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PubMed2006

Structure-based stabilization of an enzyme: the case of penicillin acylase from Alcaligenes faecalis.

The modeled structure of penicillin acylase from Alcaligenes faecali (AFPGA) was constructed by comparative modeling with the Modeller program. Candidate positions that could be replaced with cysteine were estimated by scanning the modeled structure of AFPGA with the program MODIP (modeling disulfide bond in protein). The mutant Q3C/P751C had a higher optimum temperature by three degrees than that of the wild type AFPGA. The half life of the double mutant Q3C/P751C at 55 degrees C was increased by 50%. To our knowledge, this was the first structure-based genetic modification of AFPGA.

Alcaligenes faecalis↗
PubMed2005

Purification of siderophores of Alcaligenes faecalis on Amberlite XAD.

Studies on siderophore production using Alcaligenes faecalis BCCM ID 2374 revealed hydroxamate and catecholate type of siderophores at 347 microg mL-1. These fractions were purified on Amberlite XAD-4 column, which resulted in the separation of two bands having absorption maxima at 264 and 224 nm. The amount of pure siderophore obtained in powdered form from first and second fraction was 297 and 50 microg mL-1 respectively.

Adsorption↗
PubMed1990

Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis.

The gene (azu) encoding azurin from Alcaligenes denitrificans has been cloned and sequenced. The gene codes for a pre-protein with a 19-aa signal peptide. Comparison with the sequences coding for the blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis reveals the presence of ntrA and fnr boxes in front of all three genes, instead of a regular [-10, -35]-promoter. In P. aeruginosa, the azu gene is terminated by a bidirectional terminator and flanked by open reading frames on the opposite strand.

Alcaligenes↗
PubMed2003

Bioreactor cultivation of Escherichia coli for production of recombinant penicillin G amidase from Alcaligenes faecalis.

The penicillin G amidase (PGA) from Alcaligenes faecalis, which has interesting properties for use in combinatorial biochemistry, was produced by recombinant expression in Escherichia coli. The corresponding gene was cloned into a multicopy vector under the strict regulatory control of the rhamnose inducible promoter. Cells were grown in a synthetic minimal medium in a bioreactor (5 l working vol.), and production of PGA was induced by repeated addition of the inducer rhamnose, that served also as a carbon source. The fermentation yield was about 4500 units PGA activity per liter of culture medium.

Alcaligenes↗
PubMed1986

[Antigenic polysaccharides of bacteria. 19. The structure of the O-specific polysaccharide chain of Alcaligenes faecalis lipopolysaccharide].

On mild acid hydrolysis of Alcaligenes faecalis lipopolysaccharide, the O-specific polysaccharide containing D-rhamnose and D-xylose in the 3:2 ratio was obtained. Solvolysis of the polysaccharide with hydrogen fluoride in methanol resulted in methyl glycoside of a branched tetrasaccharide including three rhamnose and one xylose residues. Smith degradation of the polysaccharide led to the glycoside of disaccharide composed of two rhamnose residues and glycerol. On the basis of identification of the oligosaccharide fragments, methylation, 1H and 13C NMR analysis (including nuclear Overhauser effect data), it was established that the polysaccharide linear chain is a rhamnan, both xylose residues being attached to one of the rhamnose residues as two branches. The repeating unit of the polysaccharide has the following structure: (Formula: see text).

Alcaligenes↗
PubMed1994

Effects of organic acids on heterotrophic nitrification by Alcaligenes faecalis OKK17.

Factors affecting heterotrophic nitrification by Alcaligenes faecalis OKK17, which was isolated from sewage sludge, were examined. Specific nitrifying activity increased as the pH increased up to 8.5. Most of the nitrogenous compounds (88%) in the culture supernatant were converted to hydroxylamine or nitrite at pH 9 but 87% of them remained as ammonium at pH 7. These results imply that the substrate for heterotrophic nitrification is ammonium and that the organism oxidizes ammonium to lower its toxic effect. Although the addition of acetate to a defined medium increased growth of the bacterium up to C/N = ca. 6, the accumulation of nitrification products almost paralleled the growth and the specific nitrifying activity decreased. Pyruvate and oxaloacetate increased the specific nitrifying activity six- to eightfold compared with the other organic acids examined, but the key enzyme activities in the glyoxylate cycle were not increased. Acetate, glyoxylate, and malonate did not increase the specific nitrifying activity, but they increased the enzyme activities. These results imply that the involvement of acetate metabolism in the heterotrophic nitrification is unlikely.

Acetates↗
PubMed1984

Proton NMR spectroscopy of cytochrome c-554 from Alcaligenes faecalis.

Cytochrome c-554 from the bacterium Alcaligenes faecalis (ATCC 8750) is a respiratory electron-transport protein homologous to other members of the cytochrome c family. Its structure has been studied by 1H NMR spectroscopy in both the ferric and ferrous states. The ferric spectrum is characterized by downfield hyperfine-shifted heme methyl resonances at 46.25, 43.60, 38.40, and 36.73 ppm (25 degrees C, pH 7.1). Chemical shifts of these resonances change with temperature opposite to expectations derived from Curie's law. The pH behavior of the hyperfine-shifted resonances titrates with a pK of 6.3 that has been interpreted as due to ionization of a heme propionate. In the ferrous state, heme methyl, meso, and thioether bridge resonances have been observed and assigned. All aromatic proteins have been assigned according to the side chain of origin, and the structural environment about the sole tryptophan residue has been examined. The electron-transfer rate between ferric and ferrous forms has been estimated to be on the order of 3 X 10(8) M-1 s-1, which is the largest such self-exchange rate yet observed for a cytochrome.

Alcaligenes↗
PubMed1981

Cytotoxic activity of pathogenic Alcaligenes faecalis in turkey tracheal organ cultures.

Turkey tracheal organ cultures were used to study the virulence of Alcaligenes faecalis isolants that have been shown to be pathogenic for turkey poults. Viable infected and noninfected tracheal rings were examined by phase-contrast microscopy, and fixed stained sections were examined by light microscopy. Alcaligenes faecalis at concentrations of 10(8) and 10(9) colony-forming units/ml caused ciliostasis, hydropic degeneration (characterized by blebbing of the plasma membrane, cellular swelling, and cytoplasmic vacuolation), and eventual sloughing of the ciliated epithelium. Only ciliated epithelial cells appeared affected. For comparison, other bacterial isolants not pathogenic for turkeys were tried in this system. These bacterial isolants included 3 isolants of A faecalis from human beings and isolants of Klebsiella pneumoniae, Escherichia coli, and A faecalis from turkeys. Inoculation of each of these bacterial cultures onto tracheal organ cultures failed to produce the lesions described.

Alcaligenes↗
PubMed1963

DEGRADATION OF ERGOTHIONEINE BY CELL-FREE EXTRACTS OF ALCALIGENES FAECALIS. II. PRODUCTION OF GLUTAMIC ACID.

Booth, James S. (University of Southern California, Los Angeles) and Milo D. Appleman. Degradation of ergothioneine by cell-free extracts of Alcaligenes faecalis. II. Production of glutamic acid. J. Bacteriol. 85:654-657. 1963.-On the basis of oxidation and paper chromatographic procedures, glutamic acid was identified as the end product of ergothioneine degradation by cell-free extracts of Alcaligenes faecalis. Hydrogen sulfide and ammonia yields were determined. Several differences between the metabolism of whole cells and cell-free extracts were noted. Cleavage of the imidazole ring by cell-free extracts appeared to be hydrolytic rather than oxidative.

Alcaligenes↗
PubMed1991

Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1.

A d-aminoacylase from Alcaligenes faecalis DA1 has been purified to homogeneity by a simple purification procedure with two columns, Fractogel DEAE-650 and HW-50. The specific activity of the purified enzyme was found to be 580 U/mg of protein with N-acetyl-dl-methionine as the reaction substrate. The apparent molecular weight and isoelectric point of this enzyme were determined to be 55,000 and 5.4, respectively.

Journal Article↗
PubMed1962

COMPARISON OF SPHEROPLAST INDUCTION IN ALCALIGENES FAECALIS BY THREE DIFFERENT AGENTS.

Lark, Cynthia (Saint Louis University, St. Louis, Mo.) and Robert Schichtel. Comparison of spheroplast induction in Alcaligenes faecalis by three different agents. J. Bacteriol. 84:1241-1244. 1962.-Alcaligenes faecalis strain LB was exposed to different concentrations of cycloserine, d-methionine, or penicillin. The time course of spheroplast induction by these agents was measured as a function of their concentration. The results were consistent with models in which cycloserine reversibly inhibited an intracellular enzyme, and d-methionine was built into a defective cell-wall unit. Penicillin simulated cycloserine. This was taken as further evidence that penicillin inhibits an enzyme associated with cell-wall synthesis.

Journal Article↗
PubMed2006

Piggery wastewater treatment using Alcaligenes faecalis strain No. 4 with heterotrophic nitrification and aerobic denitrification.

Alcaligenes faecalis strain No. 4, which has heterotrophic nitrification and aerobic denitrification abilities, was used to treat actual piggery wastewater containing high-strength ammonium under aerobic conditions. In a continuous experiment using a solids-free wastewater (SFW) mixed with feces, almost all of the 2000 NH4+ -N mg/L and 12,000 COD mg/L in the wastewater was removed and the ammonium removal rate was approximately 30 mg-N/L/h, which was 5-10 times higher than the rates achieved by other bacteria with the same abilities. The denitrification ratio was more than 65% of removed NH4+ -N, indicating that strain No. 4 exhibited its heterotrophic nitrification and aerobic denitrification abilities in the piggery wastewater.

Aerobiosis↗
PubMedDate not supplied

Evidence for adherence-dependent cytotoxicity of Alcaligenes faecalis in turkey tracheal organ cultures.

A virulent isolate of Alcaligenes faecalis was examined in turkey tracheal organ cultures (TTOC) for adherence using immunofluorescent staining and for cytotoxicity using light microscopic observation. Treatment of the bacterial culture with trypsin, antiserum specific for A. faecalis, and N-acetylneuraminic acid inhibited the ability of the organism to adhere to TTOC. Treatment of the bacterium with D-galactose partly decreased adherence of the bacterium. Those treatments that inhibited the adherence of A. faecalis also inhibited the cytolytic activity in TTOC. Treatment of the bacterial culture with D-galactose only partly decreased the cytolytic activity. These data indicate that adherence of the organism to TTOC is necessary for the cytolytic activity characteristic of A. faecalis isolates capable of causing alcaligenes rhinotracheitis in turkeys.

Adhesiveness↗
PubMed2006

Characterization of a novel long-chain acyl-CoA thioesterase from Alcaligenes faecalis.

A novel long-chain acyl-CoA thioesterase from Alcaligenes faecalis has been isolated and characterized. The protein was extracted from the cells with 1 m NaCl, which required 1.5-fold, single-step purification to yield near-homogeneous preparations. In solution, the protein exists as homomeric aggregates, of mean diameter 21.6 nm, consisting of 22-kDa subunits. MS/MS data for peptides obtained by trypsin digestion of the thiosterase did not match any peptide from Escherichia coli thioesterases or any other thioesterases in the database. The thioesterase was associated exclusively with the surface of cells as revealed by ultrastructural studies using electron microscopy and immunogold labeling. It hydrolyzed saturated and unsaturated fatty acyl-CoAs of C12 to C18 chain length with Vmax and Km of 3.58-9.73 micromol x min(-1) x (mg protein)(-1) and 2.66-4.11 microm, respectively. A catalytically important histidine residue is implicated in the active site of the enzyme. The thioesterase was active and stable over a wide range of temperature and pH. Maximum activity was observed at 65 degrees C and pH 10.5, and varied between 60% and 80% at temperatures of 25-70 degrees C and pH 6.5-10. The thioesterase also hydrolyzed p-nitrophenyl esters of C2 to C12 chain length, but substrate competition experiments demonstrated that the long-chain acyl-CoAs are better substrates for thioesterase than p-nitrophenyl esters. When assayed at 37 and 20 degrees C, the affinity and catalytic efficiency of the thioesterase for palmitoleoyl-CoA and cis-vaccenoyl-CoA were reduced approximately twofold at the lower temperature, but remained largely unaltered for palmitoyl-CoA.

Acetyl-CoA C-Acyltransferase↗
PubMedDate not supplied

Development and use of amicroagglutination test to detect antibodies to Alcaligenes faecalis in turkeys.

A neotetrazolium-chloride-stained Alcaligenes faecalis antigen was developed for use in the microagglutination (MA) test. The test was used to detect serum antibodies in naturally and experimentally infected turkeys. The highest titer observed in naturally infected birds was 1:320. In one commercial flock, antibodies were detected at 12 and 15 weeks after the initial disease outbreak. Four experiments were conducted to study the serologic responses of turkeys to A. faecalis. Antibodies were first detected at 2 weeks postexposure (PE) in poults that were exposed to the organism at 1 week of age. Peak antibody titers were detected at 3 weeks PE; isolations of the organism then declined. No antibodies were detected at 7 weeks PE in these birds. Birds infected at 5 weeks of age via various routes developed maximum antibody titers 2 weeks PE. Birds inoculated subcutaneously had the highest titers, whereas those inoculated intramuscularly had the lowest titers. Antibodies were still detected at 56 days PE in some birds. Hens vaccinated with an inactivated A. faecalis bacterin developed antibody titers. Titers not higher than 1:40 were detected at hatching in progeny of these hens. However, these poults were not protected from disease after challenge. There was some evidence that birds exposed to live or inactivated A. faecalis develop some protection against challenge. Antigens were prepared using 4 Ohio A. faecalis isolates (A, B, C, and D) and 1 North Carolina isolate for use in the MA test. The results indicated that the 5 isolates were antigenically similar. Antigens prepared using isolate B reacted best in the MA test.

Agglutination Tests↗