Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:6.3.4.6 (urease)
7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hydroxamic acids have been reported to be potent and specific inhibitors of urease (EC 3.5.1.5) activity of plant and bacterial origin. The present investigation was performed on the inhibitory effect of hydroxamic acid derivatives of naturally occurring amino acids on the urease activity of the Jack Bean and the alimentary tracts of rats. Methionine-hydroxamic acid was the most powerful inhibitor (I50=3.9 X 10(-6) M) among nineteen alpha-aminoacyl hydroxamic acids. Phenylalanine-, serine-, alanine-, glycine-, histidine-, threonine-, leucine-, and arginine-hydroxamic acids followed, in order of decreasing inhibitory power. The inhibition proceeded with time at a comparable rate to fatty acyl hydroxamic acid inhibition. The I50 values of alpha-aminoacyl hydroxamic acids were found to be almost equal to those of the corresponding fatty acyl hydroxamic acids. This fact shows that the alpha-amino group did not affect inhibitory power. However, aspartic-beta-, lysine-, and glutamic-gamma-hydroxamic acids, in descending order, were much less inhibitory, probably due to the presence of a carboxyl or omega-amino group. Furthermore, the pH optimum of the inhibition shifted to lower pH in the presence of a carboxyl group, and to a higher pH in e presence of an amino group. The results suggest that the dissociation of an acidic or a basic group reduces the inhibitory power of hydroxamic acid. Hydroxamic acid inhibits urease activity with strict specificity, excpet for aspartic-beta-hydroxamic acid, which inhibited asparaginase competitively. Hydroxamic acid derivatives of amino acids inhibited not only the urease activity of the Jack Bean, but also that of the caecum and ileum parts of the rat intestine.
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PMID:Inhibition of urease activity by hydroxamic acid derivatives of amino acids. 23 68

Algorhythm and a program for identification of bacteria of the Enterobacteriaceae family, based on Edwards and Ewing's diagnostic scheme, were worked out. Use of this program permitted to analyze different sets of abbreviated biochemical tests. To determine the genera and species of enterobacteria a minimal set of 11 tests is suggested, including indol formation, Voges-Proskauer's reaction, the presence of urease enzymes, gelatinase, lysine decraboxylase, phenylalanine deaminase, glucose fermentation (gas), or lactose, inosite, sorbit, arabinose, rhamnose. The program admits increase of both the biochemical tests, and toxonomic groups of bacteria, this permitting to consider several families. The presence of strains deviating by properties from this scheme points to the necessity of further improvement of diagnostic schemes for the enterobacteria identification.
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PMID:[Use of a computer for the purpose of identifying bacteria of the family Enterobacteriaceae and the determination of the minimal set of differential tests]. 38 11

Twenty amino acids were examined for their effects on urinary orotic acid excretion. Except for arginine and ornithine, all of the remaining amino acids tested induced a mild orotic aciduria in rats 2 hours post feeding. Two ammonium salts, and urease also acted, as inducers of orotic aciduria. The ammoneogenic properties of the amino acids tested could not solely explain the induced excretion of orotic acid. Only serine, glutamine, NH4Cl, (NH4)2CO3, and urease increased orotic acid excretion in the 24 hour fasted rat. Administration of 0.5 mmoles of arginine or ornithine ameliorated the mild orotic aciduria induced by either glycine or lysine. Arginine was shown to be more efficacious in preventing glycine induced orotic aciduria than was ornithine. Amino acid induced orotic aciduria is dependent upon the physiological state of the animal, varying with the state of digestion and the supply of arginine.
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PMID:Amino acid induced orotic aciduria. 63 45

Sixty-eight Haemophilus somnus strains isolated from the bovine in Canada and the U.S.A. were compared. In media enriched with 5% ovine serum, 5% bovine serum and 10% yeast extract, H. somnus fermented glucose, levulose, maltose, mannitol, mannose, sorbitol, trehalose and xylose, but failed to ferment arabinose, dulcitol, galactose, inositol, lactose, raffinose, rhamnose, salicin and sucrose. The organisms acidified litmus milk, produced cytochrome oxidase, indole and hydrogen sulfide (H(2)S) and reduced nitrates to nitrites. The motility, methyl-red, acetylmethyl-carbinol urease catalase, citrate, malonate, lysine, ornithine and arginine tests were negative. Haemophilus somnus was resistant to lincomycin, neomycin and triple sulfa, but susceptible to ampicillin, chloramphenicol, streptomycin, penicillin and tetracycline. No antigenic differences were noted between strains when tested against rabbit antisera of eight strains using agglutination, complement-fixation, immunodiffusion and counterimmunoelectrophoresis tests. Low titre cross-reactions were found in the agglutination tests with some of the anti-H. somnus rabbit sera with Actinobacillus lignieresi and Moraxella bovis. No distinct antigenic similarities to nine other species of pathogenic bacteria of animal origin were found. No difference was observed between H. somnus isolates from Ontario and those from western Canada and the U.S.A.
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PMID:A comparison of various Haemophilus somnus strains. 92 55

Twenty-two strains corresponding by their biochemical properties to the genus Levinea - Citrobacter were isolated. Six of the strains were referred to the species Citrobacter diversus and 12 to C. freundii, whose properties are identical with those of L. malonatica and L. amalonatica, respectively. Four strains differed from Levinea organisms by some reactions, but were fully compatible with C. freundii (in the scheme of EWING and DAVIS); two of them utilized malonate. The taxonomic position of strains displaying the following biochemical properties: dextrose positive, indole positive, H2S negative, urease on Christensen's citrate medium positive, lysine-decarboxylase negative-is discussed. In routine practice, these strains may be more accurately identified by adding of four tests: adonitol with gas production, KCN, raffinose and malonate.
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PMID:First isolations of Levinea-Citrobacter cultures in Czechoslovakia. 117 Jul

An experiment was conducted with ileally cannulated pigs to determine the apparent digestibility of amino acids and N in raw or heated conventional or low-trypsin-inhibitor soybeans. Six littermate barrows initially averaging 24 kg were fed cornstarch-based diets (10.5% CP, .68% lysine, 3,558 kcal of ME/kg) supplemented with raw (unheated), conventional soybeans; raw, low-trypsin-inhibitor soybeans; heated, conventional soybeans; heated, low-trypsin-inhibitor soybeans; or solvent-extracted soybean meal. Heating was achieved by autoclaving soybeans (after grinding) for 20 min at 110 degrees C. The urease activities of the two raw soybean sources were similar, but the trypsin inhibitor activity of the raw, low-trypsin-inhibitor soybeans was about one-half that of the raw, conventional soybeans. The lower trypsin inhibitor activity of the raw, low-trypsin-inhibitor soybeans was associated with an improvement in the apparent digestibility of amino acids and N compared with the raw, conventional soybeans (P less than .05). Heating reduced the urease and trypsin inhibitor activities and improved (P less than .05) the apparent digestibility of amino acids and N in both types of soybeans. However, the heated, conventional soybeans contained more trypsin inhibitor activity than the heated, low-trypsin-inhibitor soybeans and the digestibilities of the amino acids were lower (P less than .05). Although the urease and trypsin inhibitor activities of the two heated soybean sources were similar to or less than those of soybean meal, the digestibilities of amino acids were not as great (P less than .05) in the heated soybeans as in soybean meal.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Apparent digestibility of amino acids in raw and heated conventional and low-trypsin-inhibitor soybeans for pigs. 156 6

We have constructed an opal suppressor system in Escherichia coli to complement an existing amber suppressor system to study the structural basis of tRNA acceptor identity, particularly the role of middle anticodon nucleotide at position 35. The opal suppressor tRNA contains a UCA anticodon and the mRNA of the suppressed protein (which is easily purified and sequenced) contains a UGA nonsense triplet. Opal suppressor tRNAs of two tRNA(Arg) isoacceptor sequences each gave arginine in the suppressed protein, while the corresponding amber suppressors with U35 in their CUA anticodons each gave arginine plus a second amino acid in the suppressed protein. Since C35 but not U35 is present in the anticodon of wild-type tRNA(Arg) molecules, while the first anticodon position contains either C34 or U34, these results establish that C35 contributes to tRNA(Arg) acceptor identity. Initial characterizations of opal suppressor tRNA(Arg) mutants by suppression efficiency measurements suggest that the fourth nucleotide from the 3' end of tRNA(Arg) (A73 or G73 in different isoacceptors) also contributes to tRNA(Arg) acceptor identity. Wild-type and mutant versions of opal and amber tRNA(Lys) suppressors were examined, revealing that U35 and A73 are important determinants of tRNA(Lys) acceptor identity. Several possibilities are discussed for the general significance of having tRNA acceptor identity in the same positions in different tRNA acceptor types, as exemplified by positions 35 and 73 in tRNA(Arg) and tRNA(Lys).
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PMID:Nucleotides that determine Escherichia coli tRNA(Arg) and tRNA(Lys) acceptor identities revealed by analyses of mutant opal and amber suppressor tRNAs. 225 Dec 70

The nucleotide sequences of the complete set of tRNA species in Mycoplasma capricolum, a derivative of Gram-positive eubacteria, have been determined. This bacterium represents the first genetic system in which the sequences of all the tRNA species have been determined at the RNA level. There are 29 tRNA species: three for Leu, two each for Arg, Ile, Lys, Met, Ser, Thr and Trp, and one each for the other 12 amino acids as judged from aminoacylation and the anticodon nucleotide sequences. The number of tRNA species is the smallest among all known genetic systems except for mitochondria. The tRNA anticodon sequences have revealed several features characteristic of M. capricolum. (1) There is only one tRNA species each for Ala, Gly, Leu, Pro, Ser and Val family boxes (4-codon boxes), and these tRNAs all have an unmodified U residue at the first position of the anticodon. (2) There are two tRNAThr species having anticodons UGU and AGU; the first positions of these anticodons are unmodified. (3) There is only one tRNA with anticodon ICG in the Arg family box (CGN); this tRNA can translate codons CGU, CGC and CGA. No tRNA capable of translating codon CGG has been detected, suggesting that CGG is an unassigned codon in this bacterium. (4) A tRNATrp with anticodon UCA is present, and reads codon UGA as Trp. On the basis of these and other observations, novel codon recognition patterns in M. capricolum are proposed. A comparatively small total, 13, of modified nucleosides is contained in all M. capricolum tRNAs. The 5' end nucleoside of the T psi C-loop (position 54) of all tRNAs is uridine, not modified to ribothymidine. The anticodon composition, and hence codon recognition patterns, of M. capricolum tRNAs resemble those of mitochondrial tRNAs.
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PMID:Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum. Resemblance to mitochondria. 247 13

In this paper, we describe a reduced sequence of identification that includes T-mod medium, a selective and differential isolation medium which allows accurate presumptive identification of the most common gram-negative bacteria encountered in urine samples. The present study, performed on bacteria isolated from 1,762 independent urine samples, has shown that a few selected tests (lysine and ornithine decarboxylase, urease and trehalose fermentation tests) improve the identification accuracy of T-mod, making it possible both to identify the less frequent species and to prevent some misidentifications of Klebsiella pneumoniae and Proteus mirabilis. The proposed work flow agreed with conventional identification protocols to a 99.3% extent and allowed identification of 87.4% of the isolates directly from the primary plate, 11.4% after 1 to 3 additional tests, and 1.2% after an identification gallery.
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PMID:T-mod pathway, a reduced sequence for identification of gram-negative urinary tract pathogens. 276 51

Six conventional biochemical tests were combined to produce an identification scheme. These tests included decarboxylation of lysine and ornithine, fermentation of glucose and cellobiose, indole production and urease production. Three hundred antibiotic resistant coliforms from urine specimens were tested by this scheme and also by the API 20E for comparison. Two hundred and seventy nine (93%) of organisms were correctly identified using the six tests, 17 (5.7%) were referred for further study, and four (1.3%) were misidentified. It is concluded that this combination of tests provides an inexpensive, accurate, and rapid tool for identification.
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PMID:Rapid conventional scheme for biochemical identification of antibiotic resistant enterobacteriaceae isolates from urine. 305 81


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