Oxygen sensitivity of sugar metabolism and interconversion of pyruvate formate-lyase in intact cells of Streptococcus mutans and Streptococcus sanguis

Takahashi, Nobutaka; Abbe, K; Takahashi-Abbe, S.; Yamada, Tadashi

doi:10.1128/iai.55.3.652-656.1987

Cited by 61 publications

(47 citation statements)

References 34 publications

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“…are: Fru, fructose; Gal, galactose; LDH, lactate dehydrogenase; PFL, pyruvate-formiate lyase; Pi, inorganic orthophosphate; PK, pyruvate kinase. et al, 1987;Hillman et al, 1994;de Soet et al, 2000;Takahashi-Abbe et al, 2003). These extracellular compounds being the responsible of acidic activity ascribed to S. mutans (Takahashi et al, 1991;de Soet et al, 2000;Takahashi and Nyvad, 2011).…”

Section: Discussionmentioning

confidence: 99%

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

Diez

Demonte

Guerrero

et al. 2013

Molecular Microbiology

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Streptococcus mutans is the leading cause of dental caries worldwide. The bacterium accumulates a glycogen-like internal polysaccharide, which mainly contributes to its carionegic capacity. S.mutans has two genes (glgC and glgD) respectively encoding putative ADP-glucose pyrophosphorylases (ADP-Glc PPase), a key enzyme for glycogen synthesis in most bacteria. Herein, we report the molecular cloning and recombinant expression of both genes (separately or together) followed by the characterization of the respective enzymes. When expressed individually GlgC had ADP-Glc PPase activity, whereas GlgD was inactive. Interestingly, the coexpressed GlgC/GlgD protein was one order of magnitude more active than GlgC alone. Kinetic characterization of GlgC and GlgC/GlgD pointed out remarkable differences between them. Fructose-1,6-bis-phosphate activated GlgC by twofold, but had no effect on GlgC/GlgD. Conversely, phospho-enol-pyruvate and inorganic salts inhibited GlgC/GlgD without affecting GlgC. However, in the presence of fructose-1,6-bis-phosphate GlgC acquired a GlgC/GlgD-like behaviour, becoming sensitive to the stated inhibitors. Results indicate that S. mutans ADP-Glc PPase is an allosteric regulatory enzyme exhibiting sensitivity to modulation by key intermediates of carbohydrates metabolism in the cell. The particular regulatory properties of the S.mutans enzyme agree with phylogenetic analysis, where GlgC and GlgD proteins found in other Firmicutes arrange in distinctive clusters.

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Section: Discussionmentioning

confidence: 99%

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

Diez

Demonte

Guerrero

et al. 2013

Molecular Microbiology

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“…The reaction was started with the addition of pyruvate and the activity was estimated from the reduction of methylviologen or NAD(P). Pyruvate formate-lyase (EC 2.3.1.54) was estimated from the formation of acetyl CoA from pyruvate as described previously (40). Phosphotransacetylase (EC 2.3.1.8) was estimated by the formation of acetyl CoA from acetyl phosphate and inorganic phosphate as described previously (41).…”

Section: Assay For Enzymatic Activities Involved In Aspartate Degradamentioning

confidence: 99%

Pathways for amino acid metabolism by Prevotella intermedia and Prevotella nigrescens

Takahashi

Yamada

2000

Oral Microbiology and Immunology

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Pathways for amino acid metabolism by Prevotella intermedia and Prevotella nigrescens were investigated. Prevotella strains grew anaerobically in tryptone-based medium and their growth increased upon the addition of aspartate to the medium. Washed cells of tryptone-grown strains metabolized aspartate to succinate, acetate, fumarate, malate, formate and ammonia, while from tryptone they produced isobutyrate and isovalerate in addition to the end products from aspartate. Cell extracts obtained from the tryptone-grown cells had aspartate ammonia-lyase for the conversion of aspartate to fumarate. Methylviologen-dependent fumarate reductase was found to reduce fumarate to succinate. A series of enzymatic activities, including fumarase, NAD-dependent malate dehydrogenase, oxaloacetate decarboxylase, methylviologen-dependent pyruvate oxidoreductase, phosphotransacetylase and acetate kinase, was detected for the oxidative conversion of fumarate to acetate. Pyruvate formate-lyase and NAD-dependent formate dehydrogenase were also found for the production and consumption of formate, respectively. Methylviologen: NAD(P) oxidoreductase was found to be responsible for linkage between these reductive and oxidative pathways. Furthermore, the cell extracts had branched-chain amino acid aminotransferase and methylviologen-dependent branched-chain 2-oxoacid oxidoreductase, concomitantly with NAD-dependent glutamate dehydrogenase. Valine and leucine could be converted to isobutyryl CoA and isovaleryl CoA, respectively, through the sequential catalyses of these enzymes, and consequently to isobutyrate and isovalerate, respectively.

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“…The samples were stored at 4°C until assayed. The solutions were assayed for lactate, acetate, pyruvate, formate, propionate, citrate, malate and succinate by a carboxylic acid analyzer as described previously (30,32).…”

Section: Assay Of Oxygen Consumption Conversion Of Oxygen To Hydrogementioning

confidence: 99%

Catabolic pathway for aerobic degradation of lactate by Actinomyces naeslundii

Takahashi

Yamada

1996

Oral Microbiology and Immunology

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The aerobic metabolism of lactate by oral Actinomyces was studied. Six of 7 strains of Actinomyces naeslundii increased their growth in the presence of lactate under aerobic conditions. Washed cells grown on lactate aerobically degraded lactate and pyruvate to acetate with a concomitant consumption of oxygen. In the presence of catalase, the molar ratios of oxygen consumed to acetate produced were 1 for lactate degradation and 0.5 for pyruvate degradation. The enzymatic activities found in cell extracts revealed that lactate could be converted to pyruvate by NAD-independent lactate dehydrogenase (iLDH) and further to acetyl CoA by pyruvate dehydrogenase (PDH). The acetyl CoA formed could be metabolized into acetate by phosphotransacetylase (PTA) and acetate kinase (AK) with the formation of ATP. These results indicate that A. naeslundii metabolizes lactate into acetate by the sequential enzymatic reactions iLDH, PDH, PTA and AK and that hydrogens produced by iLDH and PDH are transferred to oxygen. The activity of lactate degradation and oxygen consumption may modify the environmental conditions of dental plaque.

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Oxygen sensitivity of sugar metabolism and interconversion of pyruvate formate-lyase in intact cells of Streptococcus mutans and Streptococcus sanguis

Cited by 61 publications

References 34 publications

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

Pathways for amino acid metabolism by Prevotella intermedia and Prevotella nigrescens

Catabolic pathway for aerobic degradation of lactate by Actinomyces naeslundii

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