SEARCH · Search PubMed

Results for “AEROBACTER”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 37 records · Page 2Linked to original sources

PubMed1966

Cystathionine as a precursor of methionine in Escherichia coli and Aerobacter aerogenes.

Balish, Edward (Argonne National Laboratory, Argonne, Ill.), and Stanley K. Shapiro. Cystathionine as a precursor of methionine in Escherichai coli and Aerobacter aerogenes. J. Bacteriol. 92:1331-1336. 1966.-Cystathionine has been shown to be a precursor of methionine biosynthesis in Escherichia coli and Aerobacter aerogenes. A double enzyme assay was developed to show the formation of homocysteine from cystathionine. The results obtained support the concept that cystathionine serves as a precursor of methionine via the intermediate formation of homocysteine. The latter compound is methylated by the homocysteine methyltransferase of these microorganisms. Sulfhydryl and keto acid assays were used to demonstrate cystathionase activity. Methionine represses both homocysteine methyltransferase formation and cystathionase formation. However, the presence of methionine in reaction mixtures resulted in product inhibition of homocysteine methyltransferase activity, but not of cystathionase activity.

Amino Acids↗

PubMed1966

Diaphorases from Aerobacter aerogenes.

Bernofsky, Carl (The University of Kansas, Kansas City), and Russell C. Mills. Diaphorases from Aerobacter aerogenes. J. Bacteriol. 92:1404-1414. 1966.-Five enzymes which catalyze the reduction of 2,6-dichlorophenol-indophenol by reduced nicotinamide adenine dinucleotide (NADH(2)) have been separated from sonic extracts of Aerobacter aerogenes B199 by diethylaminoethyl (DEAE) cellulose chromatography. Three major chromatographic fractions (enzymes I, II, and III) account for most of the activity in the extract. Of the two minor fractions, one is associated with cytochrome b(1). The other is extremely labile, and was not studied further. The chromatographed diaphorases appear to have a specific requirement for flavin mononucleotide. They are also readily inactivated by dilution; however, this can be prevented by a combination of phosphate buffer, bovine serum albumin, and flavin mononucleotide. The different enzymes are clearly distinguishable by their activities with NADH(2) and reduced nicotinamide adenine dinucleotide phosphate (NADPH(2)) in the presence of various electron acceptors (2,6-dichlorophenol-indophenol, ferricyanide, menadione, and cytochrome c), and by their responses to inhibitors (amobarbital, antimycin A, Atabrine, p-chloromercuribenzenesulfonate, dicumarol, and 2,4-dinitrophenol). With 2,6-dichlorophenol-indophenol as acceptor, enzymes I, II, and III have comparable activities with either NADH(2) or NADPH(2). With menadione and ferricyanide as acceptors, enzymes II and III exhibit very high, NADH(2)-specific activities. When cytochrome c is the acceptor, however, enzyme III shows greater activity with NADPH(2) as the electron donor. Ferricyanide is the most active acceptor for the cytochrome b(1)-containing fraction. Coenzyme Q(6) does not appear to serve as an acceptor. All the diaphorases, with the exception of that in the cytochrome b(1)-containing fraction, are inhibited by p-chloromercuribenzenesulfonate. Amobarbital is relatively ineffective and inhibits only the indophenol reductase activity of enzyme I. The menadione reductase activity of enzymes I, and II, and the diaphorases in the cytochrome b(1)-containing fraction are strongly inhibited by antimycin A, 2,4-dinitrophenol, dicumarol, and Atabrine. However, the menadione reductase activity of enzyme III is affected only by the last three of these inhibitors. The diaphorases in sonic-treated extracts do not appear to be associated with a particulate fraction.

Antimetabolites↗

PubMed1966

Metabolism of D-mannose in Aerobacter aerogenes: evidence for a cyclic pathway.

Kamel, M. Y. (Michigan State University, East Lansing), and R. L. Anderson. Metabolism of d-mannose in Aerobacter aerogenes: evidence for a cyclic pathway. J. Bacteriol. 92:1689-1697. 1966.-Evidence is presented which suggests a cyclic pathway for the constitutive utilization of d-mannose in extracts of Aerobacter aerogenes PRL-R3. d-Mannose is phosphorylated with d-glucose-6-phosphate to yield d-mannose-6-phosphate and d-glucose. d-Glucose-6-phosphate may be regenerated by isomerization of d-mannose-6-phosphate through d-fructose-6-phosphate, or by phosphorylation of d-glucose with adenosine-5'-triphosphate. The pathway involves the participation of four constitutive enzymes: d-glucose-6-phosphate isomerase, d-mannose-6-phosphate isomerase, a stereospecific d-glucokinase, and a phosphotransferase which phosphorylates d-mannose with d-glucose-6-phosphate, acetyl phosphate, or carbamyl phosphate. The absence of d-mannokinase (adenosine-5'-triphosphate:d-mannose phosphotransferase) activity in extracts of this organism suggests that the pathway may be of functional significance. Also, the pathway accounts for an apparent 2-epimerization of d-mannose to d-glucose that was observed in extracts.

Adenosine Triphosphate↗

PubMed1976

Complement consumption in fresh blood sera by double culture of Paramecium caudatum and Aerobacter cloacae compared with survival and stage of disease in some malignant tumors in man.

Using the complement consumption test by double culture of Paramecium caudatum and Aerobacter cloacae (DPA) as antigen we examined blood sera and compared survival rates and stage of disease in 124 patients with carcinoma of cervix uteri, corpus uteri, ovaries and breast. The evidence suggests that bacteria Aerobacter cloacae constitute the proper antigenically effective substances of DPA. The intensity of reaction and therapy the relative titres of antibodies detected by the test were expressed by the amount of complement consumed in the reaction and designated by the abbreviation "NMHD", i. e. number of minimum haemolytic doses of complement fixed by antigen in the reaction. Patients with NMHD above 8 (i. e. with an intensive reaction corresponding to a high level of antibodies) exhibited partly higher three-year survival rates -- starting from the time of diagnosis, partly more often the clinical stages of disease I or II as compared with patients with NMHD below 4. The best survival rates were found in patients with NMHD above 8 and clinical stage I or II. NMHD values in patients with the initial period of disease and in healthy women did not differ substantially.

Animals↗

PubMed1963

ACTION OF FORMALDEHYDE ON MICROORGANISMS. III. BACTERICIDAL ACTION OF SUBLETHAL CONCENTRATIONS OF FORMALDEHYDE ON AEROBACTER AEROGENES.

Neely, W. Brock (The Dow Chemical Co., Midland, Mich.). Action of formaldehyde on microorganisms. III. Bactericidal action of sublethal concentrations of formaldehyde on Aerobacter aerogenes. J. Bacteriol. 86:445-448. 1963.-Bacteriostatic concentrations of formaldehyde were found to be bactericidal during the initial growth period. This bactericidal activity was due to the primary induction of unbalanced growth by formaldehyde. The subsequent formation of 1,3-thiazane-4-carboxylic acid prevented the synthesis of methionine. This dual activity of formaldehyde resulted in an inhibition of both nuclear and cytoplasmic syntheses, and created the normal bacteriostatic condition that has been observed before with sublethal concentrations of formaldehyde.

Anti-Bacterial Agents↗

PubMed1984

Stimulation by glutamine of the formation of N6-hydroxylysine in a cell-free extract from Aerobacter aerogenes 62-1.

Glutamine may serve as an activator and/or regulator of the N6-hydroxylase (E.C. 1.14.99) of Aerobacter aerogenes 62-1. Activation and stabilization of N6-hydroxylase activity was observed both in vivo and in vitro. Growth in a glutamine-supplemented medium resulted in (1) maximum N6-hydroxylase activity at an earlier stage of growth and (2) higher N6-hydroxylase activity and continued aerobactin synthesis into stationary phase. Storage of P2 in the presence of L-glutamine (1 mM) significantly increased the lifetime of the labile N6-hydroxylase activity. Inclusion of L-glutamine in the incubation mixture typically resulted in a 2-3-fold activation of the hydroxylase activity. The stimulatory effect of glutamine was independent of and additive to the enhancement of N6-hydroxylation by the active component(s) in the supernatant, S2 fraction. Glutamic acid-gamma-semihydrazide activated slightly in the absence of glutamine but activation of the system by glutamine was decreased by this compound. Azaserine was shown to be an uncompetitive inhibitor with respect to lysine and this inhibition was not reversed by glutamine.

Azaserine↗

PubMed1975

Determination of the efficiency of oxidative phosphorylation in continuous cultures of Aerobacter aerogenes.

For anaerobic glucose-limited chemostat cultures of Aerobacter aerogenes a values of 14.0 g/mole was found for Ymax/ATP and a value of 6.8 mmoles ATP/g dry weight/hr for the maintenance coefficient. Both values are much lower than those previously determined for tryptophan-limited anaerobic chemostat cultures. It is concluded that generally the largest part of the maintenance energy is not used for true maintenance processes. For aerobic glucose-limited chemostat cultures two phases could be differentiated. Acetate production started at mu values higher than 0.53. The slopes of the curves relating the specific rates of glucose- and oxygen consumption with mu became higher and lower respectively above the mu value of 0.53. Using the YATP values obtained in the anaerobic experiment a P/O ratio of about 1.3 could be calculated for glucose- and tryptophan-limited chemostat cultures. In sulfate-limited chemostat cultures acetate was produced at all growth rates. At high growth rates also pyruvate and alpha-ketoglutarate were produced. With the YATP values obtained in the anaerobic experiment a P/O ratio of about 0.4 was calculated for sulfate-limited chemostat cultures.

Acetates↗

PubMed1976

Energetic aspects of anaerobic growth of Aerobacter aerogenes in complex medium.

Molar growth yields for anaerobic growth of Aerobacter aerogenes in complex medium were much higher than for growth in minimal medium. In batch cultures the molar growth yield for glucose varied from 44 to 50 and YATP from 17.1 to 18.8. For glucose-limited chemostat cultures a value of 17.5 g/mole was found for Y max ATP and a value of 2.3 mmoles ATP/g dry weight h for the maintenance coeficient. Growth-dependent pH changes were used to control the addition of fresh medium, containing excess of glucose to a continuous culture. The specific growth rate and the population density were dependent on the pH difference between the inflowing medium and the culture. At a mu value of 1.44 h-1 the molar growth yield for glucose was about 70 and Y ATP about 28.5. An equation is presented, which gives the relation between theoretical and experimental Y max ATP values.

Adenosine Triphosphate↗

PubMed1975

Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes.

Maltohexaose producing amylase (EC 3.2.1.-) is the fourth known exo-amylase, the three previously known being glucoamylase, beta-amylase and Pseudomonas stutzeri maltotetraose producing amylase. The enzyme after release from Aerobacter aerogenes cells by 0.1% sodium lauryl sulfate extraction was purified by ammonium sulfate precipitation, DEAE-Sephadex column chromatography and Sephadex G-100 gel filtration to 80-fold of the original sodium lauryl sulfate extract activity, It gave a single band on disc electrophoresis, and the molecular weight by gel filtration was 54 000. This amylase showed maximal activity at 50 degrees C and pH 6.80. The pH stability range was relatively wide, the enzyme retaining more than 90% of its initial activity in the range of 6.50-9.0. 80% of the activity was retained after 15 min at 50 degrees C. This enzyme produced maltohexaose from starch, amylose and amylopectin by exo-attack, but did not act on alpha- or beta-cyclodextrin, pullulan or maltohexaitol. Also the enzyme acted on beta-limit dextrins of amylopectin and glycogen to form branched oligosaccharides. The unusual reaction of this enzyme on beta-limit dextrin is discussed from the standpoint of the stereochemistry of 1,4-alpha- and 1,6-alpha-glucosidic bonds. This is the anomalous amylase for which it is recognized that 1,6-alpha-glucosidic linkages in the substrates can mimic the effect of 1,4-alpha-bonds, as previously observed in pseudo-priming reactions of E. coli phosphorylase.

Amylases↗

PubMed1976

The existence of three types of acetohydroxy acid synthetase in an isoleucine-requiring mutant of Aerobacter aerogenes.

The synthesis of the three types of acetolactate synthase (EC 4.1.3.18) which are responsible for the biosynthesis os isoleucine and valine, was observed in Aerobacter aerogenes I-12, an isoleucine-requiring mutant, when grown on the four kinds of media. When the cells were grown on isoleucine-rich medium, acetolactate synthase sensitive to feedback inhibition and having an optimum pH at 8.0 was formed. By increasing the amount of potassium phosphate in the medium, the catabolite repression of the enzyme having an optimum pH at 6.0 and which is insensitive to feedback inhibition, was released. In contrast, acetolactate synthase having an optimum pH at 8.0 and insensitive to feedback inhibition was formd when isoleucine was limited, irrespective of phosphate concentrations. Two insensitive enzymes were not regulated by isoleucine, leucine and valine, although sensitive pH 8.0 enzyme was repressed by them. Thus, it may be assumed that the synthesis of insensitive pH 8.0 enzyme were repressed by limiting the amount of isoleucine is still open.

Acetolactate Synthase↗

PubMed1977

Study on the mechanism of action of adenosylcobalamin-dependent glycerol dehydratase from Aerobacter aerogenes. I. Role of structural components of adenosylcobalamin the formation of the active site of glycerol dehydratase.

A new method of partial chemical synthesis of adenosylcobalamin (Co alpha-[alpha-5,6-diemethylbenzimidazolyl)]-Co beta-adenosylcobamide, AdoCbl) analogs has been developed. A series of derivatives of AdoCbl modified in the nucleoside and nucleotide ligands and corrin macrocycle have been obtained. The interaction of AdoCl analogs with glycerol dehydratase (EC 4.2.1.30) from Aerobacter aerogenes has been investigated. It has been shown that the nucleoside ligand of AdoCbl provides no essential contribution to the binding of apoenzyme but the preservation of the exact structure of the 1-N and 2-C positions of adenine appears essential for the catalysis. The coordination bond between the Co and nucleotide ligand of AdoCl does not play a decisive role in glycerol dehydratase activity. To form the active site of the glycerol dehydrates, the nucleotide in the AdoCbl structure is essential since nucleotide elimination results in a 100-fold increase of Ki for the corresponding analog. In the binding of AdoCbl with apoenzyme, the main role belongs to the corrin macrocycle, in which the e-propionamide group is significant for binding with apoenzyme, but presumably not essential for catalysis.

Adenine Nucleotides↗

PubMed1979

Studies on the formation of N6-hydroxylysine in cell-free extracts of Aerobacter aerogenes 62-1.

We have investigated conditions optimal for the conversion of L-lysine to its N6-hydroxy derivative by partially purified cell-free extracts of Aerobacter aerogenes 62-1. The enzyme system was highly specific to L-lysine: the D-isomer and, the N2- or N6-derivatives of lysine, and alpha-amino acids were not hydroxylated. Most of the latter compounds had little effect onthe hydroxylation of L-lysine. However, -l-glutamic acid and L-glutamine enhanced the hydroxylation, with half-maximal activation achieved at 100 micrometers concentration of the effector. The Km values for pyruvate and L-(+)-lactate (compounds known to stimulate N-hydroxylysine formation) were found to be approx. 100 micrometers. The data show that N-hydroxylation of the amino acid precedes acylation in the biosynthesis of hydroxamic acid in A. aerogenes 62-1.

Antimetabolites↗

PubMed1985

Mineral nutrition of Aerobacter aerogenes for valine production in a synthetic medium.

The effect of a number of mineral salts, like dipotassium hydrogen phosphate, magnesium sulphate, and sodium chloride, and of some trace elements including iron, copper, cobalt, nickel, molybdenum, and calcium, on the production of valine by Aerobacter aerogenes in a synthetic medium was investigated. It was found that all the mineral salts were necessary for valine formation. Among the trace elements, iron and molybdenum were found to be necessary in minute concentrations for the optimum yield of the amino acid, while all the others had an adverse effect on valine production, even at lower levels.

Culture Media↗

PubMed1989

Studies on lysine:N6-hydroxylation by cell-free systems of Aerobacter aerogenes 62-1.

Electron microscopic examination has revealed the vesicular nature of the membrane component, of the cell-free system of Aerobacter aerogenes 62-1, which catalyses lysine: N6-hydroxylation. Regardless of the orientation of the vesicles, N-hydroxylation process is still stimulated by pyruvate. Both pyruvate oxidation and lysine: N6-hydroxylation were inhibited by protonophores and Gramicidin S.

Bacteriolysis↗

PubMed1978

Carbon and nitrogen nutrition of Aerobacter aerogenes for valine production.

A number of carbon and nitrogen compounds were tested for their effect on growth of Aerobacter aerogenes and valine production. Sucrose was found to be the superior carbon source for valine production, while mannose supported maximum cellular growth with very poor yield of valine. Urea was found to be the adequate nitrogen source for valine production. Supplementation of the synthetic medium with complex nutrients lowered the yield of valine. No direct relationship between the growth of the organism and the formation of the amino acid was noticed. On the basis of this study, a suitable synthetic medium for valine production has been developed.

Carbon↗

PubMed1982

Inhibition of chorismate mutase activity of chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes.

Inhibition data (I50 values) have been obtained for inhibitors of the chorismate mutase activity of chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes. Several 1-substituted adamantane derivatives were investigated; the order of decreasing inhibitory activity with the various substituents was -PO32- much greater than -P(OCH3)O2- greater than -CO2- greater than -CH2CO2- greater than -SO2- greater than SO3-. 3-Chloroadamantane-1-acetic acid was slightly less effective than adamantane-1-acetic acid. 2-(1-Carboxy-1,4-dihydrobenzyl)acrylic acid (19), an analogue of prephenate, was an effective inhibitor. Other substances investigated, including 2,4,10-trioxaadamantane-1-acetic acid (15), 5-enolpyruvylshikimic acid (20), and 1-(carboxyethyl)-1,4-dihydrobenzoic acid (18), failed to inhibit chorismate mutase activity under the conditions investigated.

Chemical Phenomena↗

PubMed1978

Kinetic studies on the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes.

Steady-state kinetic techniques have been used to investigate each of the reactions catalyzed by the bifunctional enzyme, chorismate mutase-prephenate dehydrogenase, from Aerobacter aerogenes. The results of steady-state velocity studies in the absence of products, as well as product and dead-end inhibition studies, suggest that the prephenate dehydrogenase reaction conforms to a rapid equilibrium random mechanism which involes the formation of two dead-end complexes, viz, enzyme-NADH-prephenate and enzyme-NAD+-hydroxyphenylpyruvate. Chorismate functions as an activator of the dehydrogenase while both prephenate and hydroxyphenylpyruvate acted as competitive inhibitors in the mutase reaction. By contrast. bpth NAD+ and NADH function as activators of the mutase. Values of the kinetic parameters associated with the mutase and dehydrogenase reactions have been determined and the results discussed in terms of possible relationships between the catalytic sites for the two reactions. The data appear to be consistent with the enzyme having either a single site at which both reactions occur or two separate sites which possess similar kinetic properties.

Allosteric Regulation↗

PubMed1977

Purification and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes.

The enzyme acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes was purified to electrophoretic homogeneity. The molecular weight of the enzyme as determined on Sephadex gels is 150 000. The enzyme possesses potent phosphotransferase and phosphohydrolase activities. Initial rate kinetics were used to investigate the mechanism of acyl-phosphate-hexose phosphotransferase. These studies, which involved a number of different phosphoryl donors and substrate analogues, suggest that the kinetic mechanism is of the rapid equilibrium random Bi Bi type. A number of other enzymes that exhibit both transferase and hydrolase activities involve obligatory covalent enzyme-substrate intermediates in their mechanisms of action.

Enterobacter↗