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PubMed1967

Growth Response of Lactobacillus brevis to Aeration and Organic Catalysts.

Under stationary and anaerobic conditions, greater cell yields of Lactobacillus brevis were obtained from autoclaved than from filter-sterilized glucose media. Fructose, tentatively identified as a product generated by the heating process, served as an excellent catalyst for inducing growth. The addition of micromolar quantities of pentoses or potential pentose precursors to the filter-sterilized medium was equally effective in stimulating growth. These organic catalysts were not essential for growth under aerobic conditions. Upon agitation, similar cell yields were obtained from the autoclaved and filter-sterilized media. The micromolar quantities of lactic acid produced per micromole of carbohydrate fermented appeared to be similar under aerobic and static conditions of incubation. The final concentration of acetic acid increased as the result of agitation. This increase in volatile acidity was accompanied by a significant decrease in ethyl alcohol production. The cell yield was increased nearly 50% under aerobic conditions.

Journal Article↗
PubMed1975

Properties of D-xylose isomerase from Streptomyces albus.

A partially purified D-xylose isomerase has been isolated from cells of Streptomyces albus NRRL 5778 and some of its properties have been determined. D-Glucose, D-xylose, D-ribose, L-arabinose, and L-rhamnose served as substrates for the enzyme with respective Km values of 86, 93, 350, 153, and 312 mM and Vmax values measuring 1.23, 2.9, 2.63, 0.153, and 0.048 mumol min per mg of protein. The hexose D-allose was also isomerized. The enzyme was strongly activated by 1.0 mM Mg2+ but only partially activated by 1.0 mM Co2+. The respective Km values for Mg2+ and Co2+ were 0.3 and 0.003 mM. Mg2+ and Co2+ appear to have separate binding sites on the isomerase. These cations also protect the enzyme from thermal denaturation and from D-sorbitol inhibition. The optimum temperature for ketose formation was 70 to 80 C at pH values ranging from 7 to 9. D-Sorbitol acts as a competitive inhibitor with a Ki of 5.5 mM against D-glucose, D-xylose, and D-ribose. Induction experiments, Mg2+ activation, and D-sorbitol inhibition indicated that a single enzyme (D-xylose isomerase) was responsible for the isomerization of the pentoses, methyl pentose, and glucose.

Arabinose↗
PubMed1975

Physiology of sporeforming bacteria associated with insects: metabolism of Bacillus popilliae grown in third-instar Popillia japonica Newman larvae.

The timing and relative participation of concurrent pathways of carbohydrate metabolism as well as the extent of terminal respiratory activity were determined by radiorespirometry with 14-C substrates and by enzyme assays for vegetative and sporulating cells of the bacterium Bacillus popilliae cultured in whole, intact Popillia japonica (Japanese beetle) larvae. During vegetative proliferation, the pentose phosphate pathway predominates in the bacterial cells with minor involvement of the Embden-Meyerhof-Parnas pathway. As the cells proceed through sporulation, pentose phosphate and Embden-Meyerhof-Parnas activity remains constant. No tricarboxylic cycle activity is evident during growth and sporulation of B. popilliae. The results demonstrate (i) predominantly aerobic metabolism for carbohydrate assimilation within in vivo sporulating cells, (ii) a major contrast to the metabolism of other aerobic sporeforming bacteria that exhibit derepression of tricarboxylic acid cycle enzymatic activity at the onset of sporulation, and (iii) no causal necessity of the cycle to B. popilliae sporogeny.

Acetates↗
PubMed1975

Carbohydrate catabolism of selected strains in the genus Agrobacterium.

Radiorespirometric and enzyme analyses were used to reveal the glucose-catabolizing mechanisms functioning in single strains of seven presumed Agrobacterium species. The Entner-Doudoroff and pentose cycle pathways functioned in A. radiobacter, A. tumefaciens, A. rubi, and A. rhizogenes. Whereas both catabolic pathways were utilized to an almost equal degree in the A. radiobacter and A. tumefaciens strains, use of the Entner-Doudoroff pathway predominated in the A. rubi and A. rhizogenes strains. A stellulatum catabolized glucose almost solely through the Entner-Doudoroff pathway. In A. pseudotsugae and A. gypsophilae, glucose was metabolized mainly through the Emden-Meyerhof-Parnas pathway; the pentose phosphate pathway was also utilized.

Aldehyde-Lyases↗
PubMed1976

Identification and quantitation of capsular antigen in capsulated and noncapsulated strains of Haemophilus influenzae type b by crossed-immunoelectrophoresis.

Sonicated preparations of capsulated Haemophilus influenzae type b, two of its spontaneous mutants, one containing patches of capsules (class I variant) and the other noncapsulated (class II variant), and a noncapsulated strain of H. influenzae type d were analyzed by crossed-immunoelectrophoresis using unadsorbed antiserum to capsulated H. influenzae type b. Twenty common antigens were present in all four cultures. Two type b-specific antigens were also identified in the three H. influenzae type b cultures when antiserum adsorbed with H. influenzae type d sonicates (AdR) was used. One of these, the type b capsular antigen, cross-reacted with an antigen of Bacillus pumilus. Further adsorption of AdR with the B. pumilus sonicate reduced, but did not eliminate, the antibodies to the type b capsular antigen, although all antibodies to B. pumilus were removed. Sonication sheared the type b capsular antigen, resulting in an increase in its electrophoretic mobility in agarose gel. The capsular antigen from all three H. influenzae type b cultures had the same electrophoretic characteristics. Reproducible quantitation of sheared and unsheared capsular antigen was demonstrated by rocket immunoelectrophoresis. As little as 2.5 ng of polyribophosphate pentose was identified and measured. Capsulated H. influenzae type b contained 78 ng of polyribophosphate pentose per mug of cell protein; class I contained 20 ng and class II contained 4 ng. The small amount of type b capsular antigen present in the class II variant may account for its lack of detection in this organism before now.

Antigens, Bacterial↗
PubMed1978

Effect of pH on the growth and glucose metabolism of Neisseria gonorrhoeae.

This study examined the effect of pH on the metabolism of glucose by Neisseria gonorrhoeae. Radiorespirometric studies revealed that cells growing at pH 7.2 or 8.0 metabolized glucose primarily (ca. 80%) via the Entner-Doudoroff pathway. The remainder of the glucose was metabolized via the pentose phosphate pathway (ca. 20%). The tricarboxylic acid cycle was not active during glucose catabolism at either pH 7.2 or 8.0, and acetate accumulated in the medium. Cells growing at pH 6.0 had markedly increased pentose phosphate pathway activity (ca. 50%) and a functioning tricarboxylic acid cycle. The alteration in pathways was not due to differences in growth rate, but to the pH of the medium. Chemical fractionation of labeled cells and total hexose analyses revealed that growth pH markedly affected the composition of the gonococcus.

Acetates↗
PubMed1970

Regulation of glucose metabolism in Thiobacillus intermedius.

Glucose-yeast extract or glucose-casein hydrolysate-grown Thiobacillus intermedius cells, which use glucose for energy generation, possess high specific activities of the Entner-Doudoroff pathway and related enzymes, 6-phosphogluconate dehydrase, 2-keto-3-deoxy-6-phosphogluconate aldolase, glucokinase, and glucose-6-phosphate dehydrogenase, but low activities of enzymes unique to the pentose shunt and Embden-Meyerhof pathways. Although the synthesis of the latter enzymes remains largely unaffected by the growth environment, that of the former is stimulated by glucose. Radiorespirometric measurements demonstrate an early and parallel respiration of glucose carbon atoms one and four in glucose-casein hydrolysate broth. It is concluded that the Entner-Doudoroff pathway performs an energetic role in glucose metabolism by T. intermedius with the pentose shunt and Embden-Meyerhof pathways functioning mainly in biosynthesis. The presence of thiosulfate in the growth medium inhibits the synthesis of the Entner-Doudoroff pathway and related enzymes. In addition, both thiosulfate and glucose inhibit the synthesis of the Krebs cycle enzymes, nicotinamide adenine dinucleotide phosphate-linked isocitrate and alpha-ketoglutarate dehydrogenases. Thus, repression of enzymes is of significance in the adaptation of T. intermedius to its nutritional environment. The activity of glucose-6-phosphate dehydrogenase of T. intermedius is inhibited by adenosine triphosphate. Such a control could afford the organism a mechanism to regulate the flow of glucose into major energetic and biosynthetic routes.

Carbon Dioxide↗
PubMed1973

Pathways of carbohydrate metabolism in Microcyclus species.

Radiorespirometric and enzymatic studies were conducted to determine primary and secondary pathways of carbohydrate catabolism in Microcyclus aquaticus and M. flavus. M. aquaticus catabolizes both glucose and gluconate mainly via the Entner-Doudoroff and pentose phosphate pathways with some concurrent participation of the Embden-Meyerhof pathway. M. flavus, however, oxidizes glucose mainly via the Embden-Meyerhof pathway and gluconate via the Entner-Doudoroff pathway with some simultaneous operation of the pentose phosphate pathway. Both of the organisms showed evidence of the tricarboxylic acid cycle as a secondary pathway for the oxidation of carbohydrates.

Acetates↗
PubMed1976

Kinetics of light-dark CO2 fixation and glucose assimilation by Aphanocapsa 6714.

Cells of Aphanocapsa 6714 were subjected to alternating ligh-dark periods (flashing-light experiments). The corresponding activation (in the light) and inactivation (in the dark) of the reductive pentose cycle was measured, in vivo, from initial rates of 14CO2 incorporation and also by changes in the total concentration of 14C and 32P in soluble metabolites. Two principle sites of metabolic regulation were detected: (i) CO2 fixation was inactivated 15 to 20 s after removal of the light source, but reactivated rapidly on reentering the light; (ii) hydrolysis of fructose-1,6-diphosphate (FDP) and sedoheptulose-1,7-diphosphate (SDP) by their respective phosphatase(s) (FDP + SDPase) was rapidly inhibited in the dark but only slowly reactivated in the light. The time required for reactivation of FDP + SDPase, in the light, was on the order of 20 to 30 s. As a consequence of the timing of these inactivation-reactivation reactions, newly fixed CO2 accumulated in the FDP and SDP pools during the flashing-light experiments. Changes in the concentrations of the adenylate pools (mainly in the levels of adenosine 5'-triphosphate and adenosine diphosphate) were fast in comparison to the inactivation-reactivation reactions in the reductive pentose cycle. Thus, these regulatory effects may not be under the control of the adenylates in this organism. The activation of CO2 fixation in the light is at least in part due to activation of phosphoribulokinase, which is required for formation of ribulose-1,5-diphoshate, the carboxylation substrate. Phosphoribulokinase activity in crude extracts was found to be dependent on the presence of strong reducing agents such as dithiothreitol, but not significantly dependent on adenylate levels, although adenosine 5'-triphosphate is a substrate.

Adenosine Diphosphate↗
PubMed1977

Evidence for the presence of phosphoriboisomerase and ribulose-1,5-diphosphate carboxylase in extracts of Desulfovibrio vulgaris.

Cell extracts of Desulfovibrio vulgaris were found to incorporate 14CO2 into acid-stable products when ribose-5-phosphate or ribulose-1,5-diphosphate was used as a substrate. This CO2 fixation required adenosine triphosphate and produced 3-phosphoglyceric acid as one of the products. The assimilation of CO2 by pentose phosphates was unrelated to the pyruvate-CO2 exchange reaction. The pyruvate-CO2 exchange did not require adenosine triphosphate, did not produce phosphorylated compounds, and, unlike the pentose phosphate system, required an acidic protein fraction for activity.

Adenosine Triphosphate↗
PubMed1985

Biosynthesis of riboflavin in Bacillus subtilis: origin of the four-carbon moiety.

We studied the incorporation of [1-13C]ribose and [1,3-13C2]glycerol into the riboflavin precursor 6,7-dimethyl-8-ribityllumazine, using a riboflavin-deficient mutant of Bacillus subtilis. The formation of the pyrazine ring requires the addition of a four-carbon moiety to a pyrimidine precursor. The results show that C-6 alpha, C-6, C-7, and C-7 alpha of 6,7-dimethyl-8-ribityllumazine were biosynthetically equivalent to C-1, C-2, C-3, and C-5 of a pentose phosphate. C-4 of the pentose precursor was lost through an intramolecular skeletal rearrangement. Thus, the last steps in the biosynthesis of 6,7-dimethyl-8-ribityllumazine apparently involve the same mechanism in bacteria as in fungi.

Bacillus subtilis↗
PubMed2002

Novel pathway for alcoholic fermentation of delta-gluconolactone in the yeast Saccharomyces bulderi.

Under anaerobic conditions, the yeast Saccharomyces bulderi rapidly ferments delta-gluconolactone to ethanol and carbon dioxide. We propose that a novel pathway for delta-gluconolactone fermentation operates in this yeast. In this pathway, delta-gluconolactone is first reduced to glucose via an NADPH-dependent glucose dehydrogenase (EC 1.1.1.47). After phosphorylation, half of the glucose is metabolized via the pentose phosphate pathway, yielding the NADPH required for the glucose-dehydrogenase reaction. The remaining half of the glucose is dissimilated via glycolysis. Involvement of this novel pathway in delta-gluconolactone fermentation in S. bulderi is supported by several experimental observations. (i) Fermentation of delta-gluconolactone and gluconate occurred only at low pH values, at which a substantial fraction of the substrate is present as delta-gluconolactone. Unlike gluconate, the latter compound is a substrate for glucose dehydrogenase. (ii) High activities of an NADP(+)-dependent glucose dehydrogenase were detected in cell extracts of anaerobic, delta-gluconolactone-grown cultures, but activity of this enzyme was not detected in glucose-grown cells. Gluconate kinase activity in cell extracts was negligible. (iii) During anaerobic growth on delta-gluconolactone, CO(2) production exceeded ethanol production by 35%, indicating that pyruvate decarboxylation was not the sole source of CO(2). (iv) Levels of the pentose phosphate pathway enzymes were 10-fold higher in delta-gluconolactone-grown anaerobic cultures than in glucose-grown cultures, consistent with the proposed involvement of this pathway as a primary dissimilatory route in delta-gluconolactone metabolism.

Anaerobiosis↗
PubMed2004

A genetic locus necessary for rhamnose uptake and catabolism in Rhizobium leguminosarum bv. trifolii.

Rhizobium leguminosarum bv. trifolii mutants unable to catabolize the methyl-pentose rhamnose are unable to compete effectively for nodule occupancy. In this work we show that the locus responsible for the transport and catabolism of rhamnose spans 10,959 bp. Mutations in this region were generated by transposon mutagenesis, and representative mutants were characterized. The locus contains genes coding for an ABC-type transporter, a putative dehydrogenase, a probable isomerase, and a sugar kinase necessary for the transport and subsequent catabolism of rhamnose. The regulation of these genes, which are inducible by rhamnose, is carried out in part by a DeoR-type negative regulator (RhaR) that is encoded within the same transcript as the ABC-type transporter but is separated from the structural genes encoding the transporter by a terminator-like sequence. RNA dot blot analysis demonstrated that this terminator-like sequence is correlated with transcript attenuation only under noninducing conditions. Transport assays utilizing tritiated rhamnose demonstrated that uptake of rhamnose was inducible and dependent upon the presence of the ABC transporter at this locus. Phenotypic analyses of representative mutants from this locus provide genetic evidence that the catabolism of rhamnose differs from previously described methyl-pentose catabolic pathways.

Bacterial Proteins↗
PubMed2004

Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax by use of genomic and biochemical data.

The hyperthermophilic, facultatively heterotrophic crenarchaeum Thermoproteus tenax was analyzed using a low-coverage shotgun-sequencing approach. A total of 1.81 Mbp (representing 98.5% of the total genome), with an average gap size of 100 bp and 5.3-fold coverage, are reported, giving insights into the genome of T. tenax. Genome analysis and biochemical studies enabled us to reconstruct its central carbohydrate metabolism. T. tenax uses a variant of the reversible Embden-Meyerhof-Parnas (EMP) pathway and two different variants of the Entner-Doudoroff (ED) pathway (a nonphosphorylative variant and a semiphosphorylative variant) for carbohydrate catabolism. For the EMP pathway some new, unexpected enzymes were identified. The semiphosphorylative ED pathway, hitherto supposed to be active only in halophiles, is found in T. tenax. No evidence for a functional pentose phosphate pathway, which is essential for the generation of pentoses and NADPH for anabolic purposes in bacteria and eucarya, is found in T. tenax. Most genes involved in the reversible citric acid cycle were identified, suggesting the presence of a functional oxidative cycle under heterotrophic growth conditions and a reductive cycle for CO2 fixation under autotrophic growth conditions. Almost all genes necessary for glycogen and trehalose metabolism were identified in the T. tenax genome.

Archaeal Proteins↗
PubMed1961

Glucose uptake and dissimilation by x-irradiated, starved, and division-inhibited yeast.

Spoerl, Edward (U. S. Army Medical Research Laboratory, Fort Knox, Ky.) and C. W. Quiner. Glucose uptake and dissimilation by X-irradiated, starved, and division-inhibited yeast. J. Bacteriol. 82:764-769. 1961.-Estimates of the relative participation of the pentose cycle and the Embden-Meyerhof-Parnas pathways in sugar dissimilation, by means of C(14)O(2) recoveries from yeast cells fed specifically labeled glucose, showed significant differences indicating less pentose cycle activity in starved irradiated cells than in unirradiated cells. This result is in qualitative agreement with previously observed respiratory quotient values, which indicated greater glycolytic activity in starved irradiated cells; this implicates a change in pathways of dissimilation in the responses observed following irradiation and starvation. A concurrent lower rate of uptake of glucose from the medium was observed for unirradiated, starved cells as compared to irradiated cells. The possibility that the membrane is the site of the cellular change involved in these responses is discussed.

Biological Transport↗
PubMed1966

Carbohydrate catabolism of Mima polymorpha. II. Abortive catabolism of glucose.

Marus, Adrienne (University of Cincinnati, Cincinnati, Ohio), and Emily J. Bell. Carbohydrate catabolism of Mima polymorpha. II. Abortive catabolism of glucose. J. Bacteriol. 91:2229-2236. 1966.-Mima polymorpha, unable to grow in the presence of glucose as a sole carbon and energy source, is able to obtain supplemental, utilizable energy from the partial catabolism of this substrate. Various enzymes of hexose catabolism have been assayed in this organism and in M. polymorpha M, a mutant obtained by ultraviolet irradiation. The parent strain contains a functional glucose dehydrogenase, glucose-6-phosphate dehydrogenase, diphosphofructoaldolase, and a 2-keto-3-deoxy-6-phosphogluconate aldolase, but is lacking in glucokinase, gluconokinase, 2-ketogluconokinase, and 6-phosphogluconate dehydrogenase. The enzymes present indicate partially functioning hexose diphosphate and Entner-Doudoroff pathways. The absence of kinases explains the inability of the strain to grow on glucose and an absence of 6-phosphogluconate dehydrogenase would indicate the absence of the complete pentose pathway. The mutant strain, M. polymorpha M, possesses, in addition to those enzymes produced by the wild type, both gluconokinase and 6-phosphogluconate dehydrogenase. The presence of the former explains the mutant's ability to grow on glucose, and the presence of the latter indicates a more complete pentose shunt. The supplemental energy obtained from partial glucose catabolism (to gluconic acid) may be obtained from a cytochrome-linked reaction of the glucose dehydrogenase.

Acinetobacter↗
PubMed1967

Evidence for the Calvin cycle and hexose monophosphate pathway in Thiobacillus ferrooxidans.

The enzymes of the Calvin reductive pentose phosphate cycle and the hexose monophosphate pathway have been demonstrated in cell-free extracts of Thiobacillus ferrooxidans. This, together with analyses of the products of CO(2) fixation in cell-free systems, suggests that these pathways are operative in whole cells of this microorganism. Nevertheless, the amount of CO(2) fixed in these cell-free systems was limited by the type and amount of compound added as substrate. The inability of cell extracts to regenerate pentose phosphates and to perpetuate the cyclic fixation of CO(2) is partially attributable to low activity of triose phosphate dehydrogenase under the experimental conditions found to be optimal for the enzymes involved in the utilization of ribose-5-phosphate or ribulose-1,5-diphosphate as substrate for CO(2) incorporation. With the exception of ribulose-1,5-diphosphate, all substrates required the addition of adenosine triphosphate (ATP) or adenosine diphosphate (ADP) for CO(2) fixation. Under optimal conditions, with ribose-5-phosphate serving as substrate, each micromole of ATP added resulted in the fixation of 1.5 mumoles of CO(2), whereas each micromole of ADP resulted in 0.5 mumole of CO(2) fixed. These values reflect the activity of adenylate kinase in the extract preparations. The K(m) for ATP in the phosphoribulokinase reaction was 0.91 x 10(-3)m. Kinetic studies conducted with carboxydismutase showed K(m) values of 1.15 x 10(-4)m and 5 x 10(-2)m for ribulose-1,5-diphosphate and bicarbonate, respectively.

Adenine Nucleotides↗
PubMed2006

Use of the flux model of amino acid metabolism of Escherichia coli.

A program implementing a flux model of Escherichia coli metabolism was used to analyze the effects of the addition of amino acids (tryptophan, tyrosine, phenylalanine, leucine, isoleucine, valine, histidine, lysine, threonine, cysteine, methionine, arginine, proline) to minimal medium or media lacking nitrogen, carbon, or both. The overall response of the metabolic system to the addition of various amino acids to the minimal medium is similar. Glycolysis and the synthesis of pyruvate with its subsequent degradation to acetate via acetyl-CoA become more efficient, whereas the fluxes through the pentose phosphate pathway and the TCA cycle decrease. If amino acids are used as the sole source of carbon, nitrogen, or both, the changes in the flux distribution are determined mainly by the carbon limitation. The phosphoenolpyruvate to glucose-6-phosphate flux increases; the flux through the pentose phosphate path is directed towards ribulose-5-phosphate. Other changes are determined by the compounds that are the primary products of catabolism of the added amino acid.

Amino Acids↗