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Major role of NAD-dependent lactate dehydrogenases in aerobic lactate utilization in Lactobacillus plantarum during early stationary phase
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, 2004
"... NAD-independent lactate dehydrogenases are commonly thought to be responsible for lactate utilization during the stationary phase of aerobic growth in Lactobacillus plantarum. To substantiate this view, we constructed single and double knockout mutants for the corresponding genes, loxD and loxL. Lac ..."
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NAD-independent lactate dehydrogenases are commonly thought to be responsible for lactate utilization during the stationary phase of aerobic growth in Lactobacillus plantarum. To substantiate this view, we constructed single and double knockout mutants for the corresponding genes, loxD and loxL. Lactate-to-acetate conversion was not impaired in these strains, while it was completely blocked in mutants deficient in NADdependent lactate dehydrogenase activities, encoded by the ldhD and ldhL genes. We conclude that NADdependent but not NAD-independent lactate dehydrogenases are involved in this process. Under anaerobic conditions, Lactobacillus plantarum produces lactate as the major fermentation end product through the reduction of glycolytic pyruvate by NAD-dependent lactate dehydrogenases (nLDHs) (7, 8). When grown in the presence of oxygen, L. plantarum ferments glucose into lactate until glucose becomes limiting. Lactic acid produced during fermentation is then converted to acetate with concomitant hydrogen peroxide, carbon dioxide, and ATP production (Fig. 1A) (20). Acetate becomes the major fermentation end product, leading
SO-LAAO, a Novel L-Amino Acid Oxidase That Enables Streptococcus oligofermentans To Outcompete Streptococcus mutans by Generating H 2O 2
, 2008
"... We previously demonstrated that Streptococcus oligofermentans suppressed the growth of Streptococcus mutans, the primary cariogenic pathogen, by producing hydrogen peroxide (H 2O 2) through lactate oxidase activity. In this study, we found that the lox mutant of S. oligofermentans regained the inhib ..."
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We previously demonstrated that Streptococcus oligofermentans suppressed the growth of Streptococcus mutans, the primary cariogenic pathogen, by producing hydrogen peroxide (H 2O 2) through lactate oxidase activity. In this study, we found that the lox mutant of S. oligofermentans regained the inhibition while growing on peptone-rich plates. Further studies demonstrated that the H 2O 2 produced on peptone by S. oligofermentans was mainly derived from
Concerted Action of Lactate Oxidase and Pyruvate Oxidase in Aerobic Growth of Streptococcus pneumoniae: Role of Lactate as an Energy Source �
, 2007
"... These include: This article cites 32 articles, 18 of which can be accessed free at: ..."
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These include: This article cites 32 articles, 18 of which can be accessed free at:
Involvement of Pyruvate Oxidase Activity and Acetate Production in the Survival of Lactobacillus plantarum during the Stationary Phase of Aerobic Growth � †
, 2006
"... In addition to the previously characterized pyruvate oxidase PoxB, the Lactobacillus plantarum genome encodes four predicted pyruvate oxidases (PoxC, PoxD, PoxE, and PoxF). Each pyruvate oxidase gene was individually inactivated, and only the knockout of poxF resulted in a decrease in pyruvate oxida ..."
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In addition to the previously characterized pyruvate oxidase PoxB, the Lactobacillus plantarum genome encodes four predicted pyruvate oxidases (PoxC, PoxD, PoxE, and PoxF). Each pyruvate oxidase gene was individually inactivated, and only the knockout of poxF resulted in a decrease in pyruvate oxidase activity under the tested conditions. We show here that L. plantarum has two major pyruvate oxidases: PoxB and PoxF. Both are involved in lactate-to-acetate conversion in the early stationary phase of aerobic growth and are regulated by carbon catabolite repression. A strain devoid of pyruvate oxidase activity was constructed by knocking out the poxB and poxF genes. In this mutant, acetate production was strongly affected, with lactate remaining the major end product of either glucose or maltose fermentation. Notably, survival during the stationary phase appeared to be dramatically improved in the poxB poxF double mutant. Acetate is the major fermentation end product of the lactic acid bacterium Lactobacillus plantarum when cultivated under aerobic conditions and sugar limitation. It is produced at the expense of lactate as glucose becomes depleted and cells enter the stationary phase of growth. The pathway for lactate-toacetate conversion under these conditions has been shown to
Lactate Racemization as a Rescue Pathway for Supplying D-Lactate to the Cell Wall Biosynthesis Machinery in Lactobacillus plantarum
, 2005
"... Lactobacillus plantarum is a lactic acid bacterium that produces D- and L-lactate using stereospecific NADdependent lactate dehydrogenases (LdhD and LdhL, respectively). However, reduction of glycolytic pyruvate by LdhD is not the only pathway for D-lactate production since a mutant defective in thi ..."
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Lactobacillus plantarum is a lactic acid bacterium that produces D- and L-lactate using stereospecific NADdependent lactate dehydrogenases (LdhD and LdhL, respectively). However, reduction of glycolytic pyruvate by LdhD is not the only pathway for D-lactate production since a mutant defective in this activity still produces both lactate isomers (T. Ferain, J. N. Hobbs, Jr., J. Richardson, N. Bernard, D. Garmyn, P. Hols, N. E. Allen, and J. Delcour, J. Bacteriol. 178:5431–5437, 1996). Production of D-lactate in this species has been shown to be connected to cell wall biosynthesis through its incorporation as the last residue of the muramoyl-pentadepsipeptide peptidoglycan precursor. This particular feature leads to natural resistance to high concentrations of vancomycin. In the present study, we show that L. plantarum possesses two pathways for D-lactate production: the LdhD enzyme and a lactate racemase, whose expression requires L-lactate. We report the cloning of a six-gene operon, which is involved in lactate racemization activity and is positively regulated by L-lactate. Deletion of this operon in an L. plantarum strain that is devoid of LdhD activity leads to the exclusive production of L-lactate. As a consequence, peptidoglycan biosynthesis is affected, and growth of this mutant is
Pyruvate:quinone oxidoreductase from Corynebacterium glutamicum: purification and biochemical characterization
- J
, 2005
"... This article cites 67 articles, 35 of which can be accessed free ..."
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This article cites 67 articles, 35 of which can be accessed free
CONTENT ALERTS
, 2007
"... This article cites 36 articles, 20 of which can be accessed free ..."
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This article cites 36 articles, 20 of which can be accessed free
pone.0057235 1..8
"... General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Comp ..."
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General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulations If you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: https://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Abstract Oxygen relieves the CO 2 and acetate dependency of Lactobacillus johnsonii NCC 533. The probiotic Lactobacillus johnsonii NCC 533 is relatively sensitive to oxidative stress; the presence of oxygen causes a lower biomass yield due to early growth stagnation. We show however that oxygen can also be beneficial to this organism as it relieves the requirement for acetate and CO 2 during growth. Both on agar-and liquid-media, anaerobic growth of L. johnsonii NCC 533 requires CO 2 supplementation of the gas phase. Switching off the CO 2 supply induces growth arrest and cell death. The presence of molecular oxygen overcomes the CO 2 dependency. Analogously, L. johnsonii NCC 533 strictly requires media with acetate to sustain anaerobic growth, although supplementation at a level that is 100-fold lower (120 microM) than the concentration in regular growth medium for lactobacilli already suffices for normal growth. Analogous to the CO 2 requirement, oxygen supply relieves this acetate-dependency for growth. The L. johnsonii NCC 533 genome indicates that this organism lacks genes coding for pyruvate formate lyase (PFL) and pyruvate dehydrogenase (PDH), both CO 2 and acetyl-CoA producing systems. Therefore, C1-and C2-compound production is predicted to largely depend on pyruvate oxidase activity (POX). This proposed role of POX in C2/C1-generation is corroborated by the observation that in a POX deficient mutant of L. johnsonii NCC 533, oxygen is not able to overcome acetate dependency nor does it relieve the CO 2 dependency. Citation: Hertzberger RY, Pridmore RD, Gysler C, Kleerebezem M, Teixeira de Mattos MJ (2013) Oxygen Relieves the CO 2 and Acetate Dependency of Lactobacillus johnsonii NCC 533. PLoS ONE 8(2): e57235.
REFERENCES CONTENT ALERTS
, 1998
"... These include: This article cites 23 articles, 14 of which can be accessed free at: ..."
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These include: This article cites 23 articles, 14 of which can be accessed free at: