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)

Mutants of Apergillus nidulans with lesions in a gene, areA (formerly called amdT), have been isolated by a variety of different selection methods. The areA mutants show a range of pleiotropic growth responses to a number of compounds as sole nitrogen sources, but are normal in utilization of carbon sources. The levels of two amidase enzymes as well as urease have been investigated in the mutants and have been shown to be affected by this gene. Most of the areA mutants have much lower amidase-specific activities when grown in ammonium-containing medium, compared with mycelium incubated in medium lacking a nitrogen source. Some of the areA mutants do not show derepression of urease upon relief of ammonium repression. The dominance relationships of areA alleles have been investigated in heterozygous diploids, and these studies lend support to the proposal that areA codes for a positively acting regulatory product. One of the new areA alleles is partially dominant to areA+ and areA102. This may be a result of negative complementation or indicate that areA has an additional negative regulatory function. Investigation of various amdR; areA double mutants has led to the conclusion that amdR and areA participate in independent regulatory circuits in the control of acetamide utilization. Studies on an amdRc; areA double mutant indicate that areA is involved in derepression of acetamidase upon relief of ammonium repression.
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PMID:Studies on the role of the areA gene in the regulation of nitrogen catabolism in Aspergillus nidulans. 5 52

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

Pseudomonas aeruginosa AI 3 was able to grow in medium containing acetanilide (N-phenylacetamide) as a carbon source when NH4+ was the nitrogen source but not when urea was the nitrogen source. AIU mutants isolated from strain AI 3 grew on either medium. Urease levels in bacteria grown in the presence of urea were 10-fold lower when NH4+ or acetanilide was also in the medium, but there were no apparent differences in urease or its synthesis between strain AI 3 and mutant AIU 1N. The first metabolic step in the acetanilide utlization is catalyzed by an amidase. Amidases in several AIU strains showed altered physiochemical properties. Urea inhibited amidase in a time-dependent reaction, but the rates of the inhibitory reaction with amidases from the AIU mutants were slower than with AI 3 amidase. The purified amidase from AIU 1N showed a marked difference in its pH/activity profile from that obtained with purified AI 3 amidase. These observations indicate that the ability of strain AIU 1N and the other mutants to grow on acetanilide/urea medium is associated with a mutation in the amidase structural gene; this was confirmed for strain AIU 1N by transduction.
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PMID:Pseudomonas aeruginosa mutants resistant to urea inhibition of growth on acetanilide. 41 Jul 88

The taxonomic relationships between Clostridium bifermentans and C. sordellii were reinvestigated by numerical taxonomy, studies of DNA-DNA homology and DNA duplex thermal stability, and by analysis of cell-wall sugar components. Although the results indicate that both species may be grouped into one geno-species, C. sordellii strains could be differentiated from C. bifermentans strains on the basis of a few phenetic criteria that include the inability to ferment mannose and sorbitol, the absence of mannose in the cell wall, the production of urease, the absence of arginine deaminase activity, and susceptibility to inhibition of growth by mannose.
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PMID:Reinvestigation of the taxonomy of Clostridium bifermentans and Clostridium sordellii. 114 17

Growth studies of Helicobacter pylori were performed involving analysis of the bacterium and its microenvironment, to lend insight into the factors responsible for the morphologic conversion phenomenon. H. pylori converted from bacillary to coccoid forms in broth culture after incubation for 5 days under microaerobic conditions with agitation. This morphologic conversion was paralleled by a dramatic decrease in colony-forming units per milliliter (CFU/ml) and a significant endogenous increase in the pH of the broth culture. In addition, removal of broth cultures from microaerobic conditions after 3 days of incubation resulted in a rapid increase in culture pH, a morphologic conversion, and a concomitant decrease of CFU/ml. These observations suggest an inhibitory effect of basic pH, endogenously produced, on the growth of H. pylori in vitro. Experiments designed to identify the reason for the endogenous increase in culture pH demonstrated that the urease enzyme of H. pylori is not primarily responsible for this phenomenon. Rather, H. pylori appears to produce a deaminase enzyme that is likely responsible for the generation of ammonia, which results in the increase in culture pH, the morphologic conversion, and the loss of culturability observed in vitro. Also indicated is the need for a buffering component (for example, bicarbonate) to maintain pH conditions favorable to the growth of H. pylori.
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PMID:Characterization of the morphologic conversion of Helicobacter pylori from bacillary to coccoid forms. 186 96

Ureidoglycolate is an intermediate of allantoin catabolism in ureide-transporting legumes. This report describes the first purification of ureidoglycolate degrading activity (UGDA) from plant tissue in which the enzyme has been separated from urease. The enzyme from developing fruits of Phaseolus vulgaris has been purified 48-fold to give a preparation free of allantoinase and urease activity. UGDA was inhibited by EDTA while the Vmax was increased in the presence of Mn2+. The Km values for ureidoglycolate in the presence and the absence of Mn2+ were 2.0 and 5.4 mM, respectively. In the absence of Mn2+ UGDA was heat labile at 40 degrees C, but in the presence of Mn2+ the activity was stable up to temperatures of 60 degrees C. The Mr of UGDA was determined to be 300,000 by gel filtration chromatography and the pH optimum ranged from pH 7.0 to 8.5. Ammonia was determined to be the nitrogen-containing product of UGDA by a microdiffusion assay. This enzyme should therefore be described as ureidoglycolate amidohydrolase. The activity was shown to be associated with peroxisomes by fractionation of a crude extract on a sucrose density gradient. The products of ureidoglycolate degradation are glyoxylate, ammonia, and presumably carbon dioxide, which can be readily utilized by pathways of metabolism that are known to be present in this organelle.
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PMID:Ureidoglycolate amidohydrolase from developing French bean fruits (Phaseolus vulgaris [L.].). 191 Feb 98

The detrimental effects of excessive Ni on plant growth have been well known for many years. More recent evidence indicates that Ni is required in small amounts for normal plant growth and development. Ni is an essential component of urease in plants and microorganisms. A deficiency of Ni in plants is reported to result in necrotic lesions in leaves in response to toxic accumulations of urea. Urease plays an essential role in mobilization of nitrogenous compounds in plants, a process that is especially important during seed germination and fruit formation when protein reserves are degraded into amino acids. Arginine, an abundant amino acid in plants, when degraded produces urea as a product and urease is needed for urea utilization. Theories of urea formation during allantoin degradation in Glycine max have been recently refuted. In G. max ureides apparently are metabolized via an amidohydrolase reaction with subsequent degradation of ureidoglycine, yielding glyoxylate, NH+4 and CO2. No evidence is available for the formation of urea in this pathway. Nitrogen-fixing symbionts, such as Rhizobium and Bradyrhizobium, contain two known Ni enzymes: urease and hydrogenase. Optimum growth of nodulated legumes and actinorhizal plants may depend on an adequate supply of Ni to meet the requirements of the Ni-requiring enzymes in host plants and endophytes. The seeds of severely Ni-deficient Hordeum are completely inviable, thus providing conclusive evidence for the essentiality of Ni for this species. The evidence indicates that Ni must be added to the list of micronutrient elements generally required by plants.
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PMID:Nickel as a micronutrient element for plants. 307 27

Several commercially available enzymes were tested for their ability to hydrolyze amino acid carbamates. No activity was found with pig liver esterase, the hydantoinase from Pseudomonas fluorescens DSM 84, or the urease from jack beans. A stereoselective cleavage of the carbamyl group yielding L-amino acids was observed by acylase and acetylcholinesterases from bovine and human erythrocytes. Racemic mixtures of N-(methoxycarbonyl)-DL-alanine, N-(ethoxycarbonyl)-DL-alanine, and the corresponding valine carbamates are hydrolyzed to L-alanine and L-valine, respectively, by acylases leaving the D-amino acid carbamates unchanged. The lysine carbamates were not hydrolyzed by acylases. In contrast only the methoxycarbonyl amino acids were split by acetylcholinesterases, which, however, also cleave alpha, epsilon-(N-methoxycarbonyl)-DL-lysine stereoselectively at the alpha position, yielding epsilon-N-methoxycarbonyl-L-lysine. The optimum pH for enzymatic activity of hog kidney acylase was 7.5 and a Km value of 8.2 mM for N-(methoxycarbonyl)-DL-alanine was determined. For the acetylcholinesterases the reaction rate reaches an optimum between pH 7.5 and 8. The Km value was 68 mM for N-(methoxycarbonyl)-DL-alanine.
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PMID:Studies on the enzymatic hydrolysis of amino acid carbamates. 311 96

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

As the present classification (19) of Clostridium sordellii and C. bifermentans is based on properties which are not conclusive for most of our strains, we investigated 80 strains from various origin of this group regarding 30 selected properties. Four of these properties were correlative and therefore particularly important for a distinct differentiation of the strains investigated: urease activity (U), growth inhibition by 1% mannose (M), arginine deaminase activity (A), and sialidase (EC 3.2.1.18) activity (S). Concerning these four characters three clusters were formed: cluster I was positive for U, M, A, and S and comprised 36 strains including C. sordellii type strain (ATCC 9714T); cluster II was positive for M and S and negative for U and A and comprised twelve strains including strain ATCC 35392; and cluster III was positive for A and negative for U, M, and S and comprised 32 strains including C. bifermentans type strain (ATCC 638T). Only two of the correlative properties (U and S, U and A, A and M, or A and S) needed to be tested to determine the affiliation of any strain of the C. sordellii/bifermentans group to one of the three clusters. Clusters I and II, representing two phenotypes of C. sordellii, can now clearly be distinguished from C. bifermentans. Sialidase formed by cluster I and II strains was inhibited by antibodies produced against cluster I strain sialidase. No cross reaction was found with other clostridial sialidases. Pathogenicity, hitherto considered as one of the distinctive properties of C. sordellii and C. bifermentans, was found with various strains of all the three clusters. Therefore, in the case of an infection caused by these two species, care should be taken as to the pathogenicity especially of C. bifermentans and treatment should be accordingly.
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PMID:Correlative properties for a differentiation of two Clostridium sordellii phenotypes and their distinction from Clostridium bifermentans. 391 62


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