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

A previously unrecognized enzyme, citrate lyase deacetylase, has been purified about 140-fold from cell extracts of Rhodopseudomonas gelatinosa. It catalyzed the conversion of enzymatically active acetyl-S-citrate lyase into the inactive HS-form and acetate. The enzyme exhibited an optimal rate of inactivation at pH 8.1. Because of the instability of acetyl-S-citrate lyase at acidic and alkaline pH values, all assays were carried out at pH 7.2, where the spontaneous hydrolysis of the acetyl-S-citrate lyase was negligible and deacetylase showed 70% of the activity at pH 8.1. The apparent Km value for citrate lyase was 10(-7) M at pH 7.2 and 30 C. The activity of the deacetylase was restricted to the citrate lyase from R. gelatinosa. The corresponding lyases from Enterobacter aerogenes (formerly Klebsiella aerogenes) and Streptococcus diacetilactis were not deacetylated; likewise, thioesters such as acetyl-S coenzyme A, acetoacetyl-S coenzyme A, and N-acetyl-S-acetyl-cysteamine were also not hydrolyzed. Citrate lyase deacetylase was present in very small amounts in cells of R. gelatinosa grown with acetate or succinate; it was induced by citrate along with the citrate lyase. L-(+)-Glutamate strongly inhibited the deacetylase. Fifty percent inhibition was obtained at a concentration of 1.4 X 10(-4) L-(+)-glutamate. D-(-)-Glutamate, alpha-ketoglutarate, L-alpha-hydroxyglutarate, L-(-)-proline, and other metabolites were less effective.
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PMID:Inactivation of citrate lyase from Rhodopseudomonas gelatinosa by a specific deacetylase and inhibition of this inactivation by L-(+1-glutamate. 0 Mar 56

1. Protein extracts obtained from Salmonella minnesota Re mutant cells by treatment with EDTA/NaC1 solution contain a protein which exhibits high affinity to bacterial lipopolysaccharides. The isolation and partial characterization of this lipopolysaccharide-binding protein is described. 2. The protein was purified from EDTA extracts by a two-step procedure consisting of ion-exchange chromatography on CM-Sephadex and preparative polyacrylamide gel electrophoresis at pH 9.5. The yield of the total purification procedure was around 16%. 3. The resulting protein preparation was homogeneous on the basis of disc gel electrophoresis, dodecylsulfate gel electrophoresis, isoelectric focusing in polyacrylamide gel and immunoelectrophoresis. 4. The isoelectric point of the protein was found to be 10.3 at 4 degrees C. Its molecular weight determined by dodecylsulfate gel electrophoresis is 15000. Its amino acid composition is characterized by the absence of histidine and proline, a low content in tyrosine and high amounts of alanine, lysine, aspartic and glutamic acid residues, or their respective amides. 5. The lipopolysaccharide-protein association was shown to be mainly due to ionic interactions of the basic protein with negatively charged groups (probably phosphate and pyrophosphate groups) of the lipid A moiety. 6. Purified lipopolysaccharide-binding protein is immunogenic in rabbits, thus enabling the preparation of specific antiserum. 7. The protein is located at the surface of Salmonella minnesota Re mutant cells as revealed by antiserum absorption with total bacteria. Ferritin-labelling studies further demonstrated that it is evenly spread over the entire cell surface. 8. Comparative antiserum absorption studies using smooth and rough strains of Salmonella minnesota, Salmonella typhimurium, Escherichia coli, Klebsiella and Shigella revealed the presence of lipopolysaccharide-binding protein (or a serologically cross-reacting antigen) in most of the strains tested. From these results the protein can be considered as a common antigen of Enterobacteriaceae.
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PMID:A lipopolysaccharide-binding cell-surface protein from Salmonella minnesota. Isolation, partial characterization and occurrence in different Enterobacteriaceae. 11 33

The paper deals with the results of analysis of 219 strains of Klebsiella using 12 tests--fermentation of adonite, asparaginic acid, sodium citrate, dulcite, d-tartrate, glutamic acid, inosite, L-proline, sodium malonate; reactions with methyl red, Foges-Proscauer, with 5-ASA. A scheme for determining fermentovars of Klebsiella is suggested which includes the tests--fermentation of adonite, dulcite, d-tartrate, glutamic acid; color reaction with 5-ASA. The groups of Klebsiella different in origin are characterized by nonhomogeneous distribution of different fermentovars. The suggested method of biochemical labelling may be one of the basic ones in complex typing of Klebsiella.
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PMID:[An evaluation of the biochemical typing of Klebsiella cultures]. 158 83

From a gene bank of Klebsiella pneumoniae M5a1, a 1.7 kb gene fragment was isolated which was able to restore the Ntr+ phenotype and ammonium (methylammonium) transport, but not glutamate synthase in an Escherichia coli glt mutant (glutamate synthase deficiency). The fragment strongly hybridized with the gltF regulatory gene from E. coli. After subcloning the fragment into an overexpression vector, a protein with a molecular weight of 27,000 dalton was identified as the gene product. The results indicate that the fragment cloned contains the gltF gene from K.pneumoniae.
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PMID:The gltF gene of Klebsiella pneumoniae: cloning and initial characterization. 194 33

Propagation and activity level of 18 enzymes catalyzing deamination reactions of dicarboxylic and oxyamino acids and enzymes of amino acid reamination and amino acid N-acyl-derivatives' deacylation have been studied in Klebsiella bacteria. Klebsiella the most actively utilizes serin, threonine, aspartic and glutamic acids and aromatic amino acids. The first three amino acids are utilized by deamination, aromatic acids- in aminotransferase reaction with alpha-ketoglutaric acid, glutamic acid--by deamination and decarboxylation. Besides, Klebsiella actively deacylates N-acyl-derivatives of amino acids.
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PMID:[Catabolism of amino acids in bacteria of the genus Klebsiella]. 208 95

Ankylosing spondylitis and Reiter's syndrome are the two major spondyloarthropathies highly associated with human leukocyte antigen (HLA) B27. Although the development of spondylitis is unclear, it has been hypothesized that HLA-B27 may predispose to spondyloarthropathies via the phenomenon of molecular mimicry. A computer search for homologies between HLA-B27 and microbes revealed a sequence of six consecutive amino acids (glutamine-threonine-aspartic acid-arginine-glutamic acid-aspartic acid) shared by HLA-B27.1 (residues 72 to 77), and Klebsiella pneumoniae nitrogenase (residues 188 to 193). Antibodies raised against a peptide derived from HLA-B27 containing this six-amino-acid sequence cross-reacted with the peptide derived from Klebsiella that contained these six amino acids, and vice-versa. These antibodies also reacted with articular tissues from HLA-B27-positive patients with ankylosing spondylitis. Sera from 53 percent of Reiter's patients and 27 percent of patients with ankylosing spondylitis showed binding to these same peptides. These results suggest that molecular mimicry may have a role in disease development.
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PMID:Molecular mimicry between human leukocyte antigen B27 and Klebsiella. Consequences for spondyloarthropathies. 246 50

Infections due to strains of Klebsiella pneumoniae, Escherichia coli, and Citrobacter freundii resistant to third-generation cephalosporins have been observed recently in France and the Federal Republic of Germany. This resistance phenotype is due to the production of new plasmid-mediated, broad-substrate-range beta-lactamases designated TEM-3 to TEM-7. DNA-DNA hybridization analysis with a probe specific for TEM-1 indicated that the corresponding genes blaT-3 to blaT-7 were variants of the structural genes for TEM-type beta-lactamases. In the present studies, a 2.5-kilobase BamHI plasmid DNA fragment encoding TEM-3 was cloned in E. coli, and the entire nucleotide sequence of blaT-3 was determined. The deduced amino acid sequence of TEM-3 differed in two positions from that of the TEM-2 enzyme: lysine (TEM-3) was substituted for glutamic acid (TEM-2) at residue 104 and serine (TEM-3) for glycine (TEM-2) at residue 238 in the numbering system of Ambler. Spontaneous mutants of TEM penicillinases with increased activity against third-generation cephalosporins were obtained in vitro by selection on cefotaxime or ceftazidime. It therefore appears that mutations in TEM-type beta-lactamases contribute to resistance to new-generation cephalosporins.
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PMID:Plasmid-mediated resistance to third-generation cephalosporins caused by point mutations in TEM-type penicillinase genes. 305 79

The structures of the capsular polysaccharides elaborated by Klebsiella types 8 (K8) and 82 (K82) have been reinvestigated. N.m.r. spectroscopy of the original and chemically modified polysaccharides was the principal method used. It is concluded that the polysaccharides are composed of repeating units having the following structures. (Formula: see text). The presence of L-glutamic acid, linked as an amide to the carboxyl group of a uronic acid, has not been observed hitherto in bacterial polysaccharides.
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PMID:Structural studies of the capsular polysaccharides from Klebsiella types 8 and 82, a reinvestigation. 337 35

A murine BALB/c IgG2a (lambda 3) myeloma immunoglobulin SAPC-15 with binding activity for negatively charged polysaccharides has been purified by affinity chromatography, and its interaction with heparin and various other polyanionic antigens has been studied. The antigen-binding activity has been demonstrated to reside in the Fab part of the immunoglobulin. The S15 myeloma protein in 0.05 M Tris buffer at pH 7.4 precipitated dextran sulfate, heparin, chondroitin sulfate A, B and C, hyaluronic acid, H. influenzae type b polysaccharide, calf thymus DNA, Klebsiella polysaccharide K63 and poly-L glutamic acid. Of these antigens only dextran sulfate was precipitated in 0.01 M phosphate buffered saline (0.15M), pH 7.4. The pepsin S15 Fab fragment did not precipitate with any of these antigens. The intrinsic tryptophanyl fluorescence of S15 was changed maximally by the addition of heparin, and the binding affinity of the immunoglobulin for this antigen was high (greater than 10(6) L/M). S15 may resemble antibody molecules that react with antigens under non-physiological conditions or in pathological conditions or in the external environment as in the lumen of the gut. All the above interactions of S15 with antigens persisted in 0.05 M Tris buffer made physiologically isotonic by the addition of sucrose, and S15 could thus be used to identify these antigens on cell surfaces.
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PMID:The interaction of mouse myeloma immunoglobulin S15 with negatively charged polysaccharide antigens. 681 62

TEM-26, an extended-spectrum beta-lactamase has been characterized in clinical isolates of Klebsiella pneumoniae and Escherichia coli derived from patients on the Paediatric Oncology Unit of St James's University Hospital, Leeds. The nucleotide sequence of this beta-lactamase gene (blaTEM26b) was determined, and compared with the nucleotide sequences of other TEM-type beta-lactamases. The blaTEM26b gene was found to differ from blaTEM12b by a single nucleotide. This difference causes the substitution of glutamic acid in blaTEM12b for lysine in blaTEM26b at position 102 in the predicted amino acid sequence. The blaTEM12b gene was first described in an isolate of Klebsiella oxytoca from a patient nursed on the same unit that yielded the strains that carry blaTEM26b. However, the blaTEM26b gene differs at no less than six nucleotides from the nucleotide sequence encoding the TEM-26 beta-lactamase that was first described in isolates from cancer patients nursed in the Children's Hospital, Stanford, California, USA. This indicates that the genes encoding TEM-26 have evolved from different progenitors.
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PMID:Convergent evolution of TEM-26, a beta-lactamase with extended-spectrum activity. 805 89


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