilli are as yet poorly understood. In this investigation, 34 subjects who required intensive care were studied; 18 (53%) were colonized with gram-negative bacilli. Oropharyngeal epithelial cells of all colonized patients contained adherent bacilli. Fewer alpha-hemolytic streptococci but greater numbers of Pseudomonas aeruginosa and Klebsiella pneumoniae (P less than or equal to 0.01) adhered in vitro to buccal epithelial cells from colonized patients than to cells from noncolonized patients. Adherence of bacilli to buccal cells was inhibited in vitro by concanavalin A but not by bovine serum albumin or phytohemagglutinin. Brief exposure of buccal cells to trypsin increased adherence of bacilli. Prior adherence of one species of bacilli inhibited subsequent adherence of a second species. These findings suggested that epithelial cells of the upper respiratory tract contain binding sites for gram-negative bacilli. Factors associated with serious illness appear to increase the availability of these binding sites, thus facilitating colonization of the upper respiratory tract with gram-negative bacilli.
 ...
PMID:Association of respiratory tract colonization with adherence of gram-negative bacilli to epithelial cells. 44 93


1 2 3 4 5 6 7 8 9 10 Next >>