Search results for "Physiology and Metabolism"
showing 9 items of 9 documents
Transport of C(4)-dicarboxylates in Wolinella succinogenes.
2000
ABSTRACT C 4 -dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes , since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C 4 -dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10 3 . The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the prese…
Availability of O 2 as a Substrate in the Cytoplasm of Bacteria under Aerobic and Microaerobic Conditions
1998
ABSTRACT The growth rates of Pseudomonas putida KT2442 and mt-2 on benzoate, 4-hydroxybenzoate, or 4-methylbenzoate showed an exponential decrease with decreasing oxygen tensions (partial O 2 tension [pO 2 ] values). The oxygen tensions resulting in half-maximal growth rates were in the range of 7 to 8 mbar of O 2 (corresponding to 7 to 8 μM O 2 ) (1 bar = 10 5 Pa) for aromatic compounds, compared to 1 to 2 mbar for nonaromatic compounds like glucose or succinate. The decrease in the growth rates coincided with excretion of catechol or protocatechuate, suggesting that the activity of the corresponding oxygenases became limiting. The experiments directly establish that under aerobic and micr…
Extracellular oxidoreduction potential modifies carbon and electron flow in Escherichia coli.
2000
ABSTRACT Wild-type Escherichia coli K-12 ferments glucose to a mixture of ethanol and acetic, lactic, formic, and succinic acids. In anoxic chemostat culture at four dilution rates and two different oxidoreduction potentials (ORP), this strain generated a spectrum of products which depended on ORP. Whatever the dilution rate tested, in low reducing conditions (−100 mV), the production of formate, acetate, ethanol, and lactate was in molar proportions of approximately 2.5:1:1:0.3, and in high reducing conditions (−320 mV), the production was in molar proportions of 2:0.6:1:2. The modification of metabolic fluxes was due to an ORP effect on the synthesis or stability of some fermentation enzy…
Influence of carboxylic acids on the stereospecific nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lac…
1971
Leuconostoc mesenteroides increased its lactic acid production from glucose threefold when malic acid was added to the culture. This increase resulted also in a reduction of the ratio of d -lactic acid to l -lactic acid (31.5 to 1.23). Addition of malic acid increased 6.5-fold the specific activity of nicotinamide adenine dinucleotide (NAD)-linked l -lactate dehydrogenase and increased 3.2-fold that of NAD-linked d -lactate dehydrogenase. The Michaelis constant ( K m ) for NAD of the NAD-linked l -lactate dehydrogenase increased with the addition of malate, but no change was observed in the K m values for the respective d -enzyme. The effect of carboxylic acids on the NAD-linked l -lactate…
Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli
1999
ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…
Nicotinamide Adenine Dinucleotide-Dependent and Nicotinamide Adenine Dinucleotide-Independent Lactate Dehydrogenases in Homofermentative and Heterofe…
1971
Three homofermentative ( Lactobacillus plantarum B38, L. plantarum B33, Pediococcus pentosaceus B30) and three heterofermentative ( Leuconostoc mesenteroides 39, L. oenos B70, Lactobacillus brevis ) lactic acid bacteria were examined for the presence or absence of nicotinamide adenine dinucleotide (NAD)-dependent and NAD-independent d - and l -lactate dehydrogenases. Two of the six strains investigated, P. pentosaceus and L. oenos , did not exhibit an NAD-independent enzyme activity capable of reducing dichlorophenol indophenol. The p H optima of the lactic dehydrogenases were determined. The NAD-dependent enzymes from homofermentative strains exhibited optima at p H 7.8 to 8.8, whereas va…
Regulation of aerobic and anaerobic D-malate metabolism of Escherichia coli by the LysR-type regulator DmlR (YeaT).
2010
ABSTRACT Escherichia coli K-12 is able to grow under aerobic conditions on d -malate using DctA for d -malate uptake and the d -malate dehydrogenase DmlA (formerly YeaU) for converting d -malate to pyruvate. Induction of dmlA encoding DmlA required an intact dmlR (formerly yeaT ) gene, which encodes DmlR, a LysR-type transcriptional regulator. Induction of dmlA by DmlR required the presence of d -malate or l - or meso -tartrate, but only d -malate supported aerobic growth. The regulator of general C 4 -dicarboxylate metabolism (DcuS-DcuR two-component system) had some effect on dmlA expression. The anaerobic l -tartrate regulator TtdR or the oxygen sensors ArcB-ArcA and FNR did not have a m…
Role of secondary transporters and phosphotransferase systems in glucose transport by Oenococcus oeni.
2011
ABSTRACT Glucose uptake by the heterofermentative lactic acid bacterium Oenococcus oeni B1 was studied at the physiological and gene expression levels. Glucose- or fructose-grown bacteria catalyzed uptake of [ 14 C]glucose over a pH range from pH 4 to 9, with maxima at pHs 5.5 and 7. Uptake occurred in two-step kinetics in a high- and low-affinity reaction. The high-affinity uptake followed Michaelis-Menten kinetics and required energization. It accumulated the radioactivity of glucose by a factor of 55 within the bacteria. A large portion (about 80%) of the uptake of glucose was inhibited by protonophores and ionophores. Uptake of the glucose at neutral pH was not sensitive to degradation …
The L-tartrate/succinate antiporter TtdT (YgjE) of L-tartrate fermentation in Escherichia coli.
2007
ABSTRACT Escherichia coli ferments l -tartrate under anaerobic conditions in the presence of an additional electron donor to succinate. The carrier for l -tartrate uptake and succinate export and its relation to the general C 4 -dicarboxylate carriers DcuA, DcuB, and DcuC were studied. The secondary carrier TtdT, encoded by the ttdT (previously called ygjE ) gene, is required for the uptake of l -tartrate. The ttdT gene is located downstream of the ttdA and ttdB genes, encoding the l -tartrate dehydratase TtdAB. Analysis of mRNA by reverse transcription-PCR showed that ttdA , ttdB , and ttdT are cotranscribed. Deletion of ttdT abolished growth by l -tartrate and degradation of l -tartrate c…