Metabolism of Pyruvate and Citrate in Lactobacilli

Hickey, M. W.; Hillier, A J; Jago, G. R.

doi:10.1071/bi9830487

Cited by 74 publications

(50 citation statements)

References 21 publications

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“…Such a coupling was invoked to explain a high level of acetate production in Lactococcus lactis when the NADH oxidase was overexpressed (35). Although an NADH oxidase activity was clearly induced at similar levels in both Lp80 and the PoxBdeficient strain under aerobic conditions, we were unable to detect any PDH activity under the different growth conditions, confirming previous observations that a POX enzyme(s) plays the major role in acetate production under aerobic conditions (6,18,30; data not shown).…”

Section: Discussionsupporting

confidence: 48%

“…This pathway is thought to be mainly active under aerobic conditions since PDH is strongly inhibited under anaerobic conditions by the relatively high NADH level (3). Although putative pdh genes were recently identified in the genome sequence, it was reported that L. plantarum had no detectable PDH activity under various growth conditions (6,18,25,30). Previous physiological studies of L. plantarum indicated that acetate production is maximal under aerobic conditions with glucose limitation.…”

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confidence: 99%

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Characterization and Functional Analysis of thepoxBGene, Which Encodes Pyruvate Oxidase inLactobacillus plantarum

et al. 2004

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The pyruvate oxidase gene (poxB) from Lactobacillus plantarum Lp80 was cloned and characterized. Northern blot and primer extension analyses revealed that transcription of poxB is monocistronic and under the control of a vegetative promoter. poxB mRNA expression was strongly induced by aeration and was repressed by glucose. Moreover, Northern blotting performed at different stages of growth showed that poxB expression is maximal in the early stationary phase when glucose is exhausted. Primer extension and in vivo footprint analyses revealed that glucose repression of poxB is mediated by CcpA binding to the cre site identified in the promoter region. The functional role of the PoxB enzyme was studied by using gene overexpression and knockout in order to evaluate its implications for acetate production. Constitutive overproduction of PoxB in L. plantarum revealed the predominant role of pyruvate oxidase in the control of acetate production under aerobic conditions. The ⌬poxB mutant strain exhibited a moderate (20 to 25%) decrease in acetate production when it was grown on glucose as the carbon source, and residual pyruvate oxidase activity that was between 20 and 85% of the wild-type activity was observed with glucose limitation (0.2% glucose). In contrast, when the organism was grown on maltose, the poxB mutation resulted in a large (60 to 80%) decrease in acetate production. In agreement with the latter observation, the level of residual pyruvate oxidase activity with maltose limitation (0.2% maltose) was less than 10% of the wild-type level of activity.

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Section: Discussionsupporting

confidence: 48%

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confidence: 99%

Characterization and Functional Analysis of thepoxBGene, Which Encodes Pyruvate Oxidase inLactobacillus plantarum

et al. 2004

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“…In the presence of inorganic phosphate, the thiamine diphosphate (ThDP)-dependent APF-POX catalyzes the oxidative decarboxylation of pyruvate to acetylϳP, carbon dioxide, and hydrogen peroxide (Fig. 9A) (188,315,402,403,444). In S. pneumoniae, ACP-POX appears responsible for formation of the majority of the acetylϳP, despite the presence of both ACK and PTA.…”

Section: Other Acetylϳp-forming Enzymesmentioning

confidence: 99%

“…Pyruvate oxidases can be divided into two classes: the acetate formers such as POXB of E. coli and the acetylϳP-formers (APF-POX [EC 1.2.3.3]) found in diverse lactobacilli, Pediococcus pseudomonas, and S. pneumoniae (49,188,315,402,403,419). In the presence of inorganic phosphate, the thiamine diphosphate (ThDP)-dependent APF-POX catalyzes the oxidative decarboxylation of pyruvate to acetylϳP, carbon dioxide, and hydrogen peroxide (Fig.…”

Section: Other Acetylϳp-forming Enzymesmentioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,082

1,274

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To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described

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“…Rhee et Park (1980) ont montré que Laetobaeillus bulgarieus en culture continue anaérobie avec limitation de glucose passe à un système hétérofermen-taire à la suite d'une augmentation du pH du milieu; dans un environnement alcalin, la biosynthèse de la lactate deshydrogé-nase diminue, et les enzymes du système hétérofermentaire (pyruvate formate lyase, acétate kinase, aldéhyde deshydrogénase et phosphotransacétylase) sont activés. Lloyd et al (1978), Hickey et al (1983) montrent que l'oxydation du pyruvate en Thomas (1987) propose deux mécanismes pour la formation d'acétate dans les fromages; l'un oxygène dépendant avec comme substrat le lactate, l'autre oxygène indépendant avec comme substrat le citrate. Tseng et Montville (1990) constatent des changements d'activités enzymatiques dans des cultures aérobies comparativement aux cultures anaérobies, ainsi que des effets en relation avec des variations de pH.…”

Section: Déterminations Enzymatiquesunclassified

Lactobacilles, oxygène, métabolisme et antagonisme

Frey

Hubert

1993

Lait

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Résumé -Les lactobacilles homo-et hétérofermentaires facultatifs oxydent le glucose; le pyruvate formé est normalement réduit en lactate par la lactate deshydrogénase (LDH) et s'accumule dans la plupart des cas. La LDH de certaines de ces bactéries est activée par le fructose 1,6 di phosphate (FDP). En l'absence de ce dernier, la LDH a une activité faible et le catabolisme aboutit à des produits terminaux tels l'acétate l'acétoïne ou l'éthanol.

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Metabolism of Pyruvate and Citrate in Lactobacilli

Cited by 74 publications

References 21 publications

Characterization and Functional Analysis of thepoxBGene, Which Encodes Pyruvate Oxidase inLactobacillus plantarum

Characterization and Functional Analysis of thepoxBGene, Which Encodes Pyruvate Oxidase inLactobacillus plantarum

The Acetate Switch

Lactobacilles, oxygène, métabolisme et antagonisme

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