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Query: UMLS:C0519030 (Klebsiella)
 21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Klebsiella aerogenes utilized arginine as the sole source of carbon or nitrogen for growth. Arginine was degraded to 2-ketoglutarate and not to succinate, since a citrate synthaseless mutant grows on arginine as the only nitrogen source. When glucose was the energy source, all four nitrogen atoms of arginine were utilized. Three of them apparently did not pass through ammonia but were transferred by transamination, since a mutant unable to produce glutamate by glutamate synthase or glutamate dehydrogenase utilized three of four nitrogen atoms of arginine. Urea was not involved as intermediate, since a unreaseless mutant did not accumulate urea and grew on arginine as efficiently as the wild-type strain. Ornithine appeared to be an intermediate, because cells grown either on glucose and arginine or arginine alone could convert arginine in the presence of hydroxylamine to ornithine. This indicates that an amidinotransferase is the initiating enzyme of arginine breakdown. In addition, the cells contained a transaminase specific for ornithine. In contrast to the hydroxylamine-dependent reaction, this activity could be demonstrated in extracts. The arginine-utilizing system (aut) is apparently controlled like the enzymes responsible for the degradation of histidine (hut) through induction, catabolite repression, and activation by glutamine synthetase.
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PMID:Utilization of arginine by Klebsiella aerogenes. 34 1

Immunization with hydroxylamine Klebsiella vaccine ensures the elimination of K. pneumoniae from the blood, the lungs, the liver, the kidneys and the spleen of mice and induces considerable immunological shifts, manifested by a rise in the level of specific antibodies and by an increase in the preventive potency of the blood serum.
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PMID:[Effect of a hydroxylamine Klebsiella vaccine on the rate of elimination of the causative agent and on indices of humoral immunity]. 306 Dec 65

S. aureus aqueous extract and K. pneumoniae hydroxylamine vaccine were studied by means of chemical and immunochemical analytical techniques. The preparations were found to contain, respectively, 7.0% nad 53.5% of neutral monosaccharides, 6.5% and 0.7% of nucleic acids, as well as protein in approximately equal amounts (11.63-14.0%). In experiment of immunodiffusion, immunoelectrophoresis and rocket immunoelectrophoresis in homologous systems with hyperimmune antimicrobial sera the preparations were characterized by serological heterogeneity. After their combination with Escherichia coli aqueous extract and Proteus hydroxylamine preparation their serological characteristics remaIned unchanged. The study of cross reactions of all components of the combined preparations with hyperimmune rabbit sera to the corresponding microorganisms revealed that only Klebsiella component of the combined vaccine reacted with all hyperimmune sera. The preparation of Proteus showed the lowest activity, it reacted only with hyperimmune sera to K. pneumoniae. Besides, no reaction of S. aureus component with sera to E. coli and no reaction of the preparation of E. coli with antistaphylococcal serum were observed.
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PMID:[ChemicaL and immunochemical characteristics of antigenic preparations from Staphylococcus aureus and Klebsiella pneumoniae as the components for an associated vaccine]. 314 May 44

The capacity of dried Klebsiella cell-free vaccine, obtained from strain No. 204 by the disintegration of microbial mass with hydroxylamine, for protecting mice from pneumococcal infection caused by S. pneumoniae, serotypes 3, 4 and 9N, has been studied. Klebsiella vaccine has been found to possess immunostimulating potency with respect to the S. pneumoniae serotypes under study. On day 5 this potency is manifested to a greater extent than 24 hours after immunization. The combination of Klebsiella vaccine with Proteus vulgaris, Staphylococcus aureus and Escherichia coli K-100 antigens enhances the stimulation of nonspecific resistance.
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PMID:[Protective activity of a cell-free Klebsiella vaccine in infection in mice caused by Streptococcus pneumoniae serotypes]. 388 15

Citrate lyase from Klebsiella aerogenes inactivated by reaction in the presence of substrate or by treatment with hydroxylamine can be reactivated with acetic anhydride only if its sulfhydryl groups are reduced. Alkaline hydrolysis of pure citrate lyase yields about 3 mol of phosphopantothenate per mol of enzyme.
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PMID:Citrate lyase: a pantothenate-containing enzyme. 450 33

The capacity of dried Klebsiella cell-free vaccine, obtained from strain No. 204 by the disintegration of microbial cells with hydroxylamine, for protecting mice from Klebsiella septic infection caused by the homologous serovar and 9 heterologous serovars of K. pneumoniae was studied. The newly developed preparation was found capable of stimulating immunity not only to the homologous K. pneumoniae serovar, but also to other K. pneumoniae heterologous serovars: K1, K9, K11, K16, K20, K61. The protective capacity of the preparation with respect to these serovars was not inferior to that of the vaccines prepared by the same method from the corresponding homologous strains. The capacity of the vaccine to protect mice from Klebsiella sepsis was manifested irrespective of the virulence of the strains used for challenge.
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PMID:[Protective activity of a cell-free Klebsiella vaccine in relation to different Klebsiella pneumoniae serovars]. 638 85

Anaerobic decarboxylation of malonate to acetate was studied with Sporomusa malonica, Klebsiella oxytoca, and Rhodobacter capsulatus. Whereas S. malonica could grow with malonate as sole substrate (Y = 2.0 g.mol-1), malonate decarboxylation by K. oxytoca was coupled with anaerobic growth only in the presence of a cosubstrate, e.g. sucrose or yeast extract (Ys = 1.1-1.8 g.mol malonate-1). R. capsulatus used malonate anaerobically only in the light, and growth yields with acetate and malonate were identical. Malonate decarboxylation in cell-free extracts of all three bacteria was stimulated by catalytic amounts of malonyl-CoA, acetyl-CoA, or Coenzyme A plus ATP, indicating that actually malonyl-CoA was the substrate of decarboxylation. Less than 5% of malonyl-CoA decarboxylase activity was found associated with the cytoplasmic membrane. Avidin (except for K. oxytoca) and hydroxylamine inhibited the enzyme completely, EDTA inhibited partially. In S. malonica and K. oxytoca, malonyl-CoA decarboxylase was active only after growth with malonate; malonyl-CoA: acetate CoA transferase was found as well. These results indicate that malonate fermentation by these bacteria proceeds via malonyl-CoA mediated by a CoA transferase and that subsequent decarboxylation to acetyl-CoA is catalyzed, at least with S. malonica and R. capsulatus, by a biotin enzyme.
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PMID:Anaerobic degradation of malonate via malonyl-CoA by Sporomusa malonica, Klebsiella oxytoca, and Rhodobacter capsulatus. 771 Feb 83

The gene for monoamine oxidase (MAO) was cloned from an Escherichia coli genomic library and MAO was overproduced in the periplasmic space. The enzyme was purified to homogeneity by preparation of a periplasmic fraction, followed by ammonium sulfate fractionation and DEAE-cellulose column chromatography. Crystals were obtained by the hanging drop method using sodium citrate as a precipitant. The enzyme was found to be a dimer of identical subunits with a molecular weight of 80,000, and showed the highest activity at pH 7.5 and 45 degrees C. The enzyme was inhibited by a MAO specific inhibitor, hydroxylamine, hydrazine, phenelzine, isoniazid, and tranycpromine. The enzyme oxidized tyramine, phenethylamine, and tryptamine at higher rates, but not oxidized diamine and polyamines such as putrescine and spermine. The antibody against E. coli MAO cross-reacted with purified MAO A from Klebsiella aerogenes.
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PMID:Purification, characterization, and crystallization of monoamine oxidase from Escherichia coli K-12. 776 83

Mucoid strains of Pseudomonas aeruginosa produce a high-molecular-weight exopolysaccharide called alginate that is modified by the addition of O-acetyl groups. To better understand the acetylation process, a gene involved in alginate acetylation called algF was identified in this study. We hypothesized that a gene involved in alginate acetylation would be located within the alginate biosynthetic gene cluster at 34 min on the P. aeruginosa chromosome. To isolate algF mutants, a procedure for localized mutagenesis was developed to introduce random chemical mutations into the P. aeruginosa alginate biosynthetic operon on the chromosome. For this, a DNA fragment containing the alginate biosynthetic operon and adjacent argF gene in a gene replacement cosmid vector was utilized. The plasmid was packaged in vivo into lambda phage particles, mutagenized in vitro with hydroxylamine, transduced into Escherichia coli, and mobilized to an argF auxotroph of P. aeruginosa FRD. Arg+ recombinants coinherited the mutagenized alginate gene cluster and were screened for defects in alginate acetylation by testing for increased sensitivity to an alginate lyase produced by Klebsiella aerogenes. Alginates from recombinants which showed increased sensitivity to alginate lyase were tested for acetylation by a colorimetric assay and infrared spectroscopy. Two algF mutants that produced alginates reduced more than sixfold in acetyl groups were obtained. The acetylation defect was complemented in trans by a 3.8-kb XbaI-BamHI fragment from the alginate gene cluster when placed in the correct orientation under a trc promoter. By a merodiploid analysis, the algF gene was further mapped to a region directly upstream of algA by examining the polar effect of Tn501 insertions. By gene replacement, DNA with a Tn501 insertion directly upstream of algA was recombined with the chromosome of mucoid strain FRD1. The resulting strain, FRD1003, was nonmucoid because of the polar effect of the transposon on the downstream algA gene. By providing algA in trans under the tac promoter, FRD1003 produced nonacetylated alginate, indicating that the transposon was within or just upstream of algF. These results demonstrated that algF, a gene involved in alginate acetylation, is located directly upstream of algA.
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PMID:Identification of algF in the alginate biosynthetic gene cluster of Pseudomonas aeruginosa which is required for alginate acetylation. 839 13

Reaction of Klebsiella aerogenes urease with diethylpyrocarbonate (DEP) led to a pseudo-first-order loss of enzyme activity by a reaction that exhibited saturation kinetics. The rate of urease inactivation by DEP decreased in the presence of active site ligands (urea, phosphate, and boric acid), consistent with the essential reactive residue being located proximal to the catalytic center. The pH dependence for the rate of inactivation indicated that the reactive residue possessed a pKa of 6.5, identical to that of a group that must be deprotonated for catalysis. Full activity was restored when the inactivated enzyme was treated with hydroxylamine, compatible with histidinyl or tyrosinyl reactivity. Spectrophotometric studies were consistent with DEP derivatization of 12 mol of histidine/mol of native enzyme. In the presence of active site ligands, however, approximately 4 mol of histidine/mol of protein were protected from reaction. Each protein molecule is known to possess two catalytic units; hence, we propose that urease possesses at least one essential histidine per catalytic unit.
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PMID:Diethylpyrocarbonate reactivity of Klebsiella aerogenes urease: effect of pH and active site ligands on the rate of inactivation. 842 33


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