Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The possibility to keep some biochemical reactions of the parent strains (urease-positive, glucose fermentation, phenylalanine-deaminase-positive, H2S but not indol production) was demonstrated in 5 L-forms, obtained from as many strains of Pr. mirabilis and in 1 L-form, isolated from a vaginal secretion and identified as belonging to the same species. The indirect hemagglutination technique, made by the sonicated antigen in 3 of the 6 L-forms with Proteus OXK antiserum, resulted positive in titers varying from 1:128 to 1:1024. Crossed tests made with antisera for different bacterial species (e. coli, Shigella, klebsiella, ecc.) and of Mycoplasma (M. hominis, M. orale, M. salivarium, M. fermentans, M. arthritidis) put in evidence aspecific reactions only in 1.3% of the bacterial antisera. On the contrary, all 5 antisera for Mycoplasma were able to agglutinate the sensitized erythrocytes at titers quite analogous to that of the homologous antiserum. The sensitivities to various antibiotics of the 6 L-forms and the parent strains has been determined. All of L-forms were more resistent to the tetracycline than L-forms of other bacterial species. On the basis of te results got by biochemical and serological tests, we confirm the necessity to make use of both the groups of tests, in order to identify the L-forms of recent isolation.
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PMID:[Researches on some biochemical and serological properties and on the sensitivity to antibiotics of L-forms of "Proteus" (author's transl)]. 40 87

A medium designed for the detection of motility, indole, lysine decarboxylase and deaminase reactions, and H2S production was devised and evaluated. Results, using 157 strains of enteric pathogens, were in agreement with reference methods. When 300 isolates from fecal cultures were screened using this medium, Shigella was easily differentiated from Escherichia and more of the Proteus species, especially P. morganii, could be eliminated from further study.
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PMID:Motility-indole-lysine-sulfide medium. 117 33

A new selective differential agar medium for rapid presumptive identification of Enterobacteriaceae from water and food samples is described (EMX ID agar). By a combination of fluorogenic and chromogenic substrates, the medium detects the presence of beta-D-glucuronidase, beta-D-galactosidase, beta-D-xylosidase, tryptophane deaminase and H2S; additionally, cytochrome-oxidase and indole production can be demonstrated. This medium provides an inexpensive means for simple and rapid presumptive identification of E. coli and coliforms and for the differentiation within the Klebsiella-Enterobacter and the Proteus-Providencia-Morganella group. Furthermore, it allows to distinguish between the H2S-positive Enterobacteriaceae Citrobacter freundii, Salmonella spp., S. arizonae, Edwardsiella, Proteus mirabilis, P. vulgaris and some oxidase-positive bacteria.
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PMID:A new plate medium for rapid presumptive identification and differentiation of Enterobacteriaceae. 177 82

Tryptophan deaminase was isolated from Proteus vulgaris and purified. The procedure for enzyme purification included the cell destruction on USD-1, fractionation by ammonium sulphate, gel chromatography on ultragel AcA34, ion exchange chromatography on DEAE-cellulose. A degree of the enzyme purification--95, yield--5.7%. The pH optimum was 7.5, the temperature optimum--47 degrees C. The enzyme molecular weight (105 kD) was estimated by gel chromatography on Sephadex G-200, Km--5.0 mM in the K-phosphate buffer (pH 7.5). The SH groups are supposed to be present in the active site of the enzyme. The enzyme does not accelerate oxidation deamination of phenylalanine and tyrosine.
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PMID:[Isolation and various characteristics of tryptophan deaminase from Proteus vulgaris]. 268 39

The faecal carriage rates of different species of Proteeae were assessed in studies with 220 faecal isolates from 219 individuals of whom approximately one-third were well and the remainder had gastro-enteritis. As a result of the development of new media that allowed replacement of the phenylalanine deaminase test with the tryptophan deaminase test and made it possible to combine tests for indole and urease production and for hydrogen sulphide and ornithine decarboxylase formation in two single-tube tests, all strains were speciated with speed, economy and accuracy. Most (96%) isolates were either Proteus mirabilis (62%) or Morganella morgani (34%). The significance of these findings in relation to urinary tract infection is discussed. P. vulgaris was found in only one (0.45%) faecal specimen and this rarity of carriage in faeces is believed to be the main reason for its rare association with urinary tract infections. The frequent association of M. morgani, in the absence of other enteropathogenic bacteria, with severe gastroenteritis was noted with interest.
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PMID:Rare occurrence of Proteus vulgaris in faeces: a reason for its rare association with urinary tract infections. 351 39

The penicillin G acylase genes from the Proteus rettgeri wild type and from a hyperproducing mutant which is resistant to succinate repression were cloned in Escherichia coli K-12. Expression of both wild-type and mutant P. rettgeri acylase genes in E. coli K-12 was independent of orientation in the cloning vehicle and apparently resulted from recognition in E. coli of the P. rettgeri promoter sequences. The P. rettgeri acylase was secreted into the E. coli periplasmic space and was composed of subunits electrophoretically identical to those made in P. rettgeri. Expression of these genes in E. coli K-12 was not repressed by succinate as it is in P. rettgeri. Instead, expression of the enzymes was regulated by glucose catabolite repression.
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PMID:Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli. 353 Nov 81

Proteus rettgeri and Escherichia coli W were shown to express structurally different penicillin G acylases. The enzymes had similar substrate specificity but differed in molecular weight, isoelectric point, and electrophoretic mobility in polyacrylamide gels and did not antigenically cross-react. When the organisms were subjected to environmental conditions which made expression of this enzyme essential for growth, spontaneous mutants were isolated that used different amides as the only source of nitrogen. These mutants acquired the ability to use amides for growth by deregulating the penicillin G acylase and by their evolution to novel substrate specificities. The enzymes expressed by mutants isolated from each genus appeared to have evolved in parallel since each acylase attained similar new substrate specificities when the organisms were subjected to identical selection pressure.
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PMID:Experimental evolution of penicillin G acylases from Escherichia coli and Proteus rettgeri. 389

Penicillin G acylase from Proteus rettgeri is an 80,000- to 90,000-dalton enzyme composed of two nonidentical subunits. Both subunits were required for enzymatic activity. The 65,000-dalton beta subunit contained a phenylmethylsulfonyl fluoride-sensitive residue required for enzymatic activity, and the 24,500-dalton alpha subunit contained the domain that imparts specificity for the penicillin side chain.
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PMID:Role of protein subunits in Proteus rettgeri penicillin G acylase. 403 Jun 97

Gram-nagative organisms were tested with commercially available reagentimpregnated strips (PATHO-TEC). Of the 291 strains, all were tested by using seven paper tests and their conventional counterparts. Excellent correlation was obtained with the oxidase, phenylalanine-deaminase, and Voges-Proskauer tests. Indole tests made on liquid medium cultures also gave complete correlation, but some false-negative results with indole-positive Proteus strains were obtained when growth from solid medium was tested by the strip method. Paper strip urease tests were positive within 2 hr with all Klebsiella and some Serratia, Herellea, and Citrobacter strains as well as with Proteus strains. Approximately 15% of citrate strip test results differed from those of the conventional tests, and reproducibility was poor on retest. The lysine decarboxylase strip test showed a number of discrepancies and posed problems of interpretation and readability. Paper reagent strip methods are simple and convenient and merit further development to increase the specificity of those which depend on pH change up to that achieved with the Voges-Proskauer, oxidase, phenylalanine, and indole methods.
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PMID:Comparative study of the efficacy of seven paper-reagent strips and conventional biochemical tests in identifying gram-negative organisms. 490 7

1. Penicillin amidase from Proteus rettgeri was purified 580-fold by a four-step chromatographic procedure. Titration with phenylmethanesulphonyl fluoride showed that the purified preparation contains 53% of the enzyme. 2. The molecular weight of the amidase was found to be 65.000. The enzyme is strongly inhibited by N-bromosuccinimide and zinc ions. It hydrolyses penicillins, cephalosporins and some synthetic substrates, and in addition it catalyses synthesis of ampicillin from methyl ester of phenylglycine and 6-aminopenicillanic acid. 3. The immobilized amidase obtained by copolymerization of the chemically modified enzyme with acrylamide was applied for preparative hydrolysis of benzylpenicillin.
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PMID:Penicillin amidase from Proteus rettgeri. 680 83


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