Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0519030 (Klebsiella)
 21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The degradative pathway of cyanuric acid [1,3,5-triazine-2,4,6(1H,3H,5H)-trione] was examined in Pseudomonas sp. strain D. The bacterium grew with cyanuric acid, biuret, urea or NH4+ as sole source of nitrogen, and each substrate was entirely metabolized concomitantly with growth. Enzymes from strain D were separated by chromatography on DEAE-cellulose and three reactions were examined. Cyanuric acid (1 mol) was converted stoichiometrically into 1.0 mol of CO2 and 1.1 mol of biuret, which was conclusively identified. Biuret (1 mol) was converted stoichiometrically into 1.1 mol of NH4+, about 1 mol of CO2 and 1.0 mol of urea, which was conclusively identified. Urea (1 mol) was converted into 1.9 mol of NH4+ and 1.0 mol of CO2. The reactions proceeded under aerobic or anoxic conditions and were presumed to be hydrolytic. Data indicate that the same pathway occurred in another pseudomonad and a strain of Klebsiella pneumoniae.
 ...
PMID:Ring cleavage and degradative pathway of cyanuric acid in bacteria. 390 35

Bacteriology was performed on 57 specimens collected by the Wimberley protected catheter bronchoscopy technique (PCB) from 42 ventilated patients with severe head trauma hospitalized in the neurosurgical intensive care unit to determine the etiology of their pneumopathy. All patients had a nasotracheal tube upon arrival at the intensive care unit. For each sample, smears were examined and cultures under aerobic and anaerobic conditions as well as with CO2 were performed. In 34 (59%) of the 57 cases, examination of smears allowed rapid diagnosis and appropriate chemotherapy. In 47 (82%) cases, culture was positive, with a single pathogen being recovered in half of cases. The most prevalent organisms among the 75 species isolated were S. aureus (38%), P. aeruginosa (15%), Klebsiella (12%), Haemophilus (8%), and Pneumococcus (9%). Consistency with positive cultures of blood or pleural effusion samples was recorded in 92% of cases. Narrow spectrum antibiotic therapy can be chosen according to the results of PCB bacteriology and rapid automated antibiotic sensitivity testing obtained within 24 hours. PCB is therefore recommended in pulmonary infections in intensive care units.
 ...
PMID:[Antibiotic therapy of pneumopathies in intensive care and protected distal bronchial samples]. 392 19

Pyruvate:flavodoxin oxidoreductase, the nifJ gene product of Klebsiella pneumoniae, was purified to homogeneity. Pyruvate:flavodoxin oxidoreductase, flavodoxin, and nitrogenase components I and II are the only proteins required for pyruvate-coupled nitrogenase activity. The physiological source of electrons to nitrogenase in K. pneumoniae is pyruvate. Flavodoxin from Azotobacter vinelandii was only one-third as effective as K. pneumoniae flavodoxin in transferring electrons from pyruvate:flavodoxin oxidoreductase to Azotobacter and Klebsiella nitrogenases. Ferredoxins from aerobic, anaerobic and photosynthetic nitrogen-fixing organisms, as well as benzyl viologen and methyl viologen, were ineffective in coupling pyruvate oxidation to nitrogenase activity. One mol each of acetyl-CoA, CO2, and ethylene are formed by pyruvate-supported acetylene reduction. The enzyme contains 8.0 +/- 0.6 mol of iron and 6.6 +/- 0.2 mol of acid-labile sulfide per mol of protein (Mr = 240,000). Pyruvate:flavodoxin oxidoreductase is irreversibly inactivated by air.
 ...
PMID:Electron transport to nitrogenase. Purification and characterization of pyruvate:flavodoxin oxidoreductase. The nifJ gene product. 635 5

A comparison was made of the results of blood cultures between 1974 and 1981 in unvented and transiently vented bottles of Tryptic soy broth under vacuum with CO2. A total of 14,646 isolates were available for statistical analysis. Significantly more isolates of Staphylococcus epidermidis, Staphylococcus aureus, Bacillus, Escherichia, Pseudomonas, Klebsiella, Serratia, Acinetobacter, Alcaligenes, Neisseria, and Candida were recovered from the vented bottle. Significantly more isolates of Corynebacterium, Haemophilus, Flavobacterium, Moraxella, Bacteroidaceae, and Peptostreptococcus were recovered from the unvented bottle.
 ...
PMID:Effects of atmosphere of incubation on recovery of bacteria and yeasts from blood cultures in Tryptic soy broth. 637 May 65

Oxaloacetate decarboxylase from Klebsiella aerogenes was shown to be composed of three different subunits alpha, beta, gamma with Mr 65 000, 34 000 and 12 000, respectively. On dodecylsulfate/polyacrylamide gels the smallest of these subunits was heavily stained with silver but poorly with Coomassie brilliant blue. All three subunits were resolved and clearly detectable by high-performance liquid chromatography in a dodecylsulfate-containing buffer. Biotin was localized exclusively in the alpha chain. Freezing and thawing of the isolated membranes in the presence of 1 M LiCl released the alpha chain which was subsequently purified to near homogeniety by affinity chromatography on monomeric avidin-Sepharose. No beta or gamma chain were detectable in this alpha chain preparation and no oxaloacetate decarboxylation was catalyzed. The isolated alpha chain, however, was a catalytically active carboxyltransferase as evidenced from the isotopic exchange between [1-14C]pyruvate and oxaloacetate. The rate of this exchange reaction was about 9 U/mg protein and was completely independent of the presence of Na+ ions. The ease with which the alpha chain was released from the membrane characterize this subunit as a peripheral membrane protein. The beta and gamma chain, on the other hand, stick so firmly in the membrane that they are only released by detergents, thus indicating that these are integral membrane proteins. Limited tryptic digestion of oxaloacetate decarboxylase led to a rapid cleavage of the alpha chain, yielding a polypeptide of Mr 51 000 which was devoid of biotin. Degradation of the beta chain required prolonged incubation periods and was markedly influenced by Na+ ions which had a protective effect against proteolysis. A proton is required in the decarboxylation of oxaloacetate and CO2 arises as primary product. The other alternative, i.e. generation of HCO3- with H2O as substrate, has been excluded.
 ...
PMID:Subunit composition of oxaloacetate decarboxylase and characterization of the alpha chain as carboxyltransferase. 641 43

Progressively increasing the input concentration of growth-limiting nutrient (glucose, ammonia, K+) to anaerobic chemostat cultures of Klebsiella aerogenes (D = 0.38 h-1; 35 degrees C; pH 6.8) led to a non-linear increase in bacterial cell concentration. At modest population densities, residual growth-limiting substrate levels increased substantially, with increasing input concentration, and the culture bacterial dry weight tended to a constant value. With the glucose-limited culture, increasing the glucose input concentration above 20 g X 1(-1) led to accumulation of unused glucose and a change in the fermentation pattern. There was a concomitant lowering of the yield value with respect to glucose consumption, and the calculated YATP value similarly declined. Addition of extra essential (non-limiting) nutrients to the culture was without effect. Similarly, addition of individual fermentation products (acetate, ethanol, D-lactate, 2,3-butanediol, succinate) to the feed medium, in varying concentrations and in different combinations, failed to influence the fermentation pattern or the energetics of cell synthesis. However, a clear correlation was observed between the yield values (of both glucose- and K+-limited cultures) and the steady state concentration of CO2 in the effluent gas. Increasing the concentration CO2 either by increasing the population density or lowering the sparging rate of nitrogen gas through the culture, effected a lowering of the yield values. It is suggested that dissolved CO2 exerts an effect on both metabolism and the energetics of cell synthesis. A possible mechanism of energy dissipation (i.e., a futile cycle) involving carboxylation and decarboxylation reactions is proposed.
 ...
PMID:Influence of metabolic end-products on the growth efficiency of Klebsiella aerogenes in anaerobic chemostat culture. 644 20

The growth of 95 strains of Klebsiella cultured in air with added CO2 is described. Twenty-two strains of K. ozaenae required CO2 for characteristic growth when cultured at 37 degrees C and growth was promoted by co-trimoxazole, tetracycline and sodium barbitone. Four strains of K. pneumoniae, two of K. edwardsii var. atlantae and one of K. edwardsii var. edwardsii gave increased viable counts after incubation in CO2. None of the 40 strains of K. aerogenes tested required CO2 for growth.
 ...
PMID:The carbon dioxide requirement of Klebsiellae. 676 35

The biotin-containing oxaloacetate decarboxylase from Klebsiella aerogenes catalyzed the Na+-dependent decarboxylation of oxaloacetate to pyruvate and bicarbonate (or CO2) but not the reversal of this reaction, not even in the presence of an oxaloacetate trapping system. The enzyme catalyzed an avidin-sensitive isotopic exchange between [1-14C]pyruvate and oxaloacetate, which indicated the intermediate formation of a carboxybiotin enzyme. Sodium ions were not required for this partial reaction, but promoted the second partial reaction, the decarboxylation of the carboxybiotin enzyme, thus accounting for the Na+ requirement of the overall reaction. Therefore, the 14CO2-enzyme which was formed upon incubation of the decarboxylase with [4-15C]oxaloacetate, could only be isolated if Na+ ions were excluded. Preincubation of the decarboxylase with avidin also prevented its labelling with 14CO2. The isolated 14CO2-labelled oxaloacetate decarboxylase revealed the following properties. It was slowly decarboxylated at neutral pH and rapidly upon acidification. The 14CO2 residues of the 14CO2-enzyme could be transferred to pyruvate yielding [4-14C]oxaloacetate. In the presence of Na+ this 14CO2 transfer was repressed by the simultaneous decarboxylation of the 14CO2-enzyme. However, Na+ alone was insufficient as a cofactor for the decarboxylation of the isolated 14CO2-enzyme, since this required pyruvate in addition to Na+. It is therefore concluded that the decarboxylation of oxaloacetate proceeds over a CO2-enzyme--pyruvate complex and that free CO2-enzyme is an abortive reaction intermediate. The activation energy of the enzymic decarboxylation of oxaloacetate changed with temperature and was about 113 kJ below 11 degrees C, 60 kJ between 11 degrees C and 31 degrees C and 36 kJ between 31--45 degrees C.
 ...
PMID:The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. 703 95

H2 production from glucose by Ruminococcus albus was almost completely inhibited by 10(-5) M molybdate only when sulfide was present in the growth medium. Inhibition was accompanied by a significant increase in the production of formate. Extracts of molybdate-sulfide-grown cells did not contain hydrogenase activity. Active enzyme in extracts of uninhibited cells was not inhibited by the molybdate-sulfide-containing growth medium. The results indicate that a complex formed from molybdate and sulfide prevents the formation of active hydrogenase and electrons otherwise used to form H2 are used to reduce CO2 to formate. Growth was significantly inhibited when molybdate was increased to 10(-4) M. Reversal of growth inhibition but not inhibition of H2 production occurred between 10(-4) and 10(-3) M molybdate. H2 production by R. bromei but not by R. flavefaciens, Butyrivibrio fibrisolvens, Veillonella alcalescens, Klebsiella pneumoniae and Escherichia coli was inhibited by molybdate and sulfide.
 ...
PMID:Molybdate and sulfide inhibit H2 and increase formate production from glucose by Ruminococcus albus. 736 26

The oadGAB genes encoding the gamma, alpha and beta-subunits of the oxaloacetate decarboxylase Na+ pump in Klebsiella pneumoniae have been cloned on plasmid pSK-GAB and expressed in Escherichia coli. The membranes of the recombinant E. coli clone contained about three times as much catalytically active oxaloacetate decarboxylase (3 mg protein/2 g wet cells) as those of the K. pneumoniae strain from which the genes were derived. The enzyme was solubilised from the membranes with Triton X-100 and purified. Its Na+ transport function was demonstrated after reconstitution into proteoliposomes. Proteoliposomes containing only the membrane-bound subunits beta and gamma (not the peripheral alpha-subunit) were unable to catalyse Na+ translocation in response to a transmembrane Na+ (delta pNa+) or electrical gradient (delta psi). Individual subunits of oxaloacetate decarboxylase and combinations of two subunits were expressed from appropriate derivatives of plasmid pSK-GAB. The hydrophobic subunits beta and beta gamma were membrane-bound as expected. Interestingly, the alpha-subunit was located in the cytoplasm if expressed separately or together with beta, but became membrane-bound if expressed together with gamma. A gamma alpha complex was isolated from such membranes by avidin-Sepharose affinity chromatography. Interactions of the gamma-subunit with the water-soluble alpha-subunit and with the membrane-bound beta-subunit are therefore required to form the oxaloacetate decarboxylase complex. The combinations of separately expressed subunits gamma alpha + beta and beta gamma+alpha were shown to yield the catalytically active enzyme. The alpha or the beta-subunit and the combinations of these subunits with the gamma-subunit were therefore expressed in E. coli in a catalytically competent state. Functional expression of the separate gamma-subunit, however, could not be demonstrated. The alpha-subunit was strongly overexpressed from a pT7-7 derived plasmid, but was only partially biotinylated under these conditions. On coexpression of the birA gene encoding biotin ligase the major part (80-100%) of the overexpressed alpha-subunit was biotinylated. Highly purified alpha-subunit was obtained by fractionated precipitation of the soluble cell fraction with ammonium sulfate. Incubation of the alpha-subunit with oxaloacetate led to a CO2 transfer to its prosthetic biotin group with the formation of stoichiometric amounts of pyruvate. The velocity of the CO2 transfer to the biotin on the alpha-subunit was about three orders of magnitude too low to account for the rate of the overall reaction. The carboxyltransfer reaction was significantly accelerated if the gamma-subunit was additionally present.(ABSTRACT TRUNCATED AT 400 WORDS)
 ...
PMID:Synthesis of the oxaloacetate decarboxylase Na+ pump and its individual subunits in Escherichia coli and analysis of their function. 764 79


<< Previous 1 2 3 4 5 Next >>