Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.17 (ornithine decarboxylase)
 6,351 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fourteen human periodontal isolates recovered from a purported Eikenella corrodens-selective medium containing 1 microgram of clindamycin per ml displayed biochemical traits which differed from those described for E. corrodens. These organisms were gram-negative rods which corroded agar. The isolates were oxidase positive and urease, indole, and esculin negative. They differed from E. corrodens in catalase, nitrate reduction, lysine decarboxylase, and ornithine decarboxylase activities. One isolate, strain UB-294, was presumptively identified as Kingella denitrificans. A second isolate, strain UB-204, differed from E. corrodens by being catalase positive and nitrate reduction negative. Twelve isolates, including strain UB-38T (T = type strain), were phenotypically similar to Kingella kingae except that they did not produce acid from maltose and were not beta-hemolytic. Essentially complete (1,480-base) 16S rRNA sequences were determined for strains UB-38T, UB-204, and UB-294 and the type strains of Neisseria animalis, Neisseria canis, Neisseria denitrificans, Neisseria elongata, Neisseria flavescens, Neisseria macaca, and Neisseria polysaccharea. These sequences were compared with the previously published sequences of six other species belonging to the family Neisseriaceae. On the basis of the results of the comparative sequence analysis, UB-294 was confirmed as a K. denitrificans strain, UB-204 was identified as a member of a new species which may belong in the genus Eikenella, and UB-38T was identified as a member of a new species of the genus Kingella, for which we propose the name Kingella oralis [corrected]. Since strain UB-204 was the only representative of a new species, it was not named.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Phylogeny of species in the family Neisseriaceae isolated from human dental plaque and description of Kingella oralis sp. nov [corrected]. 834 9

Arginine decarboxylase (encoded by adi) is induced under conditions of acidic pH, anaerobiosis, and rich medium. The DNA sequence of a 3-kb fragment of the Escherichia coli chromosome encoding biodegradative arginine decarboxylase was determined. This sequence encodes a protein of 755 amino acids with a molecular size of 84,420 daltons. The molecular weight and predicted Adi amino acid composition agree with those found in earlier work. The amino acid sequence of arginine decarboxylase showed homology to those of three other decarboxylases of E. coli: (i) CadA, encoding lysine decarboxylase; (ii) SpeC, encoding biosynthetic ornithine decarboxylase; and (iii) SpeF, encoding biodegradative ornithine decarboxylase and the lysine decarboxylase of Hafnia alvei. Unlike SpeC and SpeF, Adi is not similar to the biosynthetic arginine decarboxylase, SpeA. adi is also dissimilar to cadA and speF in that it does not appear to be part of an operon containing a metabolically related transport protein, indicating that it represents a new type of biodegradative decarboxylase regulation. Transcriptional fusions between fragments upstream of adi and lacZ, primer extension, and site-directed mutagenesis experiments defined the pH-regulated promoter. Deletion analysis of the upstream region and cloning of fragments to make adi::lacZ protein fusion implicated a region beyond an upstream SspI site in pH regulation. Induction of adi in the presence of sublethal concentrations of novobiocin or coumermycin A1, inhibitors of DNA gyrase, was dramatically decreased, indicating that DNA supercoiling is involved in adi expression. These results and those of promoter structure studies indicated that acid regulation of adi may involve a mechanism different from that of acid regulation of cad.
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PMID:Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli. 838 9

We determined the subspecies and biogroup designations for 73 strains of Morganella morganii principally recovered from routine clinical specimens. On the basis of trehalose fermentation, 90% of all strains were identified as M. morganii subsp. morganii (trehalose negative), while the remaining 10% were designated M. morganii subsp. sibonii (trehalose positive). Using three tests (ornithine decarboxylase [ODC] and lysine decarboxylase [LDC] activities and susceptibility to tetracycline), we determined the biogroup designations for these 73 strains. Four of the seven recognized biogroups within the genus Morganella were found in the study, with biogroup A (ODC positive [ODC+], LDC negative [LDC-]) predominating (78%); all M. morganii subsp. sibonii strains were found to belong to biogroup G (ODC+, LDC-). Rapid glycerol fermentation (24 h) was linked to nonmotility and biogroup B strains (ODC+, LDC+). LDC activity but not tetracycline resistance appeared to be associated with the possession of a 40- to 45-MDa plasmid. The use of three commercial systems (API ZYM, API 50 CH, and Biolog GN) failed to detect any new biochemical tests useful for subspecies identification, with the possible exception of L-phenylalanine utilization as a sole carbon source in the Biolog GN system. No Morganella strain was found to invade either HEp-2 or Vero cell lines, but four of seven M. morganii subsp. morganii strains were cytotoxic on sheets of both cells. This cytotoxic activity appeared to correlate with the rapid expression of beta-hemolytic activity.
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PMID:Biochemical investigations of biogroups and subspecies of Morganella morganii. 874 84

We examined the taxonomic position of seven Aeromonas isolates, recovered from Flemish and Scottish drinking water production plants and reservoirs, which were previously recognized by numerical analysis of genomic AFLP fingerprints as members of an unknown Aeromonas taxon that most closely resembled the species Aeromonas bestiarum (DNA hybridization group [HG] 2). The new phenotypic and DNA-DNA hybridization data obtained in this study show that the A. bestiarum-like strains constitute a separate Aeromonas species, for which the name Aeromonas popoffii sp. nov. is being proposed. The new species exhibited an internal DNA relatedness ranging from 79 to 100% and was 22 to 63% related to the type or reference strains of other Aeromonas spp. The highest DNA binding values were determined with A. bestiarum (51 to 63%), followed by Aeromonas hydrophila sensu stricto (HG1; 50 to 60%) and Aeromonas salmonicida (HG3; 39 to 55%). Although fingerprints generated by ribotyping and cellular fatty acid analysis often were highly similar, minor differences between the respective fingerprints were of significance for the differentiation of A. popoffii from its closest taxonomic neighbors, HG1, HG2, and HG3. Phenotypically, all seven strains of A. popoffii were positive for acid and gas production from D-glucose and glycerol, growth in KCN broth, arginine dihydrolase, DNase, Voges-Proskauer reaction, and resistance to vibriostatic agent O/129 and ampicillin but displayed negative reactions for production of urease, tryptophan deaminase, ornithine decarboxylase, and lysine decarboxylase (LDC). None of the strains displayed strong hemolytic activity. The lack of D-sucrose fermentation and LDC production and the ability to utilize DL-lactate as the sole energy and carbon source were useful characteristics for the biochemical separation of A. popoffii from A. bestiarum. Other Aeromonas spp. could be differentiated phenotypically from the new species by at least two features. The chromosomal G+C content of A. popoffii ranges from 57.7 to 59.6 mol%. Strain LMG 17541 is proposed as the type strain.
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PMID:Aeromonas popoffii sp. nov., a mesophilic bacterium isolated from drinking water production plants and reservoirs. 933 24

Our data should elucidate whether or not natural antibiotic susceptibility can be used as an aid for subspecies or biovar discrimination of Morganella morganii (II). Furthermore, our goal was to create a database of the natural susceptibility of M. morganii (III) and we were interested in the relative frequency of the recently described subspecific taxa (I). On the basis of trehalose fermentation (TRE), ornithine decarboxylase (ODC), and lysine decarboxylase (LDC) activities, we determined the biovar for 90 clinical isolates of M. morganii. Within these strains we examined the natural antibiotic susceptibility of 53 morganellae to 70 antibiotics by determination of the MICs with a microdilution procedure. (I): 80 strains (89%) of all morganellae belonged to M. morganii ssp. morganii (TRE-), with biovar A (LDC-, ODC+) predominating (67 strains). The remaining strains of this subspecies were identified as biovar B (LDC+, ODC+; 12 strains) and biovar C (LDC-, ODC-, one strain). Ten strains of M. morganii ssp. sibonii (TRE+) were found: four strains belonged to biovar F (LDC variable, ODC-) and six strains to biovar G (LDC-, ODC). (II): With one exception we found no significant differences in antibiotic susceptibility between different biovars. M. morganii ssp. morganii strains are more susceptible to tetracycline than strains of M. morganii ssp. sibonii, but there is no evidence that this parameter could be useful to differentiate biovars within a subspecies. It could be shown that 8 of 30 strains of biovar A and 2 of 12 strains of biovar B were tetracycline resistant. However, one M. morganii ssp. sibonii strain was clinically susceptible to tetracycline according to French and American standards. (III): The natural population of M. morganii is primarily (naturally) resistant to certain penicillins like benzylpenicillin, oxacillin, and amoxicillin, first and second generation cephalosporins (excluding cefoxitin), cefpodoxime, all antibiotics of the ML group (macrolides and lincosamides), sulfamethoxazole, glycopeptides, fosfomycin, and fusidic acid, naturally sensitive to aminoglycosides, piperacillin, mezlocillin, ticarcillin, third and fourth generation cephalosporins, carbapenems, aztreonam, quinolones, trimethoprim, cotrimoxazole, and chloramphenicol. M. morganii is naturally resistant to a wide range of antibiotics. The natural resistance pattern is useful for validation of sensitivity tests. Susceptibility to antibiotics is an unsuitable parameter for the discrimination of the described subspecific taxa of M. morganii. M. morganii strains that do not belong to biovar A are rare.
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PMID:Identification and natural antibiotic susceptibility of Morganella morganii. 957 21

This work presents the results of a study, carried out by recently developed amperometric bioelectrodes, on the interactions between carbonic anhydrase (CA) and the decarboxylating enzymes arginine decarboxylase (ADC), L-lysine decarboxylase (LDC), and L-ornithine decarboxylase (ODC). These are all pyridoxal-phosphate dependent enzymes and catalyze the decarboxylation reaction of the respective amino acids, to give carbon dioxide and the corresponding diamine (agmatine, cadaverine, and putrescine, respectively). The rate of each decarboxylase catalyzed reaction was measured by monitoring the production of the respective diamine by a plant tissue diamino oxidase (DAO) based bioelectrode. DAO is the enzyme which catalyzes the oxidation of agmatine, cadaverine, and putrescine with the production of NH and H2O2. DAO-based bioelectrodes consist of an amperometric H2O2 electrode, coupled to the biocatalytic membrane formed by a whole plant tissue (lentil cotyledon) containing the enzyme DAO, immobilized on a dialysis membrane by polyazetidine prepolymer (PAP). The bioelectrodes were calibrated and characterized in standard solutions of agmatine, cadaverine, and putrescine. Kinetic studies to measure decarboxylase activity were performed in the presence of different concentrations of ADC, LDC, and ODC, resulting in a lowest detection limit of 10, 25, and 10 U l(-1), respectively. The effect of bovine CA II (bCAII) was evaluated in the presence of 500 U l(-1) of each decarboxylase, showing a marked increase of the rate of the decarboxylation reaction. These results suggest that (i) CA can be used to enhance the performance of decarboxylase-based biosensors, and (ii) it possibly plays further physiological roles, acting synergistically, at specific cellular and subcellular sites, with low-activity decarboxylating enzymes.
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PMID:Interactions between carbonic anhydrase and some decarboxylating enzymes as studied by a new bioelectrochemical approach. 1037 69

Lysine decarboxylase (LDC; EC 4.1.1.18) of Selenomonas ruminantium is a constitutive enzyme and is involved in the synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth. We purified the S. ruminantium LDC by an improved method including hydrophobic chromatography and studied the fine characteristics of the enzyme. Kinetic study of LDC showed that S. ruminantium LDC decarboxylated both L-lysine and L-ornithine with similar Km and the decarboxylase activities towards both substrates were competitively and irreversibly inhibited by DL-alpha-difluoromethylornithine, which is a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17). We also showed a drastic descent of LDC activity owing to the degradation of LDC at entry into the stationary phase of cell growth.
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PMID:Novel characteristics of Selenomonas ruminantium lysine decarboxylase capable of decarboxylating both L-lysine and L-ornithine. 1042 92

We describe the isolation of Photorhabdus (Xenorhabdus) luminescens from four Australian patients: two with multiple skin lesions, one with bacteremia only, and one with disseminated infection. One of the patients had multiple skin lesions following the bite of a spider, while the lesions in the other patient were possibly associated with a spider bite. The source of infection for the remaining two patients is unknown. As a member of the family Enterobacteriaceae, P. luminescens is unusual in that it fails to reduce nitrate and ferments only glucose and mannose. It gives negative reactions for lysine decarboxylase, arginine dihydrolase, and ornithine decarboxylase (Moeller). The species is motile, utilizes citrate, hydrolyzes urea, and usually produces a unique type of annular hemolysis on sheep blood agar plates incubated at 25 degrees C. A weak bioluminescence is the defining characteristic. P. luminescens is an insect pathogen and is symbiotically associated with entomopathogenic nematodes. Its isolation from human clinical specimens has been reported previously from the United States. Restriction fragment length polymorphism-PCR analysis of the 16S rRNA gene demonstrated a high level of similarity among the Australian clinical strains and significant differences between the Australian clinical strains and the U.S. clinical strains. However, numerical analyses of the data suggest that the two groups of clinical strains are more similar to each other than they are to the symbiotic strains found in nematodes. This is the first report of the isolation of P. luminescens from infected humans in Australia and the second report of the isolation of this species from infected humans worldwide.
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PMID:Isolation, identification, and molecular characterization of strains of Photorhabdus luminescens from infected humans in Australia. 1052 68

Vibrio cholerae is a facultative pathogen of humans that must survive exposure to inorganic and organic acids in the stomach and small intestine. To learn more about the mechanisms by which this pathogen colonizes the intestinal tract, we used a recombinase gene fusion reporter to identify transcripts induced during infection in an adult rabbit model of cholera. One of the genes identified was cadA, which encodes an inducible lysine decarboxylase. CadA was also induced during infections of the suckling and adult mouse intestines, and in vitro under conditions of low pH and high lysine concentration. We show that V. cholerae is capable of mounting an acid tolerance response (ATR) to both inorganic and organic acid challenges. Mutational analyses revealed a significant role for cadA, but not for speF, which encodes an ornithine decarboxylase, in both inorganic and organic ATR. Potential roles for toxR, toxT and rpoS in ATR were examined, and it was found that toxR plays a ToxT-independent role in mediating organic ATR, whereas rpoS played no detectable role in either ATR. Transcriptional analysis showed that the toxR defect in ATR is not caused by decreased cadA transcription. Despite induction of cadA in these animal models, competition assays revealed that neither cadA nor speF alone or together were required for colonization of suckling or adult mice. However, acid-adapted wild-type V. cholerae exhibited a major competitive advantage over unadapted cells during colonization of suckling mice.
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PMID:The cadA gene of Vibrio cholerae is induced during infection and plays a role in acid tolerance. 1056 22

Lysine decarboxylase (LDC, EC 4.1.1.18) from Selenomonas ruminantium has decarboxylating activities towards both L-lysine and L-ornithine with similar K(m) and Vmax. Here, we identified four amino acid residues that confer substrate specificity upon S. ruminantium LDC and that are located in its catalytic domain. We have succeeded in converting S. ruminantium LDC to an enzyme with a preference in decarboxylating activity for L-ornithine when the four-residue of LDC were replaced by the corresponding residues of mouse ornithine decarboxylase (EC 4.1.1.17).
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PMID:Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase. 1058 14


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